SII-SWORD/CoKE huggingface dataset:
Pfam PF11946: Domain of unknown function (DUF3463) (family)
This presumed domain is functionally uncharacterised. This domain is found in bacteria and archaea. This domain is about 140 amino acids in length. This domain is found associated with [pfam:PF04055]. This domain has two conserved sequence motifs: CTPWG and PCYL, plus a highly conserved CxxCxxHC motif.
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 PF17239: Family of unknown function (DUF5312) (family)
This is a family of unknown function, mostly found in Spirochaeta.
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 PF16531: Centriolar protein SAS N-terminal domain (domain)
This entry represents the N-terminal domain of the SAS-6 centriolar protein, both in C.elegans and in humans. The N-terminal domain is the region through which the 9 rod-shaped homodimers that SAS-6 forms on oligomerisation interact with each other. Proper functioning of the centriole requires this correct oligomerisation.
Pfam PF24041: Domain of unknown function (DUF7350) (domain)
This domain is found in uncharacterised archaeal proteins. It is predicted to adopt Ig-like fold.
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 PF24605: CEMIP domain X (domain)
This entry represents Domain X of CEMIP, CEMIP2 and very closely related sequences which is after the beta-helix domain. Proteins in this entry proteins are involved in the metabolism of hyaluronic acid (HA) and mediate the depolymerization of high-molecular-weight HA into intermediate-sized fragments, a process crucial for various physiological functions, including the regulation of angiogenesis, heart development, and cell migration. This domain has been called domain X in, its function is still unknown.
Pfam PF20113: Family of unknown function (DUF6503) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are typically between 238 and 271 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 PF12745: Anticodon binding domain of tRNAs (domain)
This is an HGTP_anticodon binding domain, found largely on Gcn2 proteins which bind tRNA to down regulate translation in certain stress situations.
Pfam PF21767: Cohesin subunit SCC3, C-terminal domain (repeat)
This domain is found at the C-terminal end of Cohesin subunit SCC3 from Saccharomyces cerevisiae and similar proteins from yeasts. SCC3 is a component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. This domain is is composed of a continuously twisted tandem array of antiparallel alpha-helices resembling tandem HEAT repeats. It binds to two small sections within Scc1, the other component of the complex.
Pfam PF22511: PolB1 Binding Protein 2 (family)
This is a family of archaeal proteins, previously known as DUF6995, representing homologues of PolB1 Binding Protein 2 (PBP2). PBP2, is a subunit of PolB1 enzyme that is a member of the archaeal B-family of DNA polymerases. PBP2 along with PBP1, associate with distinct surfaces of the larger catalytic subunit and influence the enzymatic properties of the DNA polymerase. Members of this family adopt a winged helix (HTH) fold.
Pfam PF19020: Ta1207 family (family)
The function of this family is unknown. The protein forms a homopentameric complex in T. acidophilum. Each protein is composed of two structurally similar domains.
Pfam PF11956: Ankyrin-G binding motif of KCNQ2-3 (family)
Interactions with ankyrin-G are crucial to the localisation of voltage-gated sodium channels (VGSCs) at the axon initial segment and for neurons to initiate action potentials. This conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) is required for ankyrin-G binding and functions to localise sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system. This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3, that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localised to the surface of axons both at the axonal initial segment and more distally, and this axonal initial segment targeting of surface KCNQ channels is mediated by these ankyrin-G binding motifs of KCNQ2 and KCNQ3. KCNQ3 is a major determinant of M channel localisation to the AIS, rather than KCNQ2. Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3).
Wikipedia: In molecular biology, the ankyrin-G binding motif of KCNQ2-3 is a protein motif found in the potassium channels KCNQ2 and KCNQ3.
