SII-SWORD/CoKE huggingface dataset:
Pfam PF24226: Phage membrane protein Family of unknown function (DUF7442) (family)
This entry represents a family of putative membrane proteins found in various bacteriophages. The proteins in this family typically contain two transmembrane helices. The function of these proteins is currently unknown. They are predominantly found in phages infecting Salmonella, Escherichia, and other enterobacteria. The proteins in this family are generally short, with most members being around 80-81 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 PF15057: Domain of unknown function (DUF4537) (domain)
The function of this domain family is unknown. It is found in eukaryotes, and is typically between 119 and 141 amino acids in length. In humans, it is found in the chromosomal position C11orf16.
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 PF10998: Protein of unknown function (DUF2838) (family)
This bacterial 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 PF05788: Orbivirus RNA-dependent RNA polymerase (VP1) (family)
This family consists of the RNA-dependent RNA polymerase protein VP1 from the Orbiviruses. VP1 may have both enzymatic and structural roles in the virus life cycle.
Pfam PF23108: Two consecutive Zinc fingers C2H2 type, ZNF451 (domain)
This entry represents a domain consisting of two consecutive zinc fingers (of the C2H2 type), whose 4 beta-strands are arranged antiparallelly in a beta-sheet. This domain is found in the ZNF451 proteins. E3 SUMO-protein ligase ZNF451 is a key enzyme involved in the sumoylation process, exhibiting a preference for SUMO2 and SUMO3 over SUMO1. It facilitates the UBE2I/UBC9-mediated sumoylation of target proteins, particularly in response to DNA damage and proteasome inhibitors. ZNF451 is essential for MCM4 sumoylation,  and it negatively regulates transcriptional activation mediated by the SMAD4 complex in the context of TGF-beta signaling. Additionally, it inhibits EP300-mediated acetylation of histone H3 at 'Lys-9'.
Pfam PF03658: RnfH family Ubiquitin (domain)
A member of the RnfH family of the ubiquitin superfamily. Members of this family strongly co-occur in two distinct gene neighborhood  contexts. In one it is associated with a START domain protein, a  membrane protein SmpA and the transfer mRNA binding protein SmpB.  This association suggests a possible role in the SmpB-tmRNA-based  tagging and degadation system of bacteria, which is interesting given that other members of the ubiquitin system are analogously involved  in protein-tagging and degradation across eukaryotes and various  prokaryotes. The second context in which the RnfH genes are present  is in a membrane associated complex involved in transporting  electrons for various reductive reactions such as nitrogen  fixation.
Pfam PF17218: CBX family C-terminal motif (conserved_site)
This motif is found at the C-terminus of CBX family proteins. It is bound by the RAWUL domain of the RING1B protein.
Pfam PF13748: ABC transporter transmembrane region (family)
This family represents a unit of six transmembrane helices.
Wikipedia: ABC transporter transmembrane domain is the main transmembrane structural unit of ATP-binding cassette transporter proteins, consisting of six alpha helixes that traverse the plasma membrane. Many members of the ABC transporter family have two such regions.
Pfam PF21448: Deoxynucleotide monophosphate kinase (domain)
This entry includes Deoxynucleotide monophosphate kinases from phages which act on dGMP, dTMP and 5-hydroxymethyl-dCMP while excluding dCMP and dAMP.
Pfam PF03263: Cucumovirus protein 2B (family)
This protein may be a viral movement protein.
Pfam PF25038: Csf1 family C-terminal region (repeat)
This entry includes Csf1 protein from yeast, which is the orthologue of human BLTP1. Csf1 also known as Cold sensitive for fermentation protein 1 is a fungal membrane protein required for fermentation at low temperature. Csf1, similar to BLTP1, is a tube-forming lipid transport protein which provides phosphatidylethanolamine for glycosylphosphatidylinositol (GPI) anchor synthesis in the endoplasmic reticulum. These proteins belong to the repeating beta-groove (RBG) superfamily which are conserved lipid transfer proteins containing long hydrophobic grooves consisting of multiple repeating modules made of five beta-sheets followed by a loop.
Pfam PF01469: Pentapeptide repeats (8 copies) (repeat)
These repeats are found in many mycobacterial proteins.  These repeats are most common in the [pfam:PF00823] family of proteins, where they are found in the MPTR subfamily of PPE proteins. The function of these repeats is unknown. The repeat can be approximately described as XNXGX, where X can be any amino acid. These repeats are similar to [pfam:PF00805], however it is not clear if these two families are structurally related.
