SII-SWORD/CoKE huggingface dataset:
Pfam PF01450: Ketol-acid reductoisomerase, C-terminal domain (domain)
Ketol-acid reductoisomerase (KARI; [ec:1.1.1.86]), also known as acetohydroxy acid isomeroreductase (AHIR or AHAIR), catalyses the  conversion of acetohydroxy acids into dihydroxy valerates in the  second step of the biosynthetic pathway for the essential  branched-chain amino acids valine, leucine, and isoleucine. KARI is present only in bacteria, fungi, and plants, but not in  animals. KARIs are divided into two classes on the basis of sequence  length and oligomerisation state. Class I KARIs are ~340 amino acid residues in length and include all fungal KARIs, whereas class II  KARIs are ~490 residues long and include all plant KARIs. Bacterial  KARIs can be either class I or class II. KARIs are composed of two  types of domains, an N-terminal Rossmann fold domain and one or two  C-terminal knotted domains. Two intertwinned knotted domains are  required for function, and in the short-chain or class I KARIs, each  polypeptide chain has one knotted domain. As a result, dimerization  of two monomers forms two complete KARI active sites. In the  long-chain or class II KARIs, a duplication of the knotted domain  has occurred and, as a result, the protein does not require dimerisation to complete its active site. The alpha-helical KARI C-terminal knotted domain can be described as a six-helix core in which helices coil like cable threads around  each other, thus forming a bundle.
Pfam PF16954: Haem-transporter, endosomal/lysosomal, haem-responsive gene (family)
HRG1 is a family of conserved, membrane-bound permeases that reside in distinct intracellular compartments and bind and transport haem in metazoa. These proteins carry four transmembrane domains, 4xTMs, modelled here in two pairs, the two N-terminal and the two more C-terminal.
Pfam PF10416: Transcription-initiator DNA-binding domain IBD (domain)
In Trichomonas vaginalis, thought to be the earliest extant eukaryote, the sole initiator element for control of the start of transcription is Inr, and this is recognised by the initiator binding protein IBP39. IBP39 contains an N-terminal Inr binding domain, IBD, connected via a flexible, proteolytically sensitive, linker (residues 127-145) to a C-terminal domain. The IBD structure reveals a winged-helix-wing conformation with each element binding to DNA, the central helix-turn-helix contributing the majority of the specificity-determining contacts with the Inr core motif TCAPy(T/A). The binding of IBP39 to the Inr directly recruits RNA polymerase II and in this way initiates transcription.
Pfam PF10782: Zinc-finger (family)
This bacterial family of proteins is a zinc-finger domain of the C2HC type with an additional cysteine.
Pfam PF21568: 1,3-alpha-isomaltosidase-like, N-terminal domain (domain)
This domain is found at the N-terminal 1,3-alpha-isomaltosidase from Kribbella flavida (AIMA, also known as Kfla1895) and sequences from actinomycetes. AIMA is involved in the intracellular degradation of the cyclic tetrasaccharide cyclobis-1-6-alpha-nigerosyl formed extracellularly from starch. It catalyses the hydrolysis of the alpha-1,3-glucosidic linkage of cyclobis-1-6-alpha-nigerosyl to yield isomaltose via a possible linear tetrasaccharide. This domain folds into an Ig-like beta-sandwich.
Pfam PF17219: Yaf2/RYBP C-terminal binding motif (conserved_site)
This motif is found in the Yaf2 and RYBP proteins that are homologous parts of the PRC1 complex. This motif forms a beta hairpin structure when it binds to the RAWUL domain [pfam:PF16207].
Pfam PF15098: TMEM89 protein family (family)
The function of this family of transmembrane proteins, TMEM89, has not, as yet, been determined. Members of this family are as yet uncharacterised. This family of proteins is found in eukaryotes. Proteins in this family are approximately 159 amino acids in length.
Pfam PF00843: Arenavirus nucleocapsid N-terminal domain (domain)
This N-terminal domain folds into a novel structure with a deep cavity for binding the m7GpppN cap structure that is required for viral RNA transcription.
Pfam PF00295: Glycosyl hydrolases family 28 (repeat)
Glycosyl hydrolase family 28 includes polygalacturonase [ec:3.2.1.15] as well as rhamnogalacturonase A(RGase A), [ec:3.2.1.-].  These enzymes is important in cell wall metabolism.
Wikipedia: In molecular biology, glycoside hydrolase family 28 is a family of glycoside hydrolases EC 3.2.1., which 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 glycoside hydrolases