SII-SWORD/CoKE huggingface dataset:
Pfam PF11765: Hyphally regulated cell wall protein N-terminal (repeat)
The proteins in this family are all fungal and largely annotated as being hyphally regulated cell wall proteins, that are induced in response to hyphal development. Proteins containing this domain include Hpf1 from budding yeasts and Hyr1 from Candida albicans. Hpf1 can reduce haziness in white wine. Hyr1 is a GPI-anchored hyphal cell wall protein required for hyphal growth and virulence. It is involved in innate immune cell evasion through confering resistance to neutrophil killing. This entry represents the N-terminal domain, which adopts a pectate lyase-like fold.
Pfam PF10270: Membrane magnesium transporter (family)
This entry represents a novel family of membrane magnesium transporters (MMgT). The proteins, MMgT1 and MMgT2, are localised to the Golgi complex and post-Golgi vesicles, including the early endosomes, suggesting that they may provide regulated pathways for Mg(2+) transport in the Golgi and post-Golgi organelles of epithelium-derived cells.
Pfam PF00872: Transposase, Mutator family (family)
Autonomous mobile genetic elements such as transposon or insertion sequences (IS) encode an enzyme, transposase, that is required for excising and inserting the mobile element. Transposases have been grouped into various families . The mutator family of transposases consists of a number of elements that include, mutator from maize, IsT2 from Thiobacillus ferrooxidans, Is256 from Staphylococcus aureus, Is1201 from Lactobacillus helveticus, Is1081 from Mycobacterium bovis, IsRm3 from Rhizobium meliloti and others.
Pfam PF13720: Udp N-acetylglucosamine O-acyltransferase; Domain 2 (domain)
This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase.  This enzyme is a zinc-dependent enzyme that catalyses the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.
Wikipedia: An acetyltransferase is any of a class of transferase enzymes that transfers an acetyl group in a reaction called acetylation. In biological organisms, post-translational modification of a protein via acetylation can profoundly transform its functionality by altering various properties like hydrophobicity, solubility, and surface attributes. These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules.
Pfam PF20972: MASE9 (domain)
This entry represents the membrane-associated sensor domain 9 (MASE9), which has been found in combination with HD-GYP and GGDEF-EAL domains , or in MASE9-HD-GYP-GAF-GGDEF domain architecture. It has 8 predicted transmembrane (TM) segments of which two are likely to form an intramembrane hairpin. It has several charged residues in the hydrophobic core of the membrane, that, in addition to the poor conservation of the short periplasmic segments, suggests that ligand binding and/or protein-protein interactions by MASE9 may occur within the membrane.
Pfam PF05918: Apoptosis inhibitory protein 5 (API5) (repeat)
This family consists of apoptosis inhibitory protein 5 (API5) sequences from several organisms. Apoptosis or programmed cell death is a physiological form of cell death that occurs in embryonic development and organ formation. It is characterised by biochemical and morphological changes such as DNA fragmentation and cell volume shrinkage. API5 is an anti apoptosis gene located in human chromosome 11, whose expression prevents the programmed cell death that occurs upon the deprivation of growth factors and is up-regulated in various cancer cells. This protein has an elongated all alpha-helical structure, in which the N-terminal half is similar to the HEAT repeat and the C-terminal half is similar to the ARM (Armadillo-like) repeat. This suggests that API5 is involved in protein-protein interactions and may act as a scaffold for multiprotein complexes.
Pfam PF06672: Protein of unknown function (DUF1175) (family)
This family consists of several hypothetical bacterial proteins of around 210 residues in length. The function of this family is unknown.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF05055: Protein of unknown function (DUF677) (family)
This family consists of AT14A like proteins from Arabidopsis thaliana. At14a has a small domain that has sequence similarities to integrins from fungi, insects and humans. Transcripts of At14a are found in all  Arabidopsis tissues and localises partly to the plasma membrane.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF23293: ULTRAPETALA1 zinc finger domain (domain)
This domain is found in the family of ULTRAPETALA proteins ULT1/2 from Arabidopsis thaliana and related plant proteins. ULT1/2 are putative transcription factors that act as regulators of cell accumulation in shoot and floral meristems. They also act as antirepressors that counteract EMBRYONIC FLOWER1 (EMF1) action through modulation of histone marks on target genes and thus regulating their transcriptional activities. This domain contains several highly conserved cysteine and histidine residues that could be involved in metal coordination. In the core part, this domain shares similarity with CW-type zinc finger domains ([pfam:PF07496]) but it has additional clusters of conserved residues indicating the presence of four putative metal-binding sites.
