SII-SWORD/CoKE huggingface dataset:
Pfam PF00273: Serum albumin family (domain)
A number of serum transport proteins are known to be evolutionarily related, including albumin, alpha-fetoprotein, vitamin D-binding protein and afamin . Albumin is the main protein of plasma; it binds water, cations (such as Ca2+, Na+and K+), fatty acids, hormones, bilirubin and drugs - its main function is to regulate the colloidal osmotic pressure of blood. Alphafeto- protein (alpha-fetoglobulin) is a foetal plasma protein that binds various cations, fatty acids and bilirubin. Vitamin D-binding protein binds to vitamin D and its metabolites, as well as to fatty acids. The biological role of afamin (alpha-albumin) has not yet been characterised. The 3D structure of human serum albumin has been determined by X-ray crystallography to a resolution of 2.8A . It comprises three homologous domains that assemble to form a heart-shaped molecule . Each domain is a product of two subdomains that possess common structural motifs . The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. Structurally, the serum albumins are similar, each domain containing five or six internal disulphide bonds, as shown schematically below:
                    +---+          +----+                        +-----+
                    |   |          |    |                        |     |
 xxCxxxxxxxxxxxxxxxxCCxxCxxxxCxxxxxCCxxxCxxxxxxxxxCxxxxxxxxxxxxxxCCxxxxCxxxx
   |                 |       |     |              |               |
   +-----------------+       +-----+              +---------------+
Wikipedia: Albumin is a family of globular proteins, the most common of which are the serum albumins. All of the proteins of the albumin family are water-soluble, moderately soluble in concentrated salt solutions, and experience heat denaturation. Albumins are commonly found in blood plasma and differ from other blood proteins in that they are not glycosylated. Substances containing albumins are called albuminoids.
Pfam PF09354: HNF3 C-terminal domain (domain)
This presumed domain is found in the C-terminal region of Hepatocyte Nuclear Factor 3 alpha and beta chains. Its specific function is uncertain. The N-terminal region of this presumed domain contains an EH1 (engrailed homology 1) motif, that is characterised by the FxIxxIL sequence.
Pfam PF02529: Cytochrome B6-F complex subunit 5 (family)
This family consists of cytochrome B6-F complex subunit 5 (PetG). The cytochrome bf complex found in green plants, eukaryotic algae and cyanobacteria, connects photosystem I to photosystem II in the electron  transport chain, functioning as a plastoquinol:plastocyanin/cytochrome c6 oxidoreductase. PetG or subunit 5 is associated with the bf complex and the absence of PetG affects either the assembly or stability of the cytochrome bf complex in  Chlamydomonas reinhardtii.
Pfam PF07291: Methylamine utilisation protein MauE (domain)
This family consists of several bacterial methylamine utilisation MauE proteins. Synthesis of enzymes involved in methylamine oxidation via methylamine dehydrogenase (MADH) is encoded by genes present in the mau cluster. MauE and MauD are specifically involved in the processing, transport, and/or maturation of the beta-subunit and that the absence of each of these proteins leads to production of a non-functional beta-subunit which becomes rapidly degraded.
Pfam PF11572: Protein of unknown function (DUF3234) (family)
This bacterial family of proteins has no known function. Some members in this family of proteins are annotated as TTHA0547 however this cannot be confirmed.
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 PF22024: Major capsid protein VP16-like (family)
This family includes the major capsid protein VP16 from Thermus virus P23-77, which shows two turrets, producing a crenellated appearance.
Pfam PF22750: Ant venom allergen Sol i 2 family (domain)
Sol i 2, one of four known potent allergens from the venom of red imported fire ant, is a powerful trigger of anaphylaxis. It causes production of IgE antibody in many individuals stung by fire ants. The closest structure homolog of Sol I 2 is the odorant binding protein and pheromone binding protein LUSH of the fruit fly Drosophila ([pfam:PF01395]), suggesting a possible similar biological function.
Pfam PF10215: Oligosaccaryltransferase (family)
Ost4 is a very short, approximately 30 residues, enzyme found from fungi to vertebrates. It is a member of the ER oligosaccaryltansferase complex, EC 2.4.1.119, that catalyses the asparagine-linked glycosylation of proteins. It appears to be an integral membrane protein that mediates the en bloc transfer of a preassembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum (RER).
Wikipedia: In molecular biology, OST4 is a subunit of the oligosaccharyltransferase complex.
OST4 is a very short, approximately 30 amino acids, protein found from fungi to vertebrates. It appears to be an integral membrane protein that mediates the en bloc transfer of a pre-assembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum.
