SII-SWORD/CoKE huggingface dataset:
Pfam PF12581: Protein of unknown function (DUF3756) (family)
This domain family is found in viruses, and is approximately 40 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 PF13296: Putative type VI secretion system Rhs element Vgr (family)
This is a family of putative type VI secretion system Rhs element Vgr proteins from Proteobacteria.
Pfam PF01185: Fungal hydrophobin (family)
The surface of many fungal spores is covered by a hydrophobic sheath, the rodlet layer, whose main component is a protein known as the rodlet protein . The rodlet proteins of Neurospora crassa (gene eas) and Emericella nidulans (gene rodA) are evolutionary related to proteins found in the cell wall of fruiting bodies of the mushroom Schizophyllum commune (Bracket fungus) . Collectively, these low-molecular-weight, cysteine-rich (eight conserved cysteines), hydrophobic proteins, are known as hydrophobins.
Wikipedia: Hydrophobins are a group of small cysteine-rich proteins that were discovered in filamentous fungi that are lichenized or not. Later similar proteins were also found in Bacteria. Hydrophobins are known for their ability to form a hydrophobic (water-repellent) coating on the surface of an object. They were first discovered and separated in Schizophyllum commune in 1991. Based on differences in hydropathy patterns and biophysical properties, they can be divided into two categories: class I and class II. Hydrophobins can self-assemble into a monolayer on hydrophilic:hydrophobic interfaces such as a water:air interface. Class I monolayer contains the same core structure as amyloid fibrils, and is positive to Congo red and thioflavin T. The monolayer formed by class I hydrophobins has a highly ordered structure, and can only be dissociated by concentrated trifluoroacetate or formic acid. Monolayer assembly involves large structural rearrangements with respect to the monomer.
Pfam PF14168: YjzC-like protein (family)
The YjzC-like protein family includes the B. subtilis YjzC protein [swissprot:O34585], which is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are approximately 60 amino acids in length.
Pfam PF18382: Formin N-terminal GBD (domain)
This is the N-terminal GTPase-binding domain (GBD) of formins also known as formin homology domain-containing proteins (FHOD). This GBD was initially described to be recruited by Rac and Ras GTPases in cells and to play play an essential role for FHOD1-mediated actin remodelling and transcriptional activation, localizes to specific GTPases in cells, and binds to GTPases in vitro. It exhibits structural similarity to the ubiquitin superfold as found, for example, in the Ras-binding domains of c-Raf1 or PI3 kinase, but contains an unusual loop that inserts into the first FH3 repeat. This domain has been described as a modulator of the binding specificity of the neighboring FH3 domain, making the paired domain specific for spectrin repeats rather than GTPase interaction.
Wikipedia: Formins (formin homology proteins) are a group of proteins that are involved in the polymerization of actin and associate with the fast-growing end (barbed end) of actin filaments. Most formins are Rho-GTPase effector proteins. Formins regulate the actin and microtubule cytoskeleton 
 and are involved in various cellular functions such as cell polarity, cytokinesis, cell migration and SRF transcriptional activity. Formins are multidomain proteins that interact with diverse signalling molecules and cytoskeletal proteins, although some formins have been assigned functions within the nucleus.
Pfam PF08936: Carboxysome Shell Carbonic Anhydrase, C-terminal (domain)
Carboxysome Shell Carbonic Anhydrase is a bacterial carbonic anhydrase localised in the carboxysome, where it converts bicarbonate ions to carbon dioxide for use in carbon fixation. It contains three domains, these being: (1) an N-terminal domain composed primarily of four alpha-helices; (2) a catalytic domain containing a tightly bound zinc ion and (3) a C-terminal domain with weak structural similarity to the catalytic domain. This entry represents the C-terminal domain which consists of a central five-stranded mixed beta-sheet with two helices flanking one side of the sheet and one helix flanking the other side and lacks all the necessary zinc ligand residues.
Pfam PF00114: Pilin (bacterial filament) (domain)
Proteins with only the short N-terminal methylation site are not separated from the noise.              The Prosite pattern detects those better.