Pfam PF23603: Telomere repeat-binding protein 1-like, ubiquitin-like domain (domain)
This domain is found in Telomere repeat-binding protein 1 from Arabidopsis thaliana (TPR1) and similar plant proteins. TPR1 binds specifically to the plant telomeric double-stranded DNA sequences 5'-GGTTTAG-3'. This domain is predicted to adopt a ubiquitin-like fold.
Pfam PF15058: Speriolin N terminus (family)
This family represents the N-terminus of the sperm centrosome protein speriolin.
Pfam PF06159: Trafficking protein particle complex subunit 13, N-terminal (domain)
Trafficking protein particle complex subunit 13 (TRAPPC13) is involved in regulating autophagy and survival in response to small molecule compound-induced Golgi stress. This entry represents the N-terminal domain, which may adopt a beta-sandwich fold with an insertion at the very N-terminal consisting of a short beta-strand and alpha helix connected by a long loop.
Pfam PF17337: Galactose-inhibitable lectin 35 kDa subunit (family)
The role of the cell surface D-galactose (Gal)/N-Acetyl-D-galactosamine (GalNAc), lectin in the adhesion process has been demonstrated in Entamoeba histolytica, a protozoan parasite that causes amebiasis in humans. The Gal/GalNAc lectin is a heterotrimeric protein complex. It is composed of a 260 kDa heterodimer of trans-membrane disulphide-linked heavy 170 kDa subunit and glycosylphosphatidylinositol (GPI)-anchored light 31 kDa/35 kDa subunits. The light subunits are non-covalently associated with an intermediate subunit of 150 kDa. Inhibition of expression of 35 kDa subunit of Gal/GalNAc lectin inhibits the cytotoxic and cytopathic activity of E. histolytica, but no decrease in adherence capacity to mammalian cells was evident. Interestingly, a carbohydrate-binding activity has been reported for the 35 kDa light subunit of the lectin molecules of the closely related Entamoeba invadens. This entry is related to the light subunit where this domain of unknown function is present. The light subunit consists of several polypeptide chains with considerable antigenic homology. The two light (31/35 kDa) subunits of the lectin are present in two isoforms: the 31 kDa isoform is glycerolphosphatidylinositol (GPI) anchored; and the 35 kDa isoform is more highly glycosylated.
Pfam PF12086: Protein of unknown function (DUF3563) (family)
This family of proteins is functionally uncharacterised. This protein is found in bacteria. Proteins in this family are about 50 amino acids in length. This protein has conserved AYL and DLE sequence motifs.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF06877: Regulator of ribonuclease activity B (domain)
This family of proteins regulate mRNA abundance by binding to RNaseE and inhibiting its endonucleolytic activity. A subset of these proteins are predicted to function as immunity proteins.
Pfam PF07776: Zinc-finger associated domain (zf-AD) (domain)
The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold.  The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.
Pfam PF03080: Neprosin (family)
Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes including peptidases. One of these is neprosin, characterized from the pitcher plant Nepenthes ventrata. This peptidase is of unknown catalytic type and is unaffected by standard peptidase inhibitors. Unusually, activity is directed towards prolyl bonds, but unlike most peptidase that cleave after proline, there is no restriction on sequence length or position of the proline residue. The peptidase is secreted and is presumed to possess an N-terminal activation peptide. The neprosin domain corresponds to the mature peptidase. It is not known if other proteins with this domain are peptidases.
Pfam PF10223: Menorin (family)
This family includes proteins FAM151A and FAM151B, the mammalian homologues of C. elegans menorin which is involved in generation of neurons and regulation of dendrite extension. FAM151B has been shown to be essential for retinal function. Sequence analysis and the fact that these proteins have a TIM-barrel fold similar to that in phospholipase D and glycerophosphodiester phosphodiesterase (GDPD) families, indicate that they belong to PLC-like phosphodiesterase superfamily, although their substrates and function remain unknown.
Pfam PF18761: Heliorhodopsin (domain)
Heliorhodopsins, distantly related to type-1 rhodopsins, are embedded in the membrane with their N termini facing the cell cytoplasm, an orientation that is opposite to that of type-1 or type-2 rhodopsins. Heliorhodopsins show photocycles that are longer than one second, which is suggestive of light-sensory activity. Heliorhodopsin photocycles accompany retinal isomerization and proton transfer, as in type-1 and type-2 rhodopsins, but protons are never released from the protein.The structures of several heliorhodopsins have been solved displaying seven transmembrane helices (TM), six loops and short N and C termini. Heliorhodopsins share a common fold with the type-1 rhodopsins, however there are clear structural differences, particularly within the loop regions and the large cavity in the cytoplasmic part of heliorhodpsin. Heliorhodpsins are present in Archaea, Bacteria, Eukarya, and viruses.