Pfam PF16389: Domain of unknown function (family)
This family around 200 residues locates in the N-terminal of some uncharacterized proteins in various Bacteroides and Parabacteroides species. The function of this family remains unknown.
Pfam PF08566: Mitochondrial import protein Pam17 (family)
The presequence translocase-associated motor (PAM) drives the completion of preprotein translocation into the mitochondrial matrix.  The Pam17 subunit is required for formation of a stable complex between cochaperones Pam16 and Pam18 and promotes the association of Pam16-Pam18 with the presequence translocase. Mitochondria lacking Pam17 are selectively impaired in the import of matrix proteins.
Pfam PF17682: Tau95 Triple barrel domain (domain)
TFIIIC1 is a multisubunit DNA binding factor that serves as a dynamic platform for assembly of pre-initiation complexes on class III genes. This entry represents the tau 95 subunit which holds a key position in TFIIIC, exerting both upstream and downstream influence on the TFIIIC-DNA complex by rendering the complex more stable. Once bound to tDNA-intragenic promoter elements, TFIIIC directs the assembly of TFIIIB on the DNA, which in turn recruits the RNA polymerase III (pol III) and activates multiple rounds of transcription.
Pfam PF07248: Protein of unknown function (DUF1431) (family)
This family contains a number of Drosophila melanogaster proteins of unknown function. These contain several conserved cysteine residues.
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 PF18935: Family of unknown function (DUF5683) (family)
This is a domain of unknown function found mostly 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 PF01471: Putative peptidoglycan binding domain (domain)
This domain is composed of three alpha helices.  This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation.  This domain may have a general peptidoglycan binding function.  This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.
Wikipedia: Peptidoglycan binding domains have a general peptidoglycan binding function and a common core structure consisting of a closed, three-helical bundle with a left-handed twist. It is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. Examples are:Muramoyl-pentapeptide carboxypeptidase 
N-acetylmuramoyl-L-alanine amidase cwlA precursor 
Autolytic lysozyme 
Membrane-bound lytic murein transglycosylase B
Zinc-containing D-alanyl-D-alanine-cleaving carboxypeptidase, VanX.
Pfam PF18118: Polycomb repressive complex 2 tri-helical domain (domain)
This domain can be found in the Polycomb repressive complex 2 (PRC2) present in Homo sapiens. Polycomb complexes maintain repressive chromatin states by silencing gene expression. PRC2 does this by methylating lysine 27 of histone H3. This domain makes up part of the N-lobe which is involved in regulation.
Pfam PF01112: Asparaginase (domain)
This protein family represents a group of Ntn-hydrolases from all cellular organisms that belong to the MEROPS peptidase family T2 (clan PB(T)). Members of this entry include glycosylasparaginases (3.5.1.26), which are threonine peptidases, and L-asparaginases (3.5.1.1).

Glycosylasparaginases are characterised by a threonine nucleophile at the N terminus of the mature enzyme. They catalyse:

N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-glucosaminylamine + L-aspartate

It cleaves the GlcNAc-Asn bond that links oligosaccharides to asparagine in N-linked glycoproteins. The enzyme is composed of two non-identical alpha/beta subunits joined by strong non-covalent forces, has one glycosylation site located in the alpha subunit  and plays a major role in the degradation of glycoproteins.

L-asparaginases catalyse the following reaction:

L-asparagine + H2O = L-aspartate + NH3
Wikipedia: Asparaginase is an enzyme that is used as a medication and in food manufacturing. As a medication, L-asparaginase is used to treat acute lymphoblastic leukemia (ALL) and lymphoblastic lymphoma (LBL). It is given by injection into a vein, or muscle. A pegylated version is also available. In food manufacturing it is used to decrease acrylamide.
Pfam PF18465: Rieske 3Fe-4S (domain)
This domain is comprised of the iron-sulphur cluster and Rieske subunit found in the large subunit of arsenite oxidase. Arsenite oxidase is a 100 kDa molybdenum- and iron-sulfur-containing protein located on the outer surface of the inner membrane of Gram-negative organisms. The large subunit of arsenite oxidase is similar to other members of the dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes. The large subunit of arsenite oxidase is divided into four domains, with domain I binding the [3Fe-4S] cluster . Domain I, consists of three antiparallel beta sheets and six helices. The [3Fe-4S] cluster is coordinated by the motif Cys21-X2-Cys24-X3-Cys28 near the interface with domains III and IV. A large, flattened funnel-like cavity bounded by domains I, II, and III leads to the molybdenum center [pfam:PF00384] located near the center of the molecule.
Pfam PF18403: Thioredoxin-like domain (domain)
This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
Wikipedia: Thioredoxins are small disulfide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein disulfide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of 2 cysteine thiol groups to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. The net result is the covalent interconversion of a disulfide and a dithiol.
