SII-SWORD/CoKE huggingface dataset:
Pfam PF19542: Family of unknown function (DUF6066) (family)
This entry represents a member of a biosynthetic gene cluster (BGC). This BGC (BGC0001418) is described by MIBiG as an example of the following biosynthetic classes, NRP (non-ribosomal peptide) and polyketide. This family includes a protein from the myxochromide D  biosynthetic gene cluster from Hyalangium minutum and appears to  be predominantly found in Cystobacterineae.
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 PF22343: Pilus-presented adhesin helical insertion domain (domain)
This entry represents the helical insertion domain found in surface proteins in certain pathogens, such as Streptococcus pneumoniae.
Pfam PF23358: OST48 middle domain (domain)
This entry represents the middle domain (MD) of OST48 from animals and its orthologue from yeast Wbp1. OST48/Wbp1 is a subunit of the oligosaccharyl transferase (OST) complex that catalyses the initial transfer of a defined glycan (Glc3Man9GlcNAc2 in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. This domain adopts a beta-sandwich fold, which together with the N-terminal domain ([pfam:PF03345]), interacts with riphophorin II/Swp1 subunit.
Pfam PF22260: Permutotetravirus RNA-dependent RNA polymerase thumb domain (domain)
This helical bundle domain, known as the thumb domain, is found in the RNA-dependent RNA polymerase (RdRp) of the Permutotetravirus Thosea asigna virus (TaV), C-terminal to the palm domain ([pfam:PF22152]). This domain is larger than the thumb domains of other viral ssRNA RdRPs.
Pfam PF24088: Domain of unknown function (DUF7373) N-terminal (domain)
This domain is found N-terminal in uncharacterised bacterial proteins. It is predicted to adopt a seven-stranded antiparallel beta-sheet with similarity to Mog1p/PsbP-like domains. Some proteins containing this domain have a lipoprotein attachment motif at the N-terminus suggesting they may be associated with the membrane. This domain is usually found in two copies that share little if any sequence similarity to each other.
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 PF23437: Family of unknown function (DUF7122) (domain)
This domain is found in a group of proteins from halobacteria. Members are 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 PF07710: P53 tetramerisation motif (conserved_site)
The p53 protein is a tetrameric transcription factor that plays a central role in the prevention of neoplastic transformation . Oligomerization appears to be essential for the tumour suppressing activity of p53. p53 can be divided into different functional domains: an N-terminal transactivation domain, a proline-rich domain, a DNA-binding domain (IPR008967), a tetramerisation domain and a C-terminal regulatory region. The tetramerisation domain of human p53 extends from residues 325 to 356, and has a 4-helical bundle fold. The tetramerisation domain is essential for DNA binding, protein-protein interactions, post-translational modifications, and p53 degradation .
Wikipedia: 
p53, also known as Tumor protein P53, cellular tumor antigen p53, or transformation-related protein 53 (TRP53) is a regulatory protein that is often mutated in human cancers. The p53 proteins are crucial in vertebrates, where they prevent cancer formation. As such, p53 has been described as "the guardian of the genome" because of its role in conserving stability by preventing genome mutation. Hence TP53 is classified as a tumor suppressor gene.
Pfam PF24489: Tip attachment protein J second Ig-like domain (domain)
This is the second Ig-like domain found in Tip attachment protein J from Escherichia phage lambda. J is a tail fibre protein that attaches the virion to the host receptor LamB, inducing viral DNA ejection.
Pfam PF07752: S-layer protein (family)
Archaeal S-layer proteins consist of two copies of this domain.
Wikipedia: The Methanosarcinales S-layer Tile Protein (MSTP) is a protein family found almost exclusively in Methanomicrobia members of the order Methanosarcinales. Typically a tandem repeat of two DUF1608 domains are contained in a single MSTP protein chain and these proteins self-assemble into the protective proteinaceous surface layer (S-layer) structure that encompasses the cell. The S-layer, which is found in most Archaea, and in many bacteria, serves many crucial functions including protection from deleterious extracellular substances.