Wikipedia: Heliorhodopsin is a family of rhodopsins discovered in 2018 by Alina Pushkarev in the laboratory of Professor Oded Beja. The new family of heliorhodopsins has a distinct protein sequence from known Type 1 (microbial) and Type 2 (animal) rhodopsins. Heliorhodopsins also exhibit the reverse orientation in the membrane compared with the other rhodopsins, with the N-terminus facing the inside of the cell and the C-terminus outside the cell.
Pfam PF03047: COMC family (family)
This family consists exclusively of streptococcal competence stimulating peptide precursors, which are generally up to 50 amino acid residues long. In all the members of this family, the leader sequence is cleaved after two conserved glycine residues; thus the leader sequence is of the double- glycine type. Competence stimulating peptides (CSP) are small (less than 25 amino acid residues) cationic peptides. The N-terminal amino acid residue is negatively charged, either glutamate or aspartate. The C-terminal end is positively charged. The third residue is also positively charged: a highly conserved arginine. A few COMC proteins and their precursors (not included in this family) do not fully follow the above description. In particular: the leader sequence in the CSP precursor from Streptococcus sanguis NCTC 7863 [swissprot:O33758] is not of the double-glycine type; the CSP from Streptococcus gordonii NCTC 3165 [swissprot:O33645] does not have a negatively charged N-terminus residue and has a lysine instead of arginine at the third position.  Functionally, CSP act as pheromones, stimulating competence for genetic transformation in streptococci. In streptococci, the (CSP mediated) competence response requires exponential cell growth at a critical density, a relatively simple requirement when compared to the stationary-phase requirement of Haemophilus, or the late-logarithmic- phase of Bacillus. All bacteria induced to competence by a particular CSP are said to belong to the same pherotype, because each CSP is recognised by a specific receptor (the signalling domain of a histidine kinase ComD). Pherotypes are not necessarily species-specific. In addition, an organism may change pherotype. There are two possible mechanisms for pherotype switching: horizontal gene transfer, and accumulation of point mutations. The biological significance of pherotypes and pherotype switching is not definitively determined. Pherotype switching occurs frequently enough in naturally competent streptococci to suggest that it may be an important contributor to genetic exchange between different bacterial species. The family Antibacterial16, streptolysins from group A streptococci, has been merged into this family.
Pfam PF07341: Protein of unknown function (DUF1473) (family)
This family consists of several hypothetical bacterial proteins of around 150 residues in length. Members of this family seem to be found exclusively in Borrelia burgdorferi (Lyme disease spirochete). The function of this family is unknown.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF04523: Herpes virus tegument protein U30 (family)
This family is named after the human herpesvirus protein, but has been characterised in cytomegalovirus as UL47. Cytomegalovirus UL47 is a component of the tegument, which is a protein layer surrounding the viral capsid. UL47 co-precipitates with UL48 and UL69 tegument proteins, and the major capsid protein UL86.  A UL47-containing complex is thought to be involved in the release of viral DNA from the disassembling virus particle.
Pfam PF25110: Separase-like, TPR repeats (repeat)
This region of tetratricopeptide (TPR)-like repeats is found in Separase from Arabidopsis thaliana (ESP1) and similar plant proteins. ESP1 is essential for embryo and endosperm development and may play a role in centromeric heterochromatin structure /formation during early meiosis, non-homologous centromere association and radial microtubule system.
Pfam PF19269: Anticodon binding domain (domain)
This entry represents the anticodon binding domain found at the C-terminus of the class-I glutamyl tRNA synthetase enzyme.
Pfam PF20457: Family of unknown function (DUF6710) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are typically between 220 and 300 amino acids in length.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF12602: Fertility inhibition protein N terminal (family)
This domain family is found in bacteria, and is typically between 62 and 102 amino acids in length. The family is found in association with [pfam:PF04352]. The FinOP (fertility inhibition) system of F-like plasmids consists of an antisense RNA (FinP) and a 22 kDa protein (FinO) which act in concert to prevent the translation of TraJ, the positive regulator of the transfer operon.