Wikipedia: Pilin refers to a class of fibrous proteins that are found in pilus structures in bacteria. These structures can be used for the exchange of genetic material, or as a cell adhesion mechanism. Although not all bacteria have pili or fimbriae, bacterial pathogens often use their fimbriae to attach to host cells. In Gram-negative bacteria, where pili are more common, individual pilin molecules are linked by noncovalent protein-protein interactions, while Gram-positive bacteria often have polymerized LPXTG pilin.
Pfam PF23548: FORGETTER1 second zinc ribbon domain (domain)
This domain is found in the Arabidopsis FORGETTER1 and related proteins (FGT1). FGT1 mediates stress-induced chromatin memory by modulating nucleosome occupancy. This protein interacts with chromatin remodelers of the SWI/SNF and ISWI families, which also display reduced heat stress memory. The domain represented by this entry is predicted to adopt a zinc ribbon fold and it is the second of the predicted pair of two.
Pfam PF11076: Putative inner membrane protein YbhQ (family)
This family is conserved in Proteobacteria. The function is not known but most members are annotated as being inner membrane protein YbhQ.
Pfam PF00781: Diacylglycerol kinase catalytic domain (family)
Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologues. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.
Wikipedia: Diacylglycerol kinase is a family of enzymes that catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA), utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low, allowing DAG to be used for glycerophospholipid biosynthesis, but on receptor activation of the phosphoinositide pathway, DGK activity increases, driving the conversion of DAG to PA. As both lipids are thought to function as bioactive lipid signaling molecules with distinct cellular targets, DGK therefore occupies an important position, effectively serving as a switch by terminating the signalling of one lipid while simultaneously activating signalling by another.
Pfam PF07701: Heme NO binding associated (domain)
The HNOBA domain is found associated with the HNOB domain and [pfam:PF00211] in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce  diverse downstream signals, in both bacteria and animals.
Pfam PF03482: sic protein repeat (repeat)
Serotype M1 group A Streptococcus strains cause epidemic waves of human infections. This 30 aa repeat occurs in the sic protein, an extracellular  protein (streptococcal inhibitor of complement) that inhibits human complement.
Pfam PF03836: RasGAP C-terminus (family)
This domain can be found in the C terminus of the IQGAP family members, including human IQGAP1/2/3, S. cerevisiae Iqg1 and  S. pombe  Rng2. Some members function in cytoskeletal  remodelling. Human IQGAP1 is a scaffolding protein that can  assemble multi-protein complexes involved in cell-cell interaction, cell adherence, and movement via actin/tubulin-based cytoskeletal reorganization. IQGAP1 is also a regulator of the MAPK and Wnt/beta-catenin signaling pathways.Iqg1 and Rng2 are required for actomyosin ring construction during cytokinesis.
Pfam PF06848: Disaggregatase related repeat domain (domain)
This family consists of several repeats which seem to be specific to the Methanosarcina archaea species and are often found in multiple copies in disaggregatase proteins. Members of this family are also found in single copies in several hypothetical proteins.  This repeat is also known as DNRLRE repeat and is predicted form a mainly beta-strand structure with two alpha-helices. It is found in some cell surface proteins. It is predicted to adopt a nucleoplasmin fold.
Pfam PF02672: CP12 domain (family)
The function of this domain is unknown, it does contain three conserved cysteines and a histidine, that suggests this may be a zinc binding domain (Bateman A pers. observation). This domain is found associated with CBS domains in some proteins [pfam:PF00571].
Pfam PF10280: Mediator complex protein (family)
Mediator is a large, modular protein complex that is conserved from yeast to human and conveys regulatory signals from DNA-binding transcription factors to RNA polymerase II. Not only are the polypeptides conserved but the structural organisation is also largely conserved. One or two subunits are either fungal or vertebral specific but Med11 is one of the subunits that is conserved from fungi to humans. Med11 appears to be necessary for the full and successful assembly of the core head sub-region.
Wikipedia: Mediator is a multiprotein complex that functions as a transcriptional coactivator in all eukaryotes. It was discovered in 1990 in the lab of Roger D. Kornberg, recipient of the 2006 Nobel Prize in Chemistry. Mediator complexes interact with transcription factors and RNA polymerase II. The main function of mediator complexes is to transmit signals from the transcription factors to the polymerase.
