SII-SWORD/CoKE huggingface dataset:
Pfam PF15112: Domain of unknown function (DUF4559) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in eukaryotes. This family includes human protein CXorf38.
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 PF01740: STAS domain (domain)
The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.
Pfam PF15183: Melanocortin-2 receptor accessory protein family (family)
This family is thought to be involved in cell trafficking. It is required for MC2R expression in certain cell types, suggesting that it is involved in the processing, trafficking or function of MC2R. MRAP may be involved in the intracellular trafficking pathways in adipocyte cells. This family of proteins is found in eukaryotes. Proteins in this family are typically between 47 and 205 amino acids in length.
Pfam PF24377: Family of unknown function (DUF7533) (family)
This family includes a group of proteins from archaea. Members are predicted to adopt an alpha-helical structure.
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 PF04962: KduI/IolB family (domain)
This family includes the 5-keto 4-deoxyuronate isomerase enzyme [ec:5.3.1.17] that is involved in pectin degradation. This family aldo includes bacterial Myo-inositol catabolism (IolB) proteins. The Bacillus subtilis inositol operon (iolABCDEFGHIJ) is involved in myo-inositol catabolism. Glucose repression of the iol operon induced by inositol is exerted through catabolite repression mediated by CcpA and the iol induction system mediated by IolR. The exact function of IolB is unknown. Members of this family possess a Cupin like structure.
Wikipedia: In molecular biology, the KduI/IolB isomerase family is a family of isomerase enzymes that includes 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase (KduI) and 5-deoxy-glucuronate isomerase (IolB).
Pfam PF09106: Elongation factor SelB, winged helix (domain)
Members of this family adopt a winged-helix fold, with an alpha/beta structure consisting of three alpha-helices and a twisted three-stranded antiparallel beta-sheet, with an alpha-beta-alpha-alpha-beta-beta connectivity. They are involved in both DNA and RNA binding.
Pfam PF22042: Elongation factor G domain 2 (domain)
Elongation factor G (EF-G) catalyzes the translocation step of translation. It consists of five structural domains, this entry represents the second domain. This domain adopts a beta barrel structure. This family also includes domains found in other translation factors such as translation initiation factor IF-2, peptide chain release factor, etc.
Pfam PF23428: Domain of unknown function (DUF7115) (domain)
This domain is found twice in HVO_2519 from Haloferax volcanii ([swissprot:D4GTV1]) and similar proteins mainly from halobacteria. It has several conserved motifs RTxxYR, Y/FxHxxxR an RRK. It is predicted to show an alpha-beta configuration.
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 PF18755: Restriction Enzyme Adenine Methylase Associated (domain)
An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.
Pfam PF21418: Lincosamide nucleotidyltransferase-like, C-terminal domain (domain)
This domain is found at the C-terminal end of Lincosamide nucleotidyltransferase from Enterococcus faecium (LinB) and similar proteins from bacteria. LinB catalyses adenylylation of the lincosamide class of antibiotics. This domain folds into an alpha-helical bundle, which consists of five alpha-helices.
Pfam PF18950: Family of unknown function (DUF5694) (family)
This is a family of unknown function, mostly found in bacteria.
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 PF21251: Small ribosomal subunit protein uS5m, N-terminal (domain)
This entry represents an extension found at the N-terminal of the mitochondrial 28S Small ribosomal subunit protein uS5m. This region lines a part of the mRNA entry path and connects the 28S subunit body to the head forming a latch across the mRNA channel entrance.
Pfam PF08975: Domain of unknown function (DUF1868) (domain)
This group of 2H-phosphodiesterases comprises a single family typified by the protein mlr3352 from M.loti. Members are also present in various alpha-proteobacteria, Synechocystis, Streptococcus and Chilo iridescent virus. The presence of a member of this predominantly bacterial group in a large eukaryotic DNA virus represents a potential case of horizontal transfer from a bacterial source into a virus. Several proteins of bacterial origin have been noticed in the insect viruses (L.M.Iyer, E.V.Koonin and L.Aravind, unpublished observations and these appear to have been acquired from endo-symbiotic or parasitic bacteria that share the same host cells with the viruses. Presence of 2H proteins in the proteomes of large DNA viruses (e.g. T4 57B protein and the Fowl-pox virus FPV025) may point to some role for these proteins in regulating the viral tRNA metabolism. Each member of this family contains an internal duplication, each of which contains an HXTX motif that defines the family.