Pfam PF08487: Vault protein inter-alpha-trypsin domain (family)
Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains.  ITIs play a role in extracellular matrix (ECM) stabilisation and tumour metastasis as well as in plasma protease inhibition.  The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain ([pfam:PF00092]) in ITI heavy chains (ITIHs) and their precursors.
Pfam PF21691: Alpha-galactosyl binding lectin (family)
This protein family includes Alpha-galactosyl-binding lectin from Lyophyllum decastes (LDL) and similar proteins from fungi. This protein forms a compact structure with a five-stranded anti-parallel beta-sheet and two alpha-helices packed against one side of the beta- sheet.
Pfam PF23096: Proteasome activator complex subunit 4-like, HEAT repeat-like (repeat)
This domain is found in Proteasome activator complex subunit 4 (PSME4) and in similar sequences from animals and fungi. PSME4 is an associated component of the proteasome that specifically recognises acetylated histones and promotes ATP- and ubiquitin -independent degradation of core histones during spermatogenesis and DNA damage response. This protein adopts a dome-like structure composed of HEAT repeat-like modules interconected through three long loops. This entry represents a region of HEAT repeats that contains a long loop.
Wikipedia: A HEAT repeat is a protein tandem repeat structural motif composed of two alpha helices linked by a short loop. HEAT repeats can form alpha solenoids, a type of solenoid protein domain found in a number of cytoplasmic proteins. The name "HEAT" is an acronym for four proteins in which this repeat structure is found: Huntingtin, elongation factor 3 (EF3), protein phosphatase 2A (PP2A), and the yeast kinase TOR1. HEAT repeats form extended superhelical structures which are often involved in intracellular transport; they are structurally related to armadillo repeats. The nuclear transport protein importin beta contains 19 HEAT repeats.
Pfam PF07940: Heparinase II/III-like, C-terminal (domain)
This is the C-terminal domain of Heparin and heparin-sulfate lyase (HepB, also known as heparinase II), Heparin-sulfate lyase (HepC, also known as heparinase III and distantly related sequences. The structures of Heparinase II and III have been solved. HepB cleaves both heparin and heparan sulfate glycosaminoglycans. HepC specifically cleaves heparan sulfate-rich regions of acidic polysaccharides, it does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated glucosamine linkages. HepC functions in cleaving metazoan heparan sulfate and providing carbon, nitrogen and sulfate sources for microorganisms. This entry also includes FtsZ-localized protein C (FzlC), which binds and recruits FtsZ polymers to membranes early in the cell cycle. It may also improve the efficiency of cytokinesis. This protein has been reported to have sequence similarity to heparinase II/III family proteins.
Pfam PF20381: Membrane protein Rv1476 (family)
This entry, previously known as DUF6676, represents Membrane protein Rv1476 an related proteins found in actinobacteria. Rv1476 probably affects the expression of genes linked to host macrophage apoptosis and immune response, thereby promoting the survival of Mycobacterium tuberculosis in host macrophages.
Pfam PF13380: CoA binding domain (domain)
This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pfam PF17241: Ty5 Gag N-terminal region (domain)
This entry corresponds to part of the Gag protein found in a variety of retrotransposons. It is not clear whether this covers the matrix or capsid proteins partially or entirely.
Pfam PF22237: SO2946-like, C-terminal domain (domain)
This entry represents the C-terminal domain of SO2946 from Shewanella oneidensis MR-1. The SO2946 protein consists of a short helical N-terminal domain and a large C-terminal domain with the jelly-roll topology, identified as a putative carbohydrate-binding module.
Pfam PF07808: RED-like protein N-terminal region (family)
This family contains sequences that are similar to the N-terminal region of Red protein ([swissprot:Q13123]). This and related proteins contain a RED repeat which consists of a number of RE and RD sequence elements. The region in question has several conserved NLS sequences and a putative trimeric coiled-coil region, suggesting that these proteins are expressed in the nucleus. The function of Red protein is unknown, but efficient sequestration to nuclear bodies suggests that its expression may be tightly regulated of that the protein self-aggregates extremely efficiently.
Pfam PF14328: Domain of unknown function (DUF4385) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria, archaea, eukaryotes and viruses. Proteins in this family are typically between 149 and 163 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 PF01799: [2Fe-2S] binding domain (domain)
The  binding domain is found in a range of enzymes including dehydrogenases, oxidases and oxidoreductases.