Pfam PF09702: CRISPR-associated protein (Cas_Csa5) (family)
CRISPR is a term for Clustered, Regularly Interspaced Short Palindromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This entry represents a minor family of Cas proteins found in various species of Sulfolobus and Pyrococcus (all archaeal). It is found with two different CRISPR loci in Sulfolobus solfataricus.
Pfam PF23259: Plant cation/H(+) antiporter, C-terminal domain (domain)
This domain is found at the C-terminal end of Cation/H(+) antiporter 17 from Arabidopsis thaliana (CHX17) and similar plant sequences. CHX17 functions as a K+/H+ antiporter that controls K+ acquisition and homeostasis []. This protein has a highly hydrophobic N-terminal domain ([pfam:PF00999]) and a C-terminal region predicted to be non cytoplasmic that is organised into two domains thought to have a similar alpha-beta configuration.
Pfam PF19935: Domain of unknown function (DUF6398) (domain)
This domain is functionally uncharacterised, it is present in proteins from bacteria and archaea. This domain is approximately typically 100 amino acids in length and contains a conserved WA sequence motif.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF12763: EH domain (domain)
This entry represents the EH domain.
Pfam PF08034: Trematode eggshell synthesis protein (domain)
This domain has been identified in a number of distantly related species  of trematodes. This protein domain is crucial for eggshell synthesis in trematodes (Ebersberger I).
Pfam PF11648: C-terminal domain of RIG-I (domain)
This family of proteins represents the regulatory domain RD of RIG-I, a protein which initiates a signalling cascade that provides essential antiviral protection for the host. The RD domain binds viral RNA, activating the RIG-I ATPase by RNA-dependant dimerisation. The structure of RD contains a zinc-binding domain and is thought to confer ligand specificity.
Pfam PF19961: Effector-associated domain 8 (domain)
Effector-associated domains (EADs) are predicted to function as adaptor domains mediating protein-protein interactions. The EADs show a characteristic architectural pattern. One copy is always fused, typically to the N- or C-terminus, of a core component of a biological conflict system; examples include VMAP, iSTAND, or GAP1. Further copies of the same EAD are fused to either effector or signal-transducing domains, or additional EADs. EAD pairs are frequently observed together on the genome in conserved gene neighborhoods, but can also be severed from such neighborhoods and located in distant regions, indicating the EAD-EAD coupling approximates the advantages of collinear transcription. Profile-profile searches unify EAD8 with the Death superfamily of domains.
Pfam PF17959: EF-hand domain (domain)
This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.
Pfam PF20027: Family of unknown function (DUF6435) (family)
This family of proteins found in bacteria is functionally uncharacterised. Proteins in this family are approximately 60 amino acids in length and they are predicted to have a coiled-coil structure. There are two conserved motifs: KxLxxxY and EA.
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 PF01429: Methyl-CpG binding domain (domain)
The Methyl-CpG binding domain (MBD) binds to DNA that contains one or more symmetrically methylated CpGs.  DNA methylation in animals is associated with alterations in chromatin structure and silencing of gene expression. MBD has negligible non-specific affinity for DNA. In vitro foot-printing with MeCP2 showed the MBD can protect a 12 nucleotide region surrounding a methyl CpG pair. MBDs are found in several Methyl-CpG binding proteins and also DNA demethylase.
Wikipedia: The Methyl-CpG-binding domain (MBD) in molecular biology binds to DNA that contains one or more symmetrically methylated CpGs. MBD has negligible non-specific affinity for unmethylated DNA. In vitro foot-printing with the chromosomal protein MeCP2 showed that the MBD could protect a 12 nucleotide region surrounding a methyl CpG pair.