Pfam PF16408: Domain of unknown function (DUF5016) (family)
This family of proteins is functionally uncharacterised. This family is found in various Bacteroides species. Proteins in this family are around 660 amino acids in length.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF21123: Dna2 Rift barrel domain (domain)
This entry represents a Rift barrel domain found in the Dna2 protein. This domain lies between the nuclease and helicase domains. The Dna2 nuclease-helicase maintains genomic integrity by processing DNA double-strand breaks, Okazaki fragments and stalled replication forks. Dna2 requires ssDNA ends, and is dependent on the ssDNA-binding protein Rpa, which controls cleavage polarity.
Pfam PF06161: Protein of unknown function (DUF975) (family)
Family of uncharacterised bacterial proteins.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF07540: Nucleolar complex-associated protein (family)
Nucleolar complex-associated protein (Noc3p, [swissprot:Q07896]) is conserved in eukaryotes and has essential roles in replication and rRNA processing in Saccharomyces cerevisiae.
Pfam PF06903: VirK protein (family)
This family consists of several bacterial VirK proteins of around 145 residues in length. The function of this family is unknown.
Pfam PF21300: Grass antifreeze beta roll (repeat)
The grass Lolium perenne produces an ice-binding protein (LpIBP) that helps this perennial tolerate freezing by inhibiting the recrystallization of ice. Ice-binding proteins (IBPs) are also produced by freeze-avoiding organisms to halt the growth of ice and are better known as antifreeze proteins (AFPs). The ice-binding site (IBS) is formed by a flat beta-sheet on one surface of the beta-roll. This region folds as a left-handed beta-helix. Each of the eight beta-helical coils is composed of two seven-residue tandem repeats with a consensus sequence XXNXVXG where X is a solvent-exposed residue, typically with a polar side chain.
Pfam PF06239: Evolutionarily conserved signalling intermediate in Toll pathway (repeat)
Activation of NF-kappaB as a consequence of signaling through the Toll and IL-1 receptors is a major element of innate immune responses. ECSIT plays an important role in signalling to NF-kappaB, functioning as the intermediate in the signaling pathways between TRAF-6 and MEKK-1. It is part of the MCIA ((mitochondrial complex I intermediate assembly) complex, involved in the assembly of mitochondrial complex I. This is the N-terminal helical domain of ECSIT which adopts a TPR-like structure.
Pfam PF16945: Putative lactococcus lactis phage r1t holin (family)
Phage_r1t_holin is a family of putative phage r1t holins from lactococcus. these holins carry two hydrophobic putative TMs separated by a short beta-turn region.
Pfam PF23822: Domain of unknown function (DUF7192) (domain)
This entry represents a bacterial domain of unknown function. The domain is around 270 to 300 amino acids in length. It is found in a variety of bacterial phyla including Actinobacteria, Bacteroidota, Pseudomonadota and Verrucomicrobiota. The domain is also found in some bacterial phages.  The function of this domain is unknown. The structure of this domain shows similarity to VWFA domains.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF04003: Dip2/Utp12 Family (family)
This domain is found at the C-terminus of proteins containing WD40 repeats.  These proteins are part of the U3 ribonucleoprotein the yeast protein is called Utp12 or DIP2 [swissprot:Q12220].
Pfam PF12946: MSP1 EGF domain 1 (domain)
This EGF-like domain is found at the C-terminus of the malaria parasite MSP1 protein. MSP1 is the merozoite surface protein 1. This domain is part of the C-terminal fragment that is proteolytically processed from the the rest of the protein and is left attached to the surface of the invading parasite.
Pfam PF14504: CAP-associated N-terminal (domain)
The function of this domain is unknown, but it is found towards the N-terminus of bacterial proteins carrying the CAP domain, [pfam:PF00188]. All members that do not otherwise carry an additional Cu_amine_oxidN1, [pfam:PF07833], domain are likely to be extracellular as they start with a signal-peptide. Most other non-bacterial proteins with the CAP domain are allergenic.
Pfam PF14545: Dof, BCAP, and BANK (DBB) motif, (domain)
The DBB domain is named from the Drosophila (Downstream of FGFR - Dof, also known as Heartbroken or Stumps) protein, the BANKS and BCAP, both signalling in B-cell pathway, proteins. This domain defines a minimal region required for mediating Dof dimerisation. Since this domain can interact both with itself and with a region in the C-terminal part of the molecule, it may mediate either intermolecular or intramolecular interactions. Mutants lacking this domain disrupt FGFR signal transduction and fibroblast growth-factor signalling. The DBB domain of BCAP mediates BCAP TIR dimerization and negatively regulates TLR signalling.