Pfam PF18238: LnmK N-terminal Hot Dog Fold domain (domain)
This domain is found in LnmK and is present in Streptomyces atroolivaceus. LnmK is a bifunctional acyltransferase/decarboxylase (AT/DC) that catalyzes first self-acylation using methylmalonyl-CoA as a substrate and subsequently trans-acylation of the methylmalonyl group to the phosphopantetheinyl group of the LnmL acyl carrier protein. LnmK is a homodimer composed of two monomeric double-hot-dog folds (DHDF). This domain is the N-terminal hot dog fold.
Pfam PF05397: Mediator complex subunit 15 (family)
GAL11 or MED15 is one of the up to 32 or subunits of the Mediator complex which is found from fungi to humans. The Mediator complex interacts with RNA polymerase II and other general transcription factors to form the RNA polymerase II holoenzyme, thereby affecting transcription through targetting of activators and repressors. This family is found in fungi and the small metazoan starlet anemone.
Pfam PF17938: Tetracyclin repressor-like, C-terminal domain (domain)
This domain is found in the C-terminal region of putative TetR-family regulatory proteins.
Pfam PF14439: Bd3614-like deaminase (family)
A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Bdellovibrio Bd3614. They are typified by a distinct N-terminal globular domain. The Bdellovibrio version occurs in a predicted operon with a 23S rRNA G2445-modifying methylase suggesting that it might be involved in RNA editing.
Pfam PF20104: Family of unknown function (DUF6494) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are approximately 70 amino acids in length. There is a conserved SQREIE sequence motif.
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 PF25135: Domain of unknown function (DUF7822) (domain)
This domain is found N-terminal in uncharacterised bacterial proteins. It is predicted to adopt a globular structure consisting of a curved beta-sheet and alpha helices packed on one side of it.
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 PF12910: Antitoxin of toxin-antitoxin, RelE / RelB, TA system (domain)
This domain appears to be the N-terminus of the RelB antitoxin of toxin-antitoxin stability system or prevent-host death system. Together RelE toxin and the RelB antitoxin form a non-toxic complex.  Although toxin-antitoxin gene cassettes were first found in plasmids, it is clear that these loci are abundant in free-living prokaryotes, including many pathogenic bacteria, and these toxin-antitoxin loci provide a control mechanism that helps free-living prokaryotes cope with nutritional stress.
Pfam PF14131: Domain of unknown function (DUF4298) (family)
This family of bacterial proteins includes SPy_2034 from Streptococcus pyogenes, which is though to play an important role in the virulence of the bacteria. This protein shows a unique tetrameric organisation composed of four helix-loop- helix 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 PF22861: GEO12453p1-like (family)
This protein family includes GEO12453p1 from Drosophila melanogaster ([swissprot:Q9VV11], also known as CG13067) and similar sequences from arthropods. CG13067 is the product of a small open reading frame (small ORFs) contained in a long noncoding RNA (lncRNA).
Pfam PF17591: Herpesvirus UL41A (family)
Members of this family are found in Human cytomegalovirus. No known function has been reported.
Pfam PF16182: Putative adherens-junction anchoring region of AbLIM (family)
AbLIM_anchor is a domain lying between the LIM actin-binding and the vilin-head domain of actin-binding LIM proteins. It is likely that this domain is involved in anchoring abLIMs to circumferential actin bundles in specific cell types.
Pfam PF09059: TyeA (domain)
Members of this family are composed of two pairs of parallel alpha-helices, and interact with the bacterial protein YopN via hydrophobic residues located on the helices. Association of TyeA with the C terminus of YopN is accompanied by conformational changes in both polypeptides that create order out of disorder: the resulting structure then serves as an impediment to type III secretion of YopN.
Wikipedia: 

In molecular biology, the protein domain TyeA is short for Translocation of Yops into eukaryotic cells A. It controls the release of Yersinia outer proteins (Yops) which help Yersinia evade the immune system. More specifically, it interacts with the bacterial protein YopN via hydrophobic residues located on the helices.
Pfam PF11167: Protein of unknown function (DUF2953) (family)
This family of proteins has no known function.
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 PF12963: Protein of unknown function (DUF3852) (domain)
A family of uncharacterized proteins found by clustering human gut metagenomic sequences. This domain frequently seen with DUF3848.