Pfam PF22432: PA2794-like, C-terminal (domain)
This domain is found at the C-terminal end of Exo-alpha-sialidase from Pseudomonas aeruginosa (PA2794), which adopts a trimeric structure, partly held together by an immunoglobulin-like trimerisation domain (this entry) that is C-terminal to [pfam:PF13088].
Pfam PF10040: CRISPR-associated endoribonuclease Cas6 (family)
Cas6 is a member of the RAMP (repeat-associated mysterious protein) superfamily. It is among the most widely distributed Cas proteins and is found in both bacteria and archaea. Cas6 functions in the generation of CRISPR-derived guide RNAs for invader defense in prokaryotes.
Pfam PF03745: Domain of unknown function (DUF309) (family)
This domain is found in eubacterial and archaebacterial proteins of unknown function. The proteins contain a motif HXXXEXX(W/Y) where X can be any amino acid. This motif is likely to be functionally important and may be involved in metal binding.
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 PF22265: T26-6p, second immunoglobulin-like domain (domain)
This domain is found in T26-6p from Thermococcus ([swissprot:D6MY29]) and similar archaeal sequences. T26-6p has three domains: two beta- sandwich with two sheets made of four antiparallel beta-strands ([pfam:PF22092] and this entry) and a bundle of five alpha-helices ([pfam:PF20984]).
Pfam PF01890: Cobalamin synthesis G C-terminus (domain)
Members of this family are involved in cobalamin synthesis.  The gene encoded by [swissprot:P72862] has been designated cbiH but in fact represents a fusion between cbiH and cbiG. As other multi-functional proteins involved in cobalamin biosynthesis catalyse adjacent steps in the pathway, including CysG, CobL (CbiET), CobIJ and CobA-HemD, it is therefore possible that CbiG catalyses a reaction step adjacent to CbiH. In the anaerobic pathway such a step could be the formation of a gamma lactone, which is thought to help to mediate the anaerobic ring contraction process. Within the cobalamin synthesis pathway CbiG catalyses the both the opening of the lactone ring and the extrusion of the two-carbon fragment of cobalt-precorrin-5A from C-20 and its associated methyl group (deacylation) to give cobalt-precorrin-5B. This family is the C-terminal region, and the mid- and N-termival parts are conserved independently in other families.
Wikipedia: Cobalamin biosynthesis is the process by which bacteria and archea make cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which it is used by enzymes in both the producing organisms and other species, including humans who acquire it through their diet.
Pfam PF06875: Plethodontid receptivity factor PRF (domain)
This family consists of several plethodontid receptivity factor (PRF) proteins which seem to be specific to Plethodon jordani (Jordan's salamander). PRF is a courtship pheromone produced by males increase female receptivity.
Pfam PF08214: Histone acetylation protein (domain)
Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation.  Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast.  This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11.
Pfam PF04212: MIT (microtubule interacting and transport) domain (domain)
The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.
Pfam PF19509: Family of unknown function (DUF6043) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in Bacteroidetes. Proteins in this family are typically between 293 and 398 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 PF06073: Bacterial protein of unknown function (DUF934) (family)
This family consists of several bacterial proteins of unknown function, however members have been suggested to be an accessory protein for sulfite reduction. This is based on the observation that they strongly cofit with various genes in  the sulfate assimilation pathway in various Pseudomonas as  well as in Marinobacter adhaerens HP15 and C. basilensis  4G11 (see Supplementary note 5 in.)
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 PF02522: Aminoglycoside 3-N-acetyltransferase (domain)
This family consists of bacterial aminoglycoside 3-N-acetyltransferases [ec:2.3.1.81], these catalyse the reaction: Acetyl-Co + a 2-deoxystreptamine antibiotic  CoA + N3'-acetyl-2-deoxystreptamine antibiotic. The enzyme can use a range of antibiotics with 2-deoxystreptamine rings as acceptor for its acetyltransferase activity, this inactivates and confers resistance to gentamicin, kanamycin, tobramycin, neomycin and apramycin amongst others.