Pfam PF05466: Brain acid soluble protein 1 (BASP1 protein) (disordered)
This family consists of several brain acid soluble protein 1 (BASP1) or neuronal axonal membrane protein NAP-22. The BASP1 is a neuron enriched Ca(2+)-dependent calmodulin-binding protein of unknown function.
Pfam PF13178: Protein of unknown function (DUF4005) (family)
This is a C-terminal region of plant IQ-containing putative calmodulin-binding 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 PF21822: Phage tail assembly chaperone protein, TAC (family)
This is a family of phage tail assembly chaperone proteins.
Pfam PF10235: Microtubule-associated protein CRIPT (family)
The CRIPT protein is a cytoskeletal protein involved in microtubule production. The C-terminal domain is essential for binding to the PDZ3 domain of the SAP90 protein, one of a super-family of PDZ-containing proteins that play an important role in coupling the membrane ion channels with their signalling partners.  SAP90 is concentrated in the post synaptic density of glutamatergic neurons.
Pfam PF06269: Protein of unknown function (DUF1029) (family)
This family consists of several short Chordopoxvirus proteins of unknown 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 PF18544: Polo box domain (domain)
In metazoans, Plk4 kinases control daughter centriole assembly. Plk4 homologs have an N-terminal kinase domain, a C-terminal polo box, and a central domain termed the 'cryptic polo box' (CPB) that has been shown to dimerize, to be sufficient for centriole localization and to be required for Plk4 to promote centriole assembly. Probable serine/threonine-protein kinase zyg-1 ([ec:2.7.11.1]) (ZYG-1) is a Plk4 homlog found in C. elegans. Crystal structure for the CPB of C.  elegans ZYG-1, reveals that it forms a Z-shaped dimer containing an intermolecular beta-sheet with an extended basic surface patch. Electrostatic interactions between the basic patch on the ZYG-1 CPB dimer and the SPD-2 acidic region dock ZYG-1 onto centrioles to promote new centriole assembly. ZYG-1 CPB contains two tandem polo boxes (PB1 and PB2), each containing a six-stranded beta-sheet with an alpha-helix packed against one side. This entry represents PB2.
Pfam PF14998: Transcription Regulator (family)
The precise function of this family is not clear, but it is thought to play a role in somitogenesis, development and transcriptional repression. Ripply is also known by an alternative name, Bowline. Bowline, is an associate protein of the transcriptional co-repressor XGrg-4. This family contains two conserved sequence motifs: WRPW and FPVQATI. The WRPW motif is thought to be required for binding to tle/groucho proteins. Ripply3 is also known as Down Syndrome Critical Region Protein 6 homolog.  This family of proteins is found in eukaryotes. Proteins in this family are typically between 109 and 154 amino acids in length.
Pfam PF00345: Pili and flagellar-assembly chaperone, PapD N-terminal domain (domain)
C2 domain-like beta-sandwich fold. This domain is the n-terminal part of the PapD chaperone protein for pilus and flagellar assembly.
Pfam PF15714: Stage V sporulation protein T C-terminal, transcription factor (domain)
SpoVT_C is the C-terminal part of the stage V sporulation protein T, a transcription factor involved in endospore formation in Gram-positive bacteria such as Bacillus subtilis. Sporulation is induced by conditions of environmental stress to protect the genome. SpoVT behaves as a tetramer that shows an overall significant distortion mediated by electrostatic interactions. Two monomers dimerise via the highly charged N-terminal AbrB-like domains, family [pfam:PF04014], to form swapped-hairpin beta-barrels. These asymmetric dimers then form tetramers through the formation of mixed helix bundles between their C-terminal domains. The C-termini themselves fold as GAF (cGMP-specific and cGMP-stimulated phosphodiesterases, Anabaena adenylate cyclases, and Escherichia coli FhlA) domains.
Wikipedia: The GAF domain is a type of protein domain that is found in a wide range of proteins from all species. The GAF domain is named after some of the proteins it is found in: cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. The first structure of a GAF domain solved by Ho and colleagues showed that this domain shared a similar fold with the PAS domain. In mammals, GAF domains are found in five members of the cyclic nucleotide phosphodiesterase superfamily: PDE2, PDE5, and PDE6 which bind cGMP to the GAF domain, PDE10 which binds cAMP, and PDE11 which binds both cGMP and cAMP.