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 PF08208: DNA-directed RNA polymerase I subunit RPA34.5 (family)
This is a family of proteins conserved from yeasts to human. Subunit A34.5 of RNA polymerase I is a non-essential subunit which is thought to help Pol I overcome topological constraints imposed on ribosomal DNA during the process of transcription.
Pfam PF10981: Protein of unknown function (DUF2788) (family)
This bacterial family of proteins have no known function.
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 PF19296: RelA/SpoT, AH and RIS domains (domain)
This entry represents the alpha helical (AH) and Ribosome-InterSubunit (RIS) domains found in RelA/SpoT proteins, adjacent to the ACT domain. AH domain interacts with A/R tRNA and links the very C-terminal subdomains with TGS domain. The RIS domain is part of the binding interface between the C-terminal region and the ribosome, bridging the large and the small ribosomal subunits. RIS contains a four-stranded beta-sheet and a short alpha-helix. RelA/SpoT-homologue proteins (RHS) mediate the stringent response in bacteria which enables its metabolic adaptation under stress conditions. These enzymes synthesise the second messenger (p)ppGpp, which is a regulatory metabolite of the stringent response characterised by growth arrest and the modulation of gene expression in response to various nutritional stresses.
Pfam PF20044: Family of unknown function (DUF6446) (family)
This family of proteins is functionally uncharacterised. This family of proteins is predominantly found in Rhodobacterales. Proteins in this family are typically between 160 and 175 amino acids in length. There are some conserved motifs: IDA/S, SSPxRxRACF and DG. Many members in this family are thought to be histidine kinases.
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 PF14745: WASH complex subunit 4, N-terminal (domain)
This entry is the conserved N-terminal region of proteins that form subunit 4 of the WASH complex, also known as subunit 7 or KIAA1033/SWIP. In species such as Drosophila this protein is the only component of the 'complex'. This complex is present at the surface of endosomes that recruits and activates the Arp2/3 complex to induce actin polymerisation. This domain comprises the WAHD1 and the TBR (tubulin-binding region) domains.
Pfam PF10610: Thin aggregative fimbriae synthesis protein (family)
Fimbriae are cell-surface protein polymers, of eg. E coli and Salmonella spp, that mediate interactions important for host and environmental persistence, development of biofilms, motility, colonisation and invasion of cells, and conjugation. Four general assembly pathways for different fimbriae have been proposed, one of which is extracellular nucleation-precipitation (ENP), that differs from the others in that fibre-growth occurs extracellularly. Thin aggregative fimbriae (Tafi) are the only fimbriae dependent on the ENP pathway. Tafi were first identified in Salmonella spp and the controlling operon termed agf; however subsequent isolation of the homologous operon in E coli led to its being called csg. Tafi are known as curli because, in the absence of extracellular polysaccharides, their morphology appears curled; however, when expressed with such polysaccharides their morphology appears as a tangled amorphous matrix. The gene agfC is found to be transcribed at low levels, localised to the periplasm in a mature form, and in combination with AgfE is important for AgfA extracellular assembly, which facilitates the synthesis of Tafi. The genes involved in Tafi production are organised into two adjacent divergently transcribed operons, agfBAC and agfDEFG, both of which are required for biosynthesis and assembly.
Pfam PF12484: PPE-SVP subfamily C-terminal region (family)
This domain family is found in bacteria, and is approximately 90 amino acids in length. The family is found to the C-terminus of [pfam:PF00823].  There is a conserved SVP sequence motif which is diagnostic of this subfamily. There is a single completely conserved residue W that may be functionally important. The proteins in this family are PPE proteins implicated in immunostimulation and virulence.