Pfam PF16259: Domain of unknown function (DUF4913) (family)
This family consists of uncharacterized proteins around 150 residues in length and is mainly found in various Arthrobacter species. The function of this family may be functional in enableing the growth of Arthrobacter sp. strain JBH1 with nitroglycerin as the sole source of carbon and nitrogen.
Pfam PF19166: Family of unknown function (DUF5848) (family)
This is a family of uncharacterised proteins of unknown function predominantly found in viruses. This family is also found in Bacteria and Fungi.
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 PF16877: Domain of unknown function (DUF5078) (family)
This family of unknown function is found in Mycobacterium 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 PF01590: GAF domain (domain)
This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyse ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalysed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyses the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
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 PF01301: Glycosyl hydrolases family 35 (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 35 (GH35) comprises enzymes with only one known activity; beta-galactosidase (3.2.1.23).

Mammalian beta-galactosidase is a lysosomal enzyme (gene GLB1) which cleaves the terminal galactose from gangliosides, glycoproteins, and glycosaminoglycans and whose deficiency is the cause of the genetic disease Gm(1) gangliosidosis (Morquio disease type B).
Wikipedia: In molecular biology, glycoside hydrolase family 35 is a family of glycoside hydrolases.
Pfam PF00773: RNB domain (domain)
This domain is the catalytic domain of ribonuclease II.
Pfam PF08540: Hydroxymethylglutaryl-coenzyme A synthase C terminal (domain)
Hydroxymethylglutaryl-CoA synthase (2.3.3.10) catalyses the condensation of acetyl-CoA with acetoacetyl-CoA to produce HMG-CoA and CoA, the second reaction in the mevalonate-dependent isoprenoid biosynthesis pathway. HMG-CoA synthase contains an important catalytic cysteine residue that acts as a nucleophile in the first step of the reaction: the acetylation of the enzyme by acetyl-CoA (its first substrate) to produce an acetyl-enzyme thioester, releasing the reduced coenzyme A. The subsequent nucleophilic attack on acetoacetyl-CoA (its second substrate) leads to the formation of HMG-CoA .

HMG-CoA synthase occurs in eukaryotes, archaea and certain bacteria . In vertebrates, there are two isozymes located in different subcellular compartments: a cytosolic form that is the starting point of the mevalonate pathway (leads to cholesterol and other sterolic and isoprenoid compounds), and a mitochondrial form responsible for ketone body biosynthesis. HMG-CoA is also found in other eukaryotes such as insects, plants and fungi . In bacteria, isoprenoid precursors are generally synthesised via an alternative, non-mevalonate pathway, however a number of Gram-positive pathogens utilise a mevalonate pathway involving HMG-CoA synthase that is parallel to that found in eukaryotes .
This entry represents the C-terminal domain of HMG-CoA synthase enzymes from both eukaryotes and prokaryotes.
Wikipedia: In biochemistry, hydroxymethylglutaryl-CoA synthase or HMG-CoA synthase EC 2.3.3.10 is an enzyme which catalyzes the reaction in which acetyl-CoA condenses with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). This reaction comprises the second step in the mevalonate-dependent isoprenoid biosynthesis pathway. HMG-CoA is an intermediate in both cholesterol synthesis and ketogenesis. This reaction is overactivated in patients with diabetes mellitus type 1 if left untreated, due to prolonged insulin deficiency and the exhaustion of substrates for gluconeogenesis and the TCA cycle, notably oxaloacetate. This results in shunting of excess acetyl-CoA into the ketone synthesis pathway via HMG-CoA, leading to the development of diabetic ketoacidosis.
Pfam PF25066: VPS8-like, TPR-like repeats (repeat)
This region of TPR-like repeats is found towards the C-terminal of Vacuolar protein sorting-associated protein 8 from Saccharomyces cerevisiae (VPS8) and similar eukaryotic proteins. VPS8 is involved in the retention of proteins to the late-Golgi and plays an integral role in the complex vacuolar protein sorting process.