Pfam PF13533: Biotin-lipoyl like (domain)
This entry represents the biotin-lipoyl like domain found in some bacterial membrane fusion proteins, such as AaeA and MdtA. AaeA is part of the efflux AaeAB pump , while MdtA is part of the MdtABC tripartite complex that confers resistance against novobiocin and deoxycholate .

MFPs are a component of the RND family of transporters (RND refers to resistance, nodulation, and cell division). MFPs are proposed to span the periplasm in some way linking the inner and outer membranes . However, some members of this family are found in Gram-positive bacteria, where there is no outer membrane. MFPs are involved in the export of a variety of compounds, from drug molecules to large polypeptides, and are united by their similar overall structural organisation, combined with some conserved regions .
Wikipedia: Biotin/lipoyl attachment domain has a conserved lysine residue that binds biotin or lipoic acid. Biotin plays a catalytic role in some carboxyl transfer reactions and is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme. Lipoamide acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via an amide linkage to a lysine group. The lipoic acid cofactor is found in a variety of proteins.
Pfam PF16105: Domain of unknown function (DUF4823) (family)
This family consists of hypothetical lipoproteins around 210 residues of length and is mainly found in various Pseudomonas species. The function of this family is unknown.
Pfam PF00331: Glycosyl hydrolase family 10 (domain)
O-Glycosyl hydrolases (3.2.1.) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families . This classification is available on the CAZy (CArbohydrate-Active EnZymes) website.
Glycoside hydrolase family 10 GH10 comprises enzymes with a number of known activities; xylanase (3.2.1.8); endo-1,3-beta-xylanase (3.2.1.32); cellobiohydrolase (3.2.1.91). These enzymes were formerly known as cellulase family F.

The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases (3.2.1.4), cellobiohydrolases (3.2.1.91) (exoglucanases), or xylanases (3.2.1.8) . Fungi and bacteria produces a spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be classified into families. One of these families is known as the cellulase family F  or as the glycosyl hydrolases family 10 .
The overall structure of the GH10 domain corresponds to an eightfold Î±/Î²-barrel (TIM-barrel) with a typical deep groove in the centre, allowing an 'endo' type of action on the large polysaccharide backbone .
Wikipedia: In molecular biology, Glycoside hydrolase family 10 is a family of glycoside hydrolases.
Pfam PF19023: Family of unknown function (DUF5749) (family)
The function of this family of euryarchaeal proteins is unknown. The structure of this protein forms a beta barrel.
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 PF15489: CST, telomere maintenance, complex subunit CTC1 (family)
CTC1 is one of the three components of the CST complex that assists Shelterin to protect the ends of telomeres from attack by DNA-repair mechanisms. Mutations in human CTC1 have been recognised as contributing to cerebroretinal microangiopathy.
Pfam PF00498: FHA domain (family)
The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Wikipedia: In molecular biology, the forkhead-associated domain is a phosphopeptide recognition domain found in many regulatory proteins. It displays specificity for phosphothreonine-containing epitopes but will also recognise phosphotyrosine with relatively high affinity. It spans approximately 80-100 amino acid residues folded into an 11-stranded beta sandwich, which sometimes contains small helical insertions between the loops connecting the strands.
Pfam PF03714: Bacterial pullanase-associated domain (domain)
Domain is found in pullanase - carbohydrate de-branching - proteins. It is found both to the N or the C terminii of of the alpha-amylase active site region. This domain contains several conserved aromatic residues that are suggestive of a carbohydrate binding function.
Pfam PF21425: Distal tail protein pb9, A domain, N-terminal (domain)
This entry includes phage distal tail proteins which form a hexameric ring located at the tail tube end, such as pb9 from bacteriophage T5. pb9 consists of two domains, A and B. Domain A adopts a split barrel  fold and includes residues 1 to 82-172 to 205. This entry covers the N-terminal region of the A domain. The C-terminal segment of the A domain is represented in [pfam:PF21424].
Pfam PF00980: Rotavirus major capsid protein VP6 (family)
Rotaviruses consist of three concentric protein shells.  The intermediate (middle) protein layer consists 260 trimers of VP6. VP6 in the most  abundant protein in the virion.  VP6 is also involved in virion assembly, and possesses the ability to interact with VP2, VP4 and VP7.