Pfam PF00709: Adenylosuccinate synthetase (domain)
Adenylosuccinate synthetase (6.3.4.4) plays an important role in purine biosynthesis, by catalysing the GTP-dependent conversion of IMP and aspartic acid to AMP. IMP and L-aspartate are conjugated in a two-step reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+. In the first step, the r-phosphate group of GTP is transferred to the 6-oxygen atom of IMP. An aspartate then displaces this 6-phosphate group to form the product adenylosuccinate. Adenylosuccinate synthetase has been characterised from various sources ranging from Escherichia coli (gene purA) to vertebrate tissues. In vertebrates, two isozymes are present: one involved in purine biosynthesis and the other in the purine nucleotide cycle.

The crystal structure of adenylosuccinate synthetase from E. coli reveals that the dominant structural element of each monomer of the homodimer is a central Î²-sheet of 10 strands. The first nine strands of the sheet are mutually parallel with right-handed crossover connections between the strands. The 10th strand is antiparallel with respect to the first nine strands. In addition, the enzyme has two antiparallel Î²-sheets, comprised of two strands and three strands each, 11 Î±-helices and two short 3/10-helices. Further, it has been suggested that the similarities in the GTP-binding domains of the synthetase and the p21ras protein are an example of convergent evolution of two distinct families of GTP-binding proteins . Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana when compared with the known structures from E. coli reveals that the overall fold is very similar to that of the E. coli protein .
Wikipedia: In molecular biology, adenylosuccinate synthase is an enzyme that plays an important role in purine biosynthesis, by catalysing the guanosine triphosphate (GTP)-dependent conversion of inosine monophosphate (IMP) and aspartic acid to guanosine diphosphate (GDP), phosphate and N(6)-(1,2-dicarboxyethyl)-AMP. Adenylosuccinate synthetase has been characterised from various sources ranging from Escherichia coli to vertebrate tissues. In vertebrates, two isozymes are present: one involved in purine biosynthesis and the other in the purine nucleotide cycle.
Pfam PF14459: Prokaryotic E2 family C (family)
A divergent member of the E2/UBC superfamily of proteins found in  bacteria. Members of the family contain a conserved cysteine in place of the histidine of the classical E2/UBC proteins. Members of this family are usually fused to an E1 domain at their C-terminus. The protein is usually in the gene neighborhood of a gene encoding a JAB peptidase and another encoding a predicted metal binding domain.
Pfam PF03099: Biotin/lipoate A/B protein ligase family (domain)
This family includes biotin protein ligase, lipoate-protein ligase A and B.  Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organism probably has only one BPL.  Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LPLA) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor.
Wikipedia: In molecular biology, the Cofactor transferase family is a family of protein domains that includes biotin protein ligases, lipoate-protein ligases A, octanoyl-(acyl carrier protein):protein N-octanoyltransferases, and lipoyl-protein:protein N-lipoyltransferases. The metabolism of the cofactors Biotin and lipoic acid share this family. They also share the target modification domain, and the sulfur insertion enzyme.
Pfam PF05163: DinB family (family)
DNA damage-inducible (din) genes in Bacillus subtilis are coordinately regulated and together compose a global regulatory network that has been termed the SOS-like or SOB regulon. This family includes DinB from B. subtilis.
Pfam PF17685: Transmembrane protein 250 (family)
This family includes human Transmembrane protein 250 (TM250) and similar proteins from vertebrates. TM250 is involved in cellular processes related to cell proliferation, specifically by aiding the transition into the S phase of the cell cycle. Additionally, it has a role in viral pathogenesis, as it is known to enhance the proliferation of human herpes simplex virus 1 (HHV-1).
Pfam PF06712: Protein of unknown function (DUF1199) (family)
This family consists of several hypothetical Feline immunodeficiency virus (FIV) proteins. Members of this family are typically around 67 residues long and are often annotated as ORF3 proteins. 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 PF00954: S-locus glycoprotein domain (domain)
In Brassicaceae, self-incompatible plants have a self/non-self recognition system.  This is sporophytically controlled by multiple alleles at a single locus (S). S-locus glycoproteins, as well as S-receptor kinases, are in linkage with the S-alleles. This region is inferred to be a domain due to it having other domains adjacent to it.