Pfam PF13549: ATP-grasp domain (domain)
This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pfam PF11566: PI31 proteasome regulator N-terminal (family)
PI31 is a regulatory subunit of the immuno-proteasome which is an inhibitor of the 20 S proteasome in vitro.PI31 is also an F-box protein Fbxo7.Skp1 binding partner which requires an N terminal FP domain in both proteins for the interaction to occur via the FP beta sheets. The structure of PI31 FP domain contains a novel alpha/beta-fold and two intermolecular contact surfaces. This is the N-terminal domain of the members.
Pfam PF22089: DIP2116-like, N-terminal domain (domain)
This domain is found at the N-terminal end of the putative membrane anchored protein DIP2116 from Corynebacterium diphtheriae ([swissprot:Q6NEZ3]). It shows an immunoglobulin-like fold.
Pfam PF01579: Domain of unknown function (DUF19) (domain)
This presumed domain has no known function. It is found in one or two copies in several Caenorhabditis elegans proteins.  It is roughly 130 amino acids long. The domain contains 12 conserved cysteines which suggests that the domain is an extracellular domain and that these cysteines form six intradomain disulphide bridges.  The GO annotation for this protein indicates that it has a function in nematode larval development and has a positive regulation of growth rate.
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 PF07741: Brf1-like TBP-binding domain (domain)
In budding yeasts, Brf1 forms the TFIIIB complex with TATA-binding protein (TBP) and Bdp1. The TFIIIB complex can be recruited to the Pol III promoters and form an exceptionally kinetically stable TFIIIB-DNA complex, which then recruits the Pol III enzymatic complex and helps maintain it for multiple transcription cycles in a process called facilitated recycling. This entry represents the TATA binding protein (TBP) binding domain of Brf1 that covers both the Brf homology II and III regions.
Pfam PF14664: Rapamycin-insensitive companion of mTOR, N-term (domain)
Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the N-terminal conserved section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin.
Pfam PF21038: Centrosomal protein CEP104, N-terminal domain (domain)
Centrosomal protein CEP104 localises to the distal end of centrioles that interacts through its N- and C-terminal region, respectively, with the distal end proteins Cep97 and CP110. It is required for ciliogenesis and for structural integrity at the ciliary tip, being involved in regulating microtubule length in cilia. This is a multidomain protein that consists of an N-terminal all-beta domain, a central all-alpha-helical HEAT repeat domain and a C-terminal array of four zinc fingers domain. This is the N-terminal all-beta domain of CEP104, which is structurally similar to domains of intraflagellar transport protein 25 (IFT25), DNA repair protein XRCC1 ([pfam:PF01834]) and anaphase-promoting complex APC subunit 10 and is implicated in Cep97 binding.
Pfam PF21117: MRB1590 C-terminal domain (domain)
This entry represents the C-terminal helix-turn-helix like domain from the T. brucei kRNA editing factor MRB1590.
Pfam PF17328: Family of unknown function (DUF5366) (family)
This is a family of unknown function, found in Bacillales. Members of the family are predicted to have between 4 and 5 trans-membrane regions.
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 PF00017: SH2 domain (domain)
The Src homology 2 (SH2) domain is a protein domain of about 100 amino-acid residues first identified as a conserved sequence region between the oncoproteins Src and Fps . Similar sequences were later found in many other intracellular signal-transducing proteins . SH2 domains function as regulatory modules of intracellular signalling cascades by interacting with high affinity to phosphotyrosine-containing target peptides in a sequence-specific, SH2 domains recognise between 3-6 residues C-terminal to the phosphorylated tyrosine in a fashion that differs from one SH2 domain to another, and strictly phosphorylation-dependent manner . They are found in a wide variety of protein contexts e.g., in association with catalytic domains of phospholipase Cy (PLCy) and the non-receptor protein tyrosine kinases; within structural proteins such as fodrin and tensin; and in a group of small adaptor molecules, i.e Crk and Nck. The domains are frequently found as repeats in a single protein sequence and will then often bind both mono- and di-phosphorylated substrates.