Pfam PF09962: Uncharacterized conserved protein (DUF2196) (family)
This domain, found in various hypothetical bacterial 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 PF17113: Regulatory signalling modulator protein AmpE (family)
AmpE is a family of bacterial regulatory proteins. AmpE in conjunction with AmpD sense the effect of beta-lactam on peptidoglycan synthesis and relay this signal to AmpR. AmpR regulates the production of beta-lactamase.
Pfam PF18033: SpuA C-terminal (domain)
This is the C-terminal beta sandwich domain found in Streptococcus pneumoniae Spu4 proteins. Spu4 is a large multimodular cell wall-attached enzyme involved in the degradation of glycogen.
Pfam PF10692: Protein of unknown function (DUF2498) (family)
Members of this family are Gammaproteobacteria. Many are annotated as like E coli protein YciN. The function is not known.
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 PF23842: Phage tail termination protein (domain)
This entry represents the phage tail termination protein found in a variety of tailed phages that infect Enterobacter. These proteins form a hexameric ring that caps the tail tube at the neck of these bacteriophage.
Pfam PF07247: Alcohol acetyltransferase (family)
This family contains a number of alcohol acetyltransferase ([ec:2.3.1.84]) enzymes approximately 500 residues long found in both bacteria and metazoa. These catalyse the esterification of isoamyl alcohol by acetyl coenzyme A.
Pfam PF21096: RecA C-terminal domain (domain)
This entry represents a small domain found at the C-terminus of RecA. The recA gene product is a multifunctional enzyme that plays a role in homologous recombination, DNA repair and induction of the SOS response This domain adopts a structure composed of a beta hairpin and three alpha helices. It has been shown to bind to dsDNA.
Pfam PF19795: Family of unknown function (DUF6279) (family)
This family of proteins, found in bacteria, is functionally uncharacterised. Proteins in this family are typically between 280 and 295 amino acids in length. There is a conserved WHxxxxLP sequence motif and a conserved Q residue.
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 PF24038: Domain of unknown function (DUF7347) (domain)
This is a presumed HTH domain found at the N-terminal of a group of uncharacterised archaeal sequences.
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 PF14417: MEDS: MEthanogen/methylotroph, DcmR Sensory domain (domain)
MEDS is prototyped by DcmR and is likely to function with the PocR domain in certain organisms in sensing hydrocarbon derivatives The MEDS domain occurs fused to Histidine Kinase and as stand-alone version. Sequence analysis shows that it is a catalytically  inactive version of the P-loop NTPase domain of the RecA superfamily.
Pfam PF08637: ATP synthase regulation protein NCA2 (family)
NCA2 has been shown to be required for the expression of ATP synthase subunits Atp6p and Atp8p in Saccharomyces cerevisiae.
Pfam PF11510: Fanconi Anaemia group E protein FANCE (repeat)
Fanconi Anaemia (FA) is a cancer predisposition disorder. In response to DNA damage, the FA core complex monoubiquitinates the downatream FANCD2 protein. The protein FANCE has an important role in DNA repair as it is the FANCD2-binding protein in the FA core complex so it represents the link between the FA core complex and FANCD2. The sequence shown is the C terminal domain of the protein which consists predominantly of helices and does not contain any beta-strand. The fold of the polypeptide is a continuous right-handed solenoidal pattern from the N terminal to the C terminal end.
Pfam PF24926: ACT domain-containing protein ACR9, C-terminal (domain)
This ACT domain is found at the C-terminal end of ACT domain -containing protein ACR9 from from Arabidopsis thaliana and similar plant proteins. ACR9 may bind amino acids.
Pfam PF08673: Phosphoserine phosphatase RsbU, N-terminal domain (domain)
RsbU is a phosphoserine phosphatase which acts as a positive regulator of the general stress-response factor of gram positive organisms, sigma-B.  The phosphatase activity of RsbU is stimulated by association with the RsbT kinase.  Deletions in the N terminal domain are deleterious to the activity of RsbU.
Pfam PF01465: GRIP domain (family)
The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.
Wikipedia: In molecular biology, the GRIP domain is a conserved protein domain. The GRIP domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. It contains a completely conserved tyrosine residue.