Pfam PF23524: MGAT4A C-terminal domain (domain)
This domain is found C-terminal in N-acetylglucosaminyltransferase IVa (MGAT4A) and related proteins. MGAT4A catalyses the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. This domain selectively interacts with the product N-glycans having a beta1-4 GlcNAc branch. Mutation of the residue critical for the sugar recognition impairs the enzymatic activity, suggesting that the lectin domain is a regulatory subunit for efficient catalytic reaction. This domain adopt a beta-sandwich fold typical for galactose binding domains.
Pfam PF06892: Phage regulatory protein CII (CP76) (family)
This family consists of several phage regulatory protein CII (CP76) sequences which are thought to be DNA binding proteins which are involved in the establishment of lysogeny.
Pfam PF19599: Family of unknown function (DUF6104) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are approximately 60 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 PF09710: Treponema clustered lipoprotein (Trep_dent_lipo) (family)
This entry represents a family of six predicted lipoproteins from a region of about 20 tandemly arranged genes in the Treponema denticola genome. Two other neighbouring genes share the lipoprotein signal peptide region but do not show more extensive homology. The function of this locus is unknown.
Pfam PF04277: Oxaloacetate decarboxylase, gamma chain (family)
This family comprises distantly related, low complexity, hydrophobic small subunits of several related sodium ion-pumping decarboxylases. These include oxaloacetate decarboxylase gamma subunit and methylmalonyl-CoA decarboxylase delta subunit .
Wikipedia: Oxaloacetate decarboxylase is a carboxy-lyase involved in the conversion of oxaloacetate into pyruvate.
Pfam PF23184: CFAP43, WD40 domain (repeat)
This entry represents a WD40 domain found in CFAP43 protein from Trypanosoma brucei brucei and related sequences from Kinetoplastids. This protein is located between the doublet microtubules 5 and 6 and associated with the axoneme along the paraflagellar rod.
Pfam PF21869: Distal tail component, second carbohydrate binding domain (domain)
This domain is found in the distal tail component from Lactobacillus phage J-1 (Dit), which is involved in host recognition. This entry represents the second putative carbohydrate binding domain (CBM2). It folds into a beta-sandwich with two beta-sheets gathering 12 beta-strands. This domain usually appears associated to [pfam:PF05709].
Pfam PF04722: Ssu72-like protein (family)
The highly conserved and essential protein Ssu72 has intrinsic phosphatase activity and plays an essential role in the transcription cycle. Ssu72 was originally identified in a yeast genetic screen as enhancer of a defect caused by a mutation in the transcription initiation factor TFIIB.  It binds to TFIIB and is also involved in mRNA elongation.  Ssu72 is further involved in both poly(A) dependent and independent termination. It is a subunit of the yeast cleavage and polyadenylation factor (CPF), which is part of the machinery for mRNA 3'-end formation. Ssu72 is also essential for transcription termination of snRNAs.
Pfam PF05716: A-kinase anchor protein 110 kDa (AKAP 110) (family)
This family consists of several mammalian protein kinase A anchoring protein 3 (PRKA3) or A-kinase anchor protein 110 kDa (AKAP 110) sequences. Agents that increase intracellular cAMP are potent stimulators of sperm motility. Anchoring inhibitor peptides, designed to disrupt the interaction of the cAMP-dependent protein kinase A (PKA) with A kinase-anchoring proteins (AKAPs), are potent inhibitors of sperm motility. PKA anchoring is a key biochemical mechanism controlling motility. AKAP110 shares compartments with both RI and RII isoforms of PKA and may function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction.
Pfam PF03606: C4-dicarboxylate anaerobic carrier (family)
Escherichia coli contains four different secondary carriers (DcuA, DcuB, DcuC, and DctA) for C4-dicarboxylates  DcuA is used for aerobic growth on C4-dicarboxylates , whereas the Dcu carriers (encoded by the dcuA, dcuB, and dcuC genes) are used under anaerobic conditions and form a distinct family of carriers . Each of the Dcu carriers is able to catalyze the uptake, antiport, and possibly also efflux of C4-dicarboxylates. DcuB is the major C4-dicarboxylate carrier for fumarate respiration with high fumarate-succinate exchange activity. It is synthesized only in the absence of oxygen and nitrate and in the presence of C4-dicarboxylates . DcuA is expressed constitutively in aerobic and anaerobic growth and can substitute for DcuB . These proteins are members of the C4-dicarboxylate Uptake C (DcuC) family. DcuC has 12 GES predicted transmembrane regions, is induced only under anaerobic conditions, and is not repressed by glucose. DcuC may therefore function as a succinate efflux system during anaerobic glucose fermentation. However, when overexpressed, it can replace either DcuA or DcuB in catalyzing fumarate-succinate exchange and fumarate uptake . DcuC shows the same transport modes as DcuA and DcuB (exchange, uptake, and presumably efflux of C4-dicarboxylates) .