The structure of the SH2 domain belongs to the Î±+Î² class, its overall shape forming a compact flattened hemisphere. The core structural elements comprise a central hydrophobic anti-parallel Î²-sheet, flanked by 2 short Î±-helices. The loop between strands 2 and 3 provides many of the binding interactions with the phosphate group of its phosphopeptide ligand, and is hence designated the phosphate binding loop, the phosphorylated ligand binds perpendicular to the Î²-sheet and typically interacts with the phosphate binding loop and a hydrophobic binding pocket that interacts with a pY+3 side chain. The N- and C-termini of the domain are close together in space and on the opposite face from the phosphopeptide binding surface and it has been speculated that this has facilitated their integration into surface-exposed regions of host proteins .
Wikipedia: The SH2 domain is a structurally conserved protein domain contained within the Src oncoprotein and in many other intracellular signal-transducing proteins. SH2 domains bind to phosphorylated tyrosine residues on other proteins, modifying the function or activity of the SH2-containing protein. The SH2 domain may be considered the prototypical modular protein-protein interaction domain, allowing the transmission of signals controlling a variety of cellular functions. SH2 domains are especially common in adaptor proteins that aid in the signal transduction of receptor tyrosine kinase pathways.
Pfam PF02274: Arginine deiminase (family)
This family contains arginine deiminases, [ec:3.5.3.6]., enzymes that catalyse the reaction: arginine + H2O  citrulline + NH3. These enzymes belong to the amidinotranferase (AT) superfamily, which share the alpha/beta fold including structurally important residues, i.e buried hydrophobic residues, buried hydrophilic residues hydrogen-bonded with mainchain groups and a structural hallmark of three consecutive buried Gly residues near the C-terminus, conserved among these proteins.
Pfam PF10620: Phosphoribosyl-dephospho-CoA transferase MdcG C-terminal domain (domain)
This entry represents the C-terminal catalytic domain of MdcG, which is a phosphoribosyl-dephospho-CoA transferase that is involved in the biosynthesis of the prosthetic group of malonate decarboxylase.  Malonate decarboxylase from Klebsiella pneumoniae contains an acyl carrier protein (MdcC) to which a 2'-(5' '-phosphoribosyl)-3'-dephospho-CoA prosthetic group is attached via phosphodiester linkage. MdcG catalyses the following reaction: 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + apo-[acyl-carrier-protein] = holo-[acyl-carrier-protein] + diphosphate.
Pfam PF10852: Protein of unknown function (DUF2651) (family)
This family of proteins with unknown function appears to be restricted to Bacillus spp.
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 PF07785: Protein of unknown function (DUF1623) (family)
The members of this family are all derived from  relatively short hypothetical proteins thought to  be expressed by various Nucleopolyhedroviruses.
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 PF16154: Domain of unknown function (DUF4862) (family)
This family consists of uncharacterized proteins around 300 residues in length and is mainly found in various high GC Gram+ bacteria, but also in several pathogenic and non-pathogenic enterobacteria  (Salmonella, E. coli). Distant homology analysis suggests this could  be a branch of Xylose isomerase-like TIM barrel family, but this  prediction is currently not confirmed by experiment
Pfam PF18356: Domain of unknown function (DUF5608) (domain)
The structure of Q6ZYJ4, an uncharacterized protein from Pyrobaculum spherical virus, has been determined (2x4j) . This entry represent the C-terminal domain.
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 PF18662: Cch helix turn helix domain (domain)
Staphylococcal Cassette Chromosome, or SCC elements, are a family of genomic islands found in S. aureus and closely related species. SCC elements that carry the mecA gene are called SCCmec and render S. aureus methicillin-resistant, creating the MRSA strains. Cch, the self-loading helicase encoded by SCCmec type IV, belongs to the pre-sensor II insert clade of AAA+ ATPases, as do the archaeal and eukaryotic MCM-family replicative helicases. The N-terminal domain carries [pfam:PF06048]. The central domain (residues 157-438) contains an AAA+ ATPase fold. This domain is found at the C-terminal region, it is a winged helix-turn-helix (WH) domain typical of many dsDNA-binding proteins.
Pfam PF10055: Uncharacterized small protein (DUF2292) (family)
Members of this family of hypothetical bacterial 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 PF13680: Protein of unknown function (DUF4152) (domain)
This family of proteins is functionally uncharacterised. This family of proteins is found in archaea. Proteins in this family are approximately 230 amino acids in length. The structure of PF2046 from pyrococcus furiosus has been solved.  It shows an RNaseH like fold that conserves critical catalytic residues. This suggests that these proteins may cleave nucleic acid.