SII-SWORD/CoKE huggingface dataset:
Pfam PF23249: PARP14, third type I KH domain (domain)
This domain is found in human Protein mono-ADP- ribosyltransferase PARP14 and related proteins. PARP14 is a large multidomain protein which in the N-terminal half contains a series of consecutive RRM and KH domains that are known to be nucleic acid-binding. PARP14 is involved in multiple signaling pathways linked to cancer, inflammation, and infection. PARP14 is an ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate residues on target proteins. In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation. The domain represented by this entry is a KH domain found third in the human PARP14.
Pfam PF21945: Mitochondrial-derived peptide MOTS-c (family)
This protein family represents human Mitochondrial-derived peptide MOTS-c (MT-RNR1), a 16-residue peptide that regulates insulin sensitivity and metabolic homeostasis.
Pfam PF14759: Reductase C-terminal (domain)
This domain occurs at the C-terminus of various reductase enzymes, including putidaredoxin reductase, ferredoxin reductase, 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component, benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit, rhodocoxin reductase, biphenyl dioxygenase system ferredoxin--NAD(+) reductase component, rubredoxin-NAD(+) reductase and toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component. In putidaredoxin reductase this domain is involved in dimerisation. In the FAD-containing NADH-ferredoxin reductase (BphA4) it is responsible for interaction with the Rieske-type [2Fe-2S] ferredoxin (BphA3).
Pfam PF23969: Domain of unknown function (DUF7296) (domain)
This entry represents a family of domains found in phages that infect a variety of bacterial hosts including Streptococcus, Streptomyces, Pseudomonas and Paenibacillus species.  The Domain is typically around 110-130 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 PF10228: Histone PARylation factor 1 (family)
Histone PARylation factor 1 (HPF1, previously known as C4orf27) is a key regulator of ADP-ribosylation (ADPr) signaling in response to DNA damage. It forms a complex with PARP-1 (poly(ADP-ribose) polymerase 1), creating a composite active site. HPF1 is essential for Ser-ADPr (ADPr on serine residues), which represents the major fraction of ADPr synthesised after DNA damage. This protein is organised into two tightly-associated domains connected via an elaborate linker, showing an alpha-beta structure.
Pfam PF19947: Family of unknown function (DUF6409) (family)
This entry represents a member of a biosynthetic gene cluster (BGC). This BGC (BGC0000703) is described by MIBiG as an example of the following biosynthetic class, saccharide, in particular the kanamycin biosynthetic gene cluster from Streptomyces kanamyceticus.
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 PF03466: LysR substrate binding domain (family)
The structure of this domain is known and is similar to the periplasmic binding proteins. This domain binds a variety of ligands that caries in size and structure, such as amino acids, sugar phosphates, organic acids, metal cations, flavonoids, C6-ring carboxylic acids, H2O2, HOCl, homocysteine, NADPH, ATP, sulphate, muropeptides, acetate, salicylate, citrate, phenol- and quinolone derivatives, acetylserines, fatty acid CoA, shikimate, chorismate, homocysteine, indole-3-acetic acid, Na(I), c-di-GMP, ppGpp and hydrogen peroxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pfam PF10462: Peptidase M66 (family)
This family of metallopeptidases contains StcE, a virulence factor found in Shiga toxigenic Escherichia coli organisms. StcE peptidase cleaves C1 esterase inhibitor.
Pfam PF01169: Divalent cation/proton antiporter GDT1 (family)
This entry, previously known as UPF0016, represents the budding yeast Divalent cation/proton antiporter GDT1 and its homologue, the human TMEM165 that are functionally related and form a new group of Golgi-localised cation/Ca(2+) exchangers. Budding yeast GDT1 is a Golgi-localised calcium transporter required for stress-induced calcium signalling and protein glycosylation. TMEM165, also a Golgi protein, transports Ca2+ and Mn2+, which are both required for proper protein glycosylation in cells.  Most members of the family contain two copies of a region that contains an EXGD motif. Each of these regions contains three predicted transmembrane regions.
Pfam PF04872: Poxvirus L5 protein family (family)
This family includes variola (smallpox) and vaccinia virus L5 proteins. However, not all  proteins in this family are called L5.  L5 is thought to contain a  metal-binding region.