The aldehyde oxido-reductase (Mop) from the sulphate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas is a homodimer of 907 amino acid residues subunits and is a member of the xanthine oxidase family. The protein contains a molybdopterin cofactor (Mo-co) and two different  centres. It is folded into four domains of which the first two bind the iron sulphur centres and the last two are involved in Mo-co binding. Mo-co is a molybdenum molybdopterin cytosine dinucleotide. Molybdopterin forms a tricyclic system with the pterin bicycle annealed to a pyran ring. The molybdopterin dinucleotide is deeply buried in the protein. The cis-dithiolene group of the pyran ring binds the molybdenum, which is coordinated by three more (oxygen) ligands .
Pfam PF22689: FGAR-AT PurM_N-like domain (domain)
This entry represents the PurM_N-like domain of formylglycinamide ribonucleotide amidotransferase (FGAR-AT) and related proteins. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) to formylglycinamidine ribonucleotide (FGAM) in the fourth step of the purine biosynthetic pathway. This domain consists of an antiparallel beta-sheet with two helices packed on one side.
Pfam PF04529: Herpesvirus U59 protein (family)
The proteins in this family have no known function. Cytomegalovirus UL88 is also a member of this family.
Pfam PF20595: Putative adhesive domain (group 6) (family)
This domain resembles the SdrG_C_C adhesive domain,  known to bind within a supra-domain with the Big_8  domain ([pfam:PF17961]) to fibrinogen. It is found N-terminal  to repeating stalk domains in bacterial surface proteins.
Pfam PF18984: Family of unknown function (DUF5717)N-terminal (family)
This is the N-terminal domain found in sequences of unknown function 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 PF16989: Type VI secretion, EvfE, EvfF, ImpA, BimE, VC_A0119, VasJ (family)
T6SS_VasJ is a family from Gram-negative bacteria that forms a component of the type VI pathogenic secretion system.  In the case of the Escherichia coli RS218 strain UniProtKB:G8IRL4, EvfF,it represents expression of the full-length gene; whereas it is just the C-terminal part of EvfE, UniProtKB:G8IRL3. The N-terminal part of these sequences is in family ImpA_N, [pfam:PF06812].
Pfam PF22375: Glucosyltransferase Lgt1, N-terminal domain (domain)
This domain is found at the N-terminal end of Glucosyltransferase Lgt1 from Legionella pneumophila, which has been suggested to be involved in pathogenesis. This domain adopts a completely alpha -helical configuration.
Pfam PF00209: Sodium:neurotransmitter symporter family (family)
These are twelve xTM-containing region transporters.
Wikipedia: A neurotransmitter sodium symporter (NSS) (TC# 2.A.22) is type of neurotransmitter transporter that catalyzes the uptake of a variety of neurotransmitters, amino acids, osmolytes and related nitrogenous substances by a solute:Na+ symport mechanism. The NSS family is a member of the APC superfamily. Its constituents have been found in bacteria, archaea and eukaryotes.
Pfam PF24411: Family of unknown function (DUF7545) (family)
This entry represents a family of uncharacterised proteins found mainly in Halobacteria. These proteins are likely to form a dimer structure as predicted by AlphaFold with significant ipTM score.
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 PF01452: Rotavirus non structural protein (family)
This protein has been called NSP4, NSP5, NS28, and NCVP5. The final steps in the assembly of rotavirus occur in the lumen of the endoplasmic reticulum (ER). Targeting of the immature inner capsid particle (ICP) to this compartment is mediated by the cytoplasmic tail of NSP4, located in the ER membrane.
Wikipedia: The rotavirus nonstructural protein NSP4 was the first viral enterotoxin discovered. It is a viroporin and induces diarrhea and causes Ca2+-dependent transepithelial secretion.
Pfam PF14436: Bacterial EndoU nuclease (family)
This is a bacterial virion of EndoU nuclease. It is found at C-terminal region of polymorphic toxin proteins.
Pfam PF10715: T4-page Endoribonuclease RegB (domain)
The RegB endoribonuclease encoded by bacteriophage T4 is a unique sequence-specific nuclease that cleaves in the middle of GGAG or, in a few cases, GGAU tetranucleotides, preferentially those found in the Shine-Dalgarno regions of early phage mRNAs. Phage RB49 in addition to RegB utilises Escherichia coli endoribonuclease E for the degradation of its transcripts for gene regB. The deduced primary structure of RegB proteins of 32 phages studied is almost identical to that of T4, while the sequences of RegB encoded by phages RB69, TuIa and RB49 show substantial divergence from their T4 counterpart. Rebuilding from the PDB:2hx6 structure, this family does not fall into the Lysozyme-like family, but rather is a new member of the RelE/YoeB structural and functional family of ribonucleases specialising in mRNA inactivation within the ribosome.