Wikipedia: The C4-dicarboxylate uptake C family or DcuC family (TC# 2.A.61) is a family of transmembrane ion transporters found in bacteria. A representative list of proteins belonging to the DcuC family can be found in the Transporter Classification Database.
Pfam PF22694: Activating protease CtpB N-terminal domain (domain)
This domain is found N-terminal in Carboxy-terminal processing protease CtpB and related proteins. This enzyme is involved in signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. This domain contains auto-cleavage site at which it is proteolytically cleaved. The remaining part in the mature enzyme is involved in dimerisation.
Pfam PF20605: Antitoxin-like ribbon-helix-helix (domain)
This presumed domain is found in bacteria, and is approximately 60 amino acids in length. Structure prediction suggests that it has a ribbon-helix-helix motif, a DNA-binding motif commonly found in antitoxin families. Members containing this domain may be related to CopG antitoxin family.
Pfam PF20835: Anthrax protective antigen, immunoglobulin-like domain (domain)
Anthrax protective antigen (PA) is one of the three proteins forming the anthrax toxin. It is involved in the first step of toxin entry into host cells, enabling lethal factor (LF) and oedema factor (EF) to cross to the cytosol. PA undergoes cleavage by Furin to generate PA20 and PA63. The latter, which adopts a ring-shaped heptameric assembly, shows four distinct domains. The fourth domain, a carboxy- terminal receptor-binding domain, shows an initial hairpin and helix, followed by a beta-sandwich with an immunoglobulin-like fold (this entry).
Wikipedia: The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, consisting of about 125 amino acids.
Pfam PF22195: CFP-like, C-terminal thrombospondin type 1 domain (domain)
This domain is found at the C-terminal end of human Properdin (CFP, for Complement factor P) and similar animal proteins. CFP is a positive regulator of the alternate pathway (AP) of complement. It contains six thrombospondin repeat type I (TSP 1-6 domains and an N-terminal domain ([pfam:PF18487]). This entry represents the last TSP type I domain, which binds to the first TSP type I domain ([pfam:PF00090]), contributing to multimerisation.
Pfam PF23477: Probable treble clef zinc finger (domain)
This presumed domain is found in a number of uncharacterised proteins from bacteria and archaea. This domain is predicted to adopt a treble clef fold. In some members this domain follows ([pfam:PF13451]) which is also predicted to adopt treble clef fold.
Pfam PF00513: Late Protein L2 (family)
This family includes the L2 minor capsid protein, a late protein from Human papillomavirus (HPV). HPV are dsDNA viruses with no RNA stage in their replication cycle. Their dsDNA is contained within a capsid composed of 72 L1 capsomers and about 36 L2 minor capsid proteins. L2 minor capsid proteins enter the nucleus twice during infection: in the initial phase after virion disassembly, and in the productive phase when it assembles into replicated virions along with L1 major capsid proteins. L2 proteins contain two nuclear localisation signals (NLSs), one at the N-terminal (nNLS) and the other at the C-terminal (cNLS). L2 uses its NLSs to interact with a network of karyopherins in order to enter the nucleus via several import pathways. L2 from HPV types 11 and 16 was shown to interact with karyopherins Kapbeta(2) and Kapbeta(3) . L2 capsid proteins can also interact with viral dsDNA, facilitating its release from the endocytic compartment after viral uncoating.
Wikipedia: A late protein is a viral protein that is formed after replication of the virus. One example is VP4 from simian virus 40 (SV40).
Pfam PF10908: Tlde1 domain (domain)
This domain is found in Tlde1 family of antibacterial effectors secreted by the type VI secretion system (T6SS). Tlde1 family is evolutionarily related to l,d transpeptidases which form mDAP3-mDAP3 peptidoglycan crosslinks. Tlde1 family is widespread among Proteobacteria and is divided into three subfamilies (Tlde1a, Tlde1b and Tlde1c).
