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Categories

Category: OntologyTerm
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Type Details Score
Ontology Term
PANTHER:PTHR22792 | LUPUS LA PROTEIN-RELATED
 
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Ontology Term
PANTHER:PTHR22792:SF26 | LA-RELATED PROTEIN CG11505
 
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Ontology Term
Pfam:PF05383 | La domain
Description: This presumed domain is found at the N-terminus of La RNA-binding proteins as well as other proteins [1]. The function of this region is uncertain.
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Ontology Term
PANTHER:PTHR24186 | PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT
 
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Ontology Term
Pfam:PF12796 | Ankyrin repeats (3 copies)
Description: NULL
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Ontology Term
Pfam:PF13962 | Domain of unknown function
Description: The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.
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Ontology Term
PANTHER:PTHR15952 | EXPORTIN-T/LOS1
 
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Ontology Term
PANTHER:PTHR15952:SF11 | EXPORTIN-T
 
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Ontology Term
Pfam:PF08389 | Exportin 1-like protein
Description: The sequences featured in this family are similar to a region close to the N-terminus of yeast exportin 1 (Xpo1, Crm1, Swiss:P14068). This region is found just C-terminal to an importin-beta N-terminal domain (Pfam:PF03810) in many members of this family. Exportin 1 is a nuclear export receptor that interacts with leucine-rich nuclear export signal (NES) sequences, and Ran-GTP, and is involved in translocation of proteins out of the nucleus [1,2].
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Ontology Term
PANTHER:PTHR11771 | LIPOXYGENASE
 
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Ontology Term
Pfam:PF00305 | Lipoxygenase
Description: NULL
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Ontology Term
Pfam:PF01477 | PLAT/LH2 domain
Description: This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase Pfam:PF01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.
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Ontology Term
PANTHER:PTHR30540 | OSMOTIC STRESS POTASSIUM TRANSPORTER
 
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Ontology Term
Pfam:PF02705 | K+ potassium transporter
Description: This is a family of K+ potassium transporters that are conserved across phyla, having both bacterial (KUP) Swiss:P30016 [3], yeast (HAK) Swiss:P50505 [2], and plant (AtKT) Swiss:O22397 [1] sequences as members.
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Ontology Term
PANTHER:PTHR22835 | ZINC FINGER FYVE DOMAIN CONTAINING PROTEIN
 
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Ontology Term
Pfam:PF00657 | GDSL-like Lipase/Acylhydrolase
Description: NULL
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Ontology Term
Pfam:PF03168 | Late embryogenesis abundant protein
Description: Different types of LEA proteins are expressed at different stages of late embryogenesis in higher plant seed embryos and under conditions of dehydration stress. The function of these proteins is unknown. This family represents a group of LEA proteins that appear to be distinct from those in Pfam:PF02987. The family DUF1511, Pfam:PF07427, has now been merged into this family.
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Ontology Term
PANTHER:PTHR31190 | DNA-BINDING DOMAIN
 
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Ontology Term
Pfam:PF00847 | AP2 domain
Description: This 60 amino acid residue domain can bind to DNA [2] and is found in transcription factor proteins.
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Ontology Term
PANTHER:PTHR10795 | PROPROTEIN CONVERTASE SUBTILISIN/KEXIN
 
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Ontology Term
Pfam:PF00082 | Subtilase family
Description: Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Pfam:PF00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.
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Ontology Term
Pfam:PF05922 | Peptidase inhibitor I9
Description: This family includes the proteinase B inhibitor from Saccharomyces cerevisiae and the activation peptides from peptidases of the subtilisin family. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase [1], but have also been shown to act as 'temporary inhibitors' [2].
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Ontology Term
PANTHER:PTHR10233 | TRANSLATION INITIATION FACTOR EIF-2B
 
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Ontology Term
Pfam:PF01008 | Initiation factor 2 subunit family
Description: This family includes initiation factor 2B alpha, beta and delta subunits from eukaryotes, initiation factor 2B subunits 1 and 2 from archaebacteria and some proteins of unknown function from prokaryotes. Initiation factor 2 binds to Met-tRNA, GTP and the small ribosomal subunit. Members of this family have also been characterised as 5-methylthioribose- 1-phosphate isomerases, an enzyme of the methionine salvage pathway. The crystal structure of Ypr118w, a non-essential, low-copy number gene product from Saccharomyces cerevisiae, reveals a dimeric protein with two domains and a putative active site cleft [2].
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Ontology Term
PANTHER:PTHR23073 | 26S PROTEASOME REGULATORY SUBUNIT
 