Pfam PF01222: Ergosterol biosynthesis ERG4/ERG24 family (family)
This entry represents a group of enzymes involved in the steroid biosynthetic pathway, including 7-dehydrocholesterol reductase and Delta(14)-sterol reductase LBR (lamin B receptor) from animals , Delta(14)-sterol reductase from fungi and plants  and Delta(24(24(1)))-sterol reductase from yeast . These proteins act by reducing double bonds in precursors of ergosterol, are highly hydrophobic and seem to contain seven or eight transmembrane regions.
Pfam PF14182: YgaB-like protein (coiled_coil)
The YgaB-like protein family includes the B. subtilis YgaB protein [swissprot:P71080], which is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are approximately 90 amino acids in length.
Pfam PF17051: Cytochrome C oxidase assembly factor 2 (family)
Coa2 is a cytochrome oxidase assembly factor required for efficient assembly of cytochrome c oxidase in the mitochondrial inner membrane. It may aid in stabilising an early Cox1 intermediate containing the nuclear subunits Cox5A and Cox6 .
Pfam PF10371: Domain of unknown function (domain)
EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) [pfam:PF01558] and the 4Fe-4S binding domain Fer4 [pfam:PF00037]. It contains a characteristic EKR sequence motif. The exact function of this domain is not known.
Pfam PF08611: Fungal protein of unknown function (DUF1774) (family)
This is a fungal family 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 PF12155: NADH dehydrogenase subunit 2 N-terminal (family)
This domain is found in eukaryotes, and is approximately 90 amino acids in length. It is found associated with [pfam:PF00361]. All members are annotated as being NADH dehydrogenase subunit 2, and this region is the N-terminus.
Pfam PF17295: Domain of unknown function (DUF5348) (domain)
This entry represents an uncharacterised domain found mostly in proteins from Firmicutes.
Pfam PF14981: FAM165 family (family)
This family of proteins known as FAM165 are found in eukaryotes. Members of this family are as yet uncharacterised. Proteins in this family are typically short membrane proteins between 55 and 70 amino acids in length.
Pfam PF21147: AMP-activated protein kinase, alpha subunit, autoinhibitory domain (domain)
This domain is found in the catalytic subunit (alpha) of the enzymatic complex AMP-activated protein kinase (AMPK). This protein is organised into an N-terminal kinase domain (KD, [pfam:PF00069]) and a regulatory C-terminus, which contains an autoinhibitory domain (AID, this entry). This domain can form a compact domain that stabilizes the KD and binds to CBS-2 of the gamma-subunit.
Pfam PF08744: Plant transcription factor NOZZLE (family)
NOZZLE is a transcription factor that plays a role in patterning the proximal-distal and adaxial-abaxial axes.
Pfam PF22897: TIL-like domain (domain)
The entry represents a small cysteine rich domain that is related to the Trypsin Inhibitor like cysteine rich domain found in [pfam:PF01826].
Pfam PF01149: Formamidopyrimidine-DNA glycosylase N-terminal domain (domain)
Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidised purines from damaged DNA. This family is the N-terminal domain contains eight beta-strands, forming a beta-sandwich with two alpha-helices parallel to its edges.
Pfam PF07379: Protein of unknown function (DUF1494) (family)
This family consists of several bacterial proteins of around 175 residues in length. Members of this family seem to be found exclusively in Chlamydia species. 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 PF06778: Chlorite dismutase (domain)
This family contains chlorite dismutase enzymes of bacterial and archaeal origin. This enzyme catalyses the disproportionation of chlorite into chloride and oxygen. Note that many family members are hypothetical proteins.
Pfam PF07719: Tetratricopeptide repeat (repeat)
This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by [pfam:PF00515].
Pfam PF03720: UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain (domain)
The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde  intermediate.
Pfam PF17641: Ancylostoma-associated secreted protein related (family)
This family includes members encoded by ASP-related genes which are distant homologs to ASPs (Ancylostoma-associated secreted proteins). ASPs are a diverse set of secreted cysteine-rich proteins [pfam:PF00188]. ASPRs, on the other hand are predicted to be secreted with one ASPR in Heligmosomoides bakeri shown to be secreted by parasitic adults. Thus, like ASPs, ASPRs are suggested to comprise an important element of hookworm infection in vivo.
Pfam PF23008: Tyrosine-protein kinase receptor torso, third FN3 domain (domain)
This domain is found in the Tyrosine-protein kinase receptor torso from Bombyx mori (Tor), which is involved in the initiation of metamorphosis during postembryonic development. This protein is organised into three consecutive fibronectin type III (FN3) domains and a C-terminal Kinase domain. This entry represents the third FN3 domain.