Pfam PF00365: Phosphofructokinase (domain)
The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes . One enzyme that utilises this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway . PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains), and as an octomer in yeast (where there are 4 alpha- (PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 similar domains ). PFK is ~300 amino acids in length, and structural studies of the bacterial enzyme have shown it comprises two similar (Î±/Î²) lobes: one involved in ATP binding and the other housing both the substrate-binding site and the allosteric site (a regulatory binding site distinct from the active site, but that affects enzyme activity). The identical tetramer subunits adopt 2 different conformations: in a 'closed' state, the bound magnesium ion bridges the phosphoryl groups of the enzyme products (ADP and fructose-1,6-bisphosphate); and in an 'open' state, the magnesium ion binds only the ADP , as the 2 products are now further apart. These conformations are thought to be successive stages of a reaction pathway that requires subunit closure to bring the 2 molecules sufficiently close to react .

Deficiency in PFK leads to glycogenosis type VII (Tarui's disease), an autosomal recessive disorder characterised by severe nausea, vomiting, muscle cramps and myoglobinuria in response to bursts of intense or vigorous exercise . Sufferers are usually able to lead a reasonably ordinary life by learning to adjust activity levels .
Wikipedia: Phosphofructokinase (PFK) is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis.
Pfam PF11768: WD repeat-containing and planar cell polarity effector protein Fritz (repeat)
Fritz is a probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis  and collective cell movements. In Drosophila melanogaster, fritz  regulates both the location and the number of wing cell  prehair initiation sites.
Pfam PF20124: Family of unknown function (DUF6514) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are approximately 90 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 PF06404: Phytosulfokine precursor protein (PSK) (family)
This family consists of several plant specific phytosulfokine precursor proteins. Phytosulfokines, are active as either a pentapeptide or a C-terminally truncated tetrapeptide. These compounds were first isolated because of their ability to stimulate cell division in somatic embryo cultures of Asparagus officinalis.
Pfam PF10753: Toxin GhoT_OrtT (family)
GhoT is part of the GhoT-GhoS type V toxin-antitoxin (TA) system. OrtT is homologous to GhoT, but it is not part of a TA pair. In this case, it acts as an independent  toxin to reduce growth during stress related to amino acid and DNA synthesis.
Pfam PF24328: Domain of unknown function (DUF7498) (domain)
This domain is found in a group of uncharacterised eukaryotic proteins. It contains two highly conserved cysteines. This domain is predicted to fold into Ig-like beta-sandwich.
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 PF04851: Type III restriction enzyme, res subunit (family)
This entry represents a domain found in the N terminus of several proteins, including helicases, the R subunit (HsdR) of type I restriction endonucleases (3.1.21.3), the Res subunit of type III endonucleases (3.1.21.5), and the B subunit of the UvrABC system (UvrB) .
Pfam PF18843: Large polyvalent protein associated domain 28 (domain)
This is a beta strand rich domain that lacks strongly conserved polar residues. It is fast diverging and is found in polyvalent proteins of conjugative elements.
Pfam PF24062: Domain of unknown function (DUF7362) (domain)
This entry represents a domain of unknown function found at the N-terminal of CHAT domain-containing, such as SwissProt:A0A100JVW6, protein from Streptomyces scabiei. This domain may be found in association with TCAD7 ([pfam:PF19973]) and CHAT ([pfam:PF12770]) 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 PF05902: 4.1 protein C-terminal domain (CTD) (domain)
At the C-terminus of all known 4.1 proteins is a sequence domain unique to these proteins, known as the C-terminal domain (CTD). Mammalian CTDs are associated with a growing number of protein-protein interactions, although  such activities have yet to be associated with invertebrate CTDs. Mammalian CTDs are generally defined by sequence alignment as encoded by exons 18-21. Comparison of known vertebrate 4.1 proteins with invertebrate 4.1 proteins indicates that mammalian 4.1 exon 19 represents a vertebrate adaptation that extends the sequence of the CTD with a Ser/Thr-rich sequence. The CTD was first described as a 22/24-kDa domain by chymotryptic digestion of erythrocyte 4.1 (4.1R). CTD is thought to represent an independent folding structure which has gained function since the divergence of vertebrates from invertebrates.
Pfam PF06969: HemN C-terminal domain (domain)
Members of this family are all oxygen-independent coproporphyrinogen-III oxidases (HemN). This enzyme catalyses the oxygen-independent conversion of coproporphyrinogen-III to protoporphyrinogen-IX, one of the last steps in haem biosynthesis. The function of this domain is unclear, but comparison to other proteins containing a radical SAM domain ([pfam:PF04055]) suggest it may be a substrate binding domain.