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Ontology Term
PANTHER:PTHR23073:SF13 | 26S PROTEASOME REGULATORY SUBUNIT 7
 
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Ontology Term
Pfam:PF00004 | ATPase family associated with various cellular activities (AAA)
Description: AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].
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Ontology Term
PANTHER:PTHR24420 | LEUCINE-RICH REPEAT RECEPTOR-LIKE PROTEIN KINASE
 
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Ontology Term
PANTHER:PTHR24420:SF440 | PROTEIN STRUBBELIG-RECEPTOR FAMILY 8
 
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Ontology Term
Pfam:PF00069 | Protein kinase domain
Description: NULL
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Ontology Term
Pfam:PF00560 | Leucine Rich Repeat
Description: CAUTION: This Pfam may not find all Leucine Rich Repeats in a protein. Leucine Rich Repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
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Ontology Term
Pfam:PF12799 | Leucine Rich repeats (2 copies)
Description: Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
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Ontology Term
PANTHER:PTHR24093 | CATION TRANSPORTING ATPASE
 
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Ontology Term
PANTHER:PTHR24093:SF127 | SODIUM TRANSPORT ATPASE 1-RELATED
 
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Ontology Term
Pfam:PF00690 | Cation transporter/ATPase, N-terminus
Description: Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport.
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Ontology Term
Pfam:PF00702 | haloacid dehalogenase-like hydrolase
Description: This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain [1]. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria [2].
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Ontology Term
Pfam:PF13246 | Cation transport ATPase (P-type)
Description: This domain is found in cation transport ATPases, including phospholipid-transporting ATPases, calcium-transporting ATPases, and sodium-potassium ATPases [1-2].
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Ontology Term
Pfam:PF08137 | DVL family
Description: This family consists of the DVL family of proteins. In a gain-of-function genetic screen for genes that influence fruit development in Arabidopsis, DEVIL (DVL) gene was identified. DVL is a small protein and overexpression of the protein results in pleiotropic phenotypes featured by shortened stature, rounder rosette leaves, clustered inflorescences, shortened pedicles, and siliques with pronged tips. DVL family is a novel class of small polypeptides and the overexpression phenotypes suggest that these polypeptides may have a role in plant development [1].
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Ontology Term
Pfam:PF07714 | Protein tyrosine and serine/threonine kinase
Description: Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [1]; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.
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Ontology Term
Pfam:PF08263 | Leucine rich repeat N-terminal domain
Description: Leucine Rich Repeats Pfam:PF00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.
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Ontology Term
Pfam:PF13855 | Leucine rich repeat
Description: NULL
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Ontology Term
PANTHER:PTHR32440 | PHOSPHATASE DCR2-RELATED-RELATED
 
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Ontology Term
PANTHER:PTHR32440:SF0 | PHOSPHATASE DCR2-RELATED
 
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Ontology Term
Pfam:PF00149 | Calcineurin-like phosphoesterase
Description: This family includes a diverse range of phosphoesterases [1], including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD Swiss:P13457 or yeast MRE11 Swiss:P32829. The most conserved regions in this superfamily centre around the metal chelating residues.
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Ontology Term
PANTHER:PTHR21649 | CHLOROPHYLL A/B BINDING PROTEIN
 
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Ontology Term
Pfam:PF00504 | Chlorophyll A-B binding protein
Description: NULL
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Ontology Term
PANTHER:PTHR31140 | B3 DOMAIN-CONTAINING TRANSCRIPTION FACTOR ABI3
 
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Ontology Term
Pfam:PF02362 | B3 DNA binding domain
Description: This is a family of plant transcription factors with various roles in development, the aligned region corresponds the B3 DNA binding domain as described in [1] this domain is found in VP1/AB13 transcription factors [2]. Some proteins also have a second AP2 DNA binding domain Pfam:PF00847 such as RAV1 Swiss:Q9ZWM9 [1]. DNA binding activity was demonstrated by [3].
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Ontology Term
PANTHER:PTHR14950 | DICER-RELATED
 