Pfam PF23748: LRRK2 beta propeller (repeat)
This entry represents the beta-propeller found at the C-terminal in Leucine-rich repeat serine/threonine-protein kinase 2 (LRRK2) from eukaryotes. LRRK2 is a serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, primary ciliogenesis, autophagy, and vesicle trafficking. Mutations in LRRK2 are the most common genetic cause of Parkinson's disease (PD).The beta-propeller domain is suggested to mediate LRRK2 dimerization and autophosphorylation, and plays an important role in neurotoxicity associated to LRRK2 PD mutations.
Pfam PF03288: Poxvirus D5 protein-like (domain)
This family includes D5 from Poxviruses which is necessary for viral DNA replication, and is a nucleic acid independent nucleoside triphosphatase. Members of this family are also found outside of poxviruses. This domain is a DNA-binding winged HTH domain.
Pfam PF20460: Family of unknown function (DUF6713) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are typically between 117 and 141 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 PF08751: TrwC relaxase (domain)
Relaxases are DNA strand transferases which function during the conjugative cell to cell DNA transfer.  TrwC binds to the origin of transfer (oriT) and melts the double helix.
Pfam PF01447: Thermolysin metallopeptidase, catalytic domain (domain)
Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation which is usually zinc, but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidases, two metal ions are observed in crystal structures ligated by five amino acids, with one amino acid ligating both metal ions. The known metal ligands are His, Glu, Asp or Lys. At least one other residue is required for catalysis, which may play an electrophillic role. Many metalloproteases contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site . The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases .
This group of metallopeptidases that belong to the MEROPS peptidase family M4 (thermolysin family, clan MA(E)). The protein fold of the peptidase domain of thermolysin (MEROPS identifier M04.001), is the type example for members of the clan MA. The thermolysin family is composed only of secreted eubacterial endopeptidases. The zinc-binding residues of thermolysin are H-142, H-146 and E-166, with E-143 acting as the catalytic residue. Thermolysin also contains four calcium-binding sites, which contribute to its unusual thermostability. The family also includes enzymes from a number of pathogens, including Legionella and Listeria, and the protein pseudolysin (MEROPS identifier M04.005), all with a substrate specificity for an aromatic residue in the P1' position. Three-dimensional structure analysis has shown that the enzymes undergo a hinge-bend motion during catalysis. Pseudolysin has a broader specificity, acting on large molecules such as elastin and collagen, possibly due to its wider active site cleft .
This entry represents a domain found in peptidase M4 family members.
Pfam PF20316: Family of unknown function (DUF6612) (domain)
This family of proteins is functionally uncharacterised. However, based on similarity to other families it is likely to be involved in lipoprotein biosynthesis. This family of proteins is found in bacteria. Proteins in this family are typically between 263 and 293 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 PF24196: Family of unknown function (DUF7421) (family)
This entry represents a small family of uncharacterised enterobacterial phage 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 PF00028: Cadherin domain (domain)
This entry represents the extracellular repeated domains found in cadherins and related proteins.
Cadherins are a group of transmembrane proteins that serve as the major adhesion molecules located within adherens junctions. They can regulate cell-cell adhesion through their extracellular domain and their cytosolic domains connect to the actin cytoskeleton by binding to catenins . These proteins preferentially interact with themselves in a homophilic manner in connecting cells; thus acting as both receptor and ligand. They may play an important role in the sorting of different cell types during morphogenesis, histogenesis and regeneration. They may also be involved in the regulation of tight and gap junctions, and in the control of intercellular spacing. Cadherins are evolutionary related to the desmogleins which are component of intercellular desmosome junctions involved in the interaction of plaque proteins.

Structurally, cadherins comprise a number of domains: classically, these include a signal sequence; a propeptide of around 130 residues; a single transmembrane domain and five tandemly repeated extracellular cadherin domains, 4 of which are cadherin repeats, and the fifth contains 4 conserved cysteines and a C-terminal cytoplasmic domain . However, proteins are designated as members of the broadly defined cadherin family if they have one or more cadherin repeats. A cadherin repeat is an independently folding sequence of approximately 110 amino acids that contains motifs with the conserved sequences DRE, DXNDNAPXF, and DXD. Crystal structures have revealed that multiple cadherin domains form Ca2+-dependent rod-like structures with a conserved Ca2+-binding pocket at the domain-domain interface. Cadherins depend on calcium for their function: calcium ions bind to specific residues in each cadherin repeat to ensure its proper folding, to confer rigidity upon the extracellular domain and is essential for cadherin adhesive function and for protection against protease digestion.
Wikipedia: Cadherins (named for "calcium-dependent adhesion") are cell adhesion molecules important in forming adherens junctions that let cells adhere to each other. Cadherins are a class of type-1 transmembrane proteins, and they depend on calcium (Ca2+) ions to function, hence their name. Cell-cell adhesion is mediated by extracellular cadherin domains, whereas the intracellular cytoplasmic tail associates with numerous adaptors and signaling proteins, collectively referred to as the cadherin adhesome.
Pfam PF18058: SbsC C-terminal domain (domain)
This is the C-terminal domain found in Bacterial Cell Surface Layer Protein SbsC which can be found in species such as Geobacillus stearothermophilus. The C-terminal domain is the third and last triple-helical bundle and adopts a canonical coiled-coil structure. A similar overall arrangement of antiparallel triple-helical bundles has been found in the cytoskeletal protein spectrin (2SPC).
Pfam PF08501: Shikimate dehydrogenase substrate binding domain (domain)
This domain is the substrate binding domain of shikimate dehydrogenase.
Wikipedia: In enzymology, a shikimate dehydrogenase (EC 1.1.1.25) is an enzyme that catalyzes the chemical reactionshikimate + NADP+  3-dehydroshikimate + NADPH + H+
Pfam PF04224: Protein of unknown function, DUF417 (family)
This family of uncharacterised proteins appears to be restricted to proteobacteria.
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 PF17944: Arginine decarboxylase C-terminal helical extension (domain)
This small three helical domain is found at the C-terminus of the arginine decarboxylase enzyme.
Pfam PF20422: DHR-2, Lobe B (domain)
DOCK (dedicator of cytokinesis) proteins are guanine nucleotide exchange factors (GEFs) that activate some small GTPases, such as Rac or Cdc42, by exchanging bound GDP for free GTP to control cell migration, morphogenesis, and phagocytosis. These proteins share a DOCK-type C2 domain (also termed the DOCK-homology region (DHR)-1) at the N-terminal, and the DHR-2 domain (also termed the DOCKER domain) at the C-terminal. DHR-2 is the GEF catalytic domain organised into three lobes A, B and C, with the Rho-family binding site and catalytic centre generated entirely from lobes B and C. This entry represents Lobe B which adopts an unusual architecture of two antiparallel beta sheets disposed in a loosely packed orthogonal arrangement. This lobe changes its position relative to lobe C and the bound GTPase, which suggests that lobe B distinguishes between the switch 1 conformations of Rac1 and Cdc42.
Pfam PF01232: Mannitol dehydrogenase Rossmann domain (domain)
Mannitol-1-phosphate 5-dehydrogenase catalyses the NAD-dependent reduction of mannitol-1-phosphate to fructose-6-phosphate  as part of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). The PTS facilitates the vectorial translocation of metabolisable carbohydrates to form the corresponding sugar phosphates, which are then converted to glycolytic intermediates . Mannitol 2-dehydrogenase catalyses the NAD-dependent reduction of mannitol to fructose . Several dehydrogenases have been shown  to be evolutionary related, including mannitol-1-phosphate 5-dehydrogenase (1.1.1.17) (gene mtlD), mannitol 2-dehydrogenase (1.1.1.67) (gene mtlK); mannonate oxidoreductase (1.1.1.57) (fructuronate reductase) (gene uxuB); Escherichia coli hypothetical proteins ydfI and yeiQ; and yeast hypothetical protein YEL070w. This domain has a Rossmann-type fold.
Pfam PF22496: Class III superoxide reductase, N-terminal (domain)
This short domain is found at the N-terminal end of class III superoxide reductase from Treponema pallidum (SOR, [swissprot:O83795]), a small protein that catalyse the one -electron reduction of superoxide to hydrogen peroxide, having rubredoxin as their putative electron donor. It is organised into two distinct domains: an N-terminal (this entry) that shows four beta-strands and a C-terminal that harbours the catalytic site and displays an immunoglobulin-like fold.
Pfam PF07549: SecD/SecF GG Motif (conserved_site)
This family consists of various prokaryotic SecD and SecF protein export membrane proteins. This SecD and SecF proteins are part of the multimeric protein export complex comprising SecA, D, E, F, G, Y, and YajC. SecD and SecF are required to maintain a proton motive force. This alignment encompasses a -GG- motif typically found in N-terminal half of the SecD/SecF proteins .