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Ontology Term
Pfam:PF00270 | DEAD/DEAH box helicase
Description: Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
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Ontology Term
Pfam:PF00271 | Helicase conserved C-terminal domain
Description: The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
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Ontology Term
Pfam:PF02170 | PAZ domain
Description: This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain is found in two families of proteins that are involved in post-transcriptional gene silencing. These are the Piwi family and the Dicer family, that includes the Carpel factory protein. The function of the domains is unknown but has been suggested to mediate complex formation between proteins of the Piwi and Dicer families by hetero-dimerisation. The three-dimensional structure of this domain has been solved [2-4]. The PAZ domain is composed of two subdomains. One subdomain is similar to the OB fold, albeit with a different topology. The OB-fold is well known as a single-stranded nucleic acid binding fold. The second subdomain is composed of a beta-hairpin followed by an alpha-helix. The PAZ domains shows low-affinity nucleic acid binding and appears to interact with the 3' ends of single-stranded regions of RNA in the cleft between the two subdomains. PAZ can bind the characteristic two-base 3' overhangs of siRNAs, indicating that although PAZ may not be a primary nucleic acid binding site in Dicer or RISC, it may contribute to the specific and productive incorporation of siRNAs and miRNAs into the RNAi pathway.
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Ontology Term
Pfam:PF03368 | Dicer dimerisation domain
Description: This domain is found in members of the Dicer protein family which function in RNA interference, an evolutionarily conserved mechanism for gene silencing using double-stranded RNA (dsRNA) molecules. It is essential for the activity of Dicer [1,2]. It is a divergent double stranded RNA-binding domain [3]. The N-terminal alpha helix of this domain is in a different orientation to that found in canonical dsRNA-binding domains. This results in a change of charge distribution at the potential dsRNA-binding surface and in the N- and C-termini of the domain being in close proximity [4]. This domain has weak dsRNA-binding activity. It mediates heterodimerisation of Dicer proteins with their respective protein partners [4].
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Ontology Term
Pfam:PF00035 | Double-stranded RNA binding motif
Description: Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localisation of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.
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Ontology Term
Pfam:PF00636 | Ribonuclease III domain
Description: NULL
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Ontology Term
Pfam:PF14709 | double strand RNA binding domain from DEAD END PROTEIN 1
Description: A C-terminal domain in human dead end protein 1 (DND1_HUMAN) homologous to double strand RNA binding domains (PF00035, PF00333)
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Ontology Term
PANTHER:PTHR10286 | INORGANIC PYROPHOSPHATASE
 
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Ontology Term
Pfam:PF00719 | Inorganic pyrophosphatase
Description: NULL
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Ontology Term
PANTHER:PTHR12802 | SWI/SNF COMPLEX-RELATED
 
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Ontology Term
PANTHER:PTHR31415 | OS05G0367900 PROTEIN
 
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Ontology Term
PANTHER:PTHR31415:SF0 | LATE EMBRYOGENESIS ABUNDANT HYDROXYPROLINE-RICH GLYCOPROTEIN-RELATED
 
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Ontology Term
PANTHER:PTHR31319 | ZINC FINGER PROTEIN CONSTANS-LIKE 4
 
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Ontology Term
Pfam:PF06203 | CCT motif
Description: This short motif is found in a number of plant proteins. It is rich in basic amino acids and has been called a CCT motif after Co, Col and Toc1 [1]. The CCT motif is about 45 amino acids long and contains a putative nuclear localisation signal within the second half of the CCT motif [1]. Toc1 mutants have been identified in this region.
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Ontology Term
PANTHER:PTHR26402 | RESPONSE REGULATOR OF TWO-COMPONENT SYSTEM
 
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Ontology Term
Pfam:PF00072 | Response regulator receiver domain
Description: This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.
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Ontology Term
PANTHER:PTHR24016 | CONSERVED OLIGOMERIC GOLGI COMPLEX SUBUNIT 4
 
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Ontology Term
PANTHER:PTHR24016:SF0 | CONSERVED OLIGOMERIC GOLGI COMPLEX SUBUNIT 4
 
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Ontology Term
Pfam:PF08318 | COG4 transport protein
Description: This region is found in yeast oligomeric golgi complex component 4 which is involved in ER to Golgi an intra Golgi transport [1].
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Ontology Term
Pfam:PF12854 | PPR repeat
Description: This family matches additional variants of the PPR repeat that were not captured by the model for Pfam:PF01535. The exact function is not known.
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Ontology Term
Pfam:PF13041 | PPR repeat family
Description: This repeat has no known function. It is about 35 amino acids long and is found in up to 18 copies in some proteins. The family appears to be greatly expanded in plants and fungi. The repeat has been called PPR [1].
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Ontology Term
PANTHER:PTHR21141 | 60S ACIDIC RIBOSOMAL PROTEIN FAMILY MEMBER
 
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Ontology Term
Pfam:PF00428 | 60s Acidic ribosomal protein
Description: This family includes archaebacterial L12, eukaryotic P0, P1 and P2.
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Ontology Term
Pfam:PF14009 | PADRE domain
Description: This entry represents the Pathogen and abiotic stress response, cadmium tolerance, disordered region-containing (PADRE) domain, which is specifically found in plants. PADRE typically occurs in small single-domain proteins with a bipartite architecture. PADRE contains conserved sequence motifs at the N-terminal, and its C-terminal includes an intrinsically disordered region with multiple phosphorylation sites. This domain is associated with plant defense upon diverse stress stimulus and has a role in disease resistance to fungi [1].
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Ontology Term
PANTHER:PTHR24011 | FAMILY NOT NAMED
 
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Ontology Term
Pfam:PF00076 | RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)
Description: The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins (Swiss:P05455) have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteristic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins (Swiss:P05455) are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.
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Ontology Term
PANTHER:PTHR31561 | 3-KETOACYL-COA SYNTHASE
 
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Ontology Term
Pfam:PF08392 | FAE1/Type III polyketide synthase-like protein
Description: The members of this family are described as 3-ketoacyl-CoA synthases, type III polyketide synthases, fatty acid elongases and fatty acid condensing enzymes, and are found in both prokaryotic and eukaryotic (mainly plant) species. The region featured in this family contains the active site residues, as well as motifs involved in substrate binding [1].
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Ontology Term
Pfam:PF08541 | 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal
Description: This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
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Ontology Term
PANTHER:PTHR24347 | SERINE/THREONINE-PROTEIN KINASE
 
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Ontology Term
Pfam:PF03822 | NAF domain
Description: NULL
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Ontology Term
PANTHER:PTHR23177 | MKIAA1688 PROTEIN
 
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Ontology Term
Pfam:PF00620 | RhoGAP domain
Description: GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
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Ontology Term
Pfam:PF00786 | P21-Rho-binding domain
Description: Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).
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Ontology Term
PANTHER:PTHR31374 | AUXIN-INDUCED PROTEIN-LIKE-RELATED
 
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Ontology Term
Pfam:PF02519 | Auxin responsive protein
Description: This family consists of the protein products of the ARG7 auxin responsive genes family none of which have any identified functional role.
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Ontology Term
PANTHER:PTHR19359 | CYTOCHROME B5
 
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Ontology Term
Pfam:PF00173 | Cytochrome b5-like Heme/Steroid binding domain
Description: This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors such as Swiss:O00264 [1,2]. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
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Ontology Term
Pfam:PF13301 | Protein of unknown function (DUF4079)
Description: This is an uncharacterised family of proteins.
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Ontology Term
PANTHER:PTHR14155 | RING FINGER DOMAIN-CONTAINING
 
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Ontology Term
Pfam:PF13639 | Ring finger domain
Description: NULL
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Ontology Term
Pfam:PF03331 | UDP-3-O-acyl N-acetylglycosamine deacetylase
Description: The enzymes in this family catalyse the second step in the biosynthetic pathway for lipid A.
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Ontology Term
Pfam:PF14363 | Domain associated at C-terminal with AAA
Description: This domain is found in association with the AAA family, Pfam:PF00004.
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Ontology Term
Pfam:PF00213 | ATP synthase delta (OSCP) subunit
Description: The ATP D subunit from E. coli is the same as the OSCP subunit which is this family. The ATP D subunit from metazoa are found in family Pfam:PF00401.
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Ontology Term
PANTHER:PTHR10891 | EF-HAND CALCIUM-BINDING DOMAIN CONTAINING PROTEIN
 
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Ontology Term
Pfam:PF13833 | EF-hand domain pair
Description: NULL
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Ontology Term
PANTHER:PTHR32463 | L-FUCOSE KINASE
 
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Ontology Term
PANTHER:PTHR32463:SF0 | L-FUCOSE KINASE
 
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Ontology Term
Pfam:PF00385 | Chromo (CHRromatin Organisation MOdifier) domain
Description: NULL
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Ontology Term
Pfam:PF08544 | GHMP kinases C terminal
Description: This family includes homoserine kinases, galactokinases and mevalonate kinases.
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Ontology Term
Pfam:PF04970 | Lecithin retinol acyltransferase
Description: The full-length members of this family, eg Swiss:P53816, are representatives of a novel class II tumour-suppressor family, designated as H-REV107-like. This domain is the catalytic N-terminal proline-rich region of the protein. The downstream region is a putative C-terminal transmembrane domain which is found to be crucial for cellular localisation, but not necessary for the enzyme activity [1]. H-REV107-like proteins are homologous to lecithin retinol acyltransferase (LRAT), an enzyme that catalyses the transfer of the sn-1 acyl group of phosphatidylcholine to all-trans-retinol and forming a retinyl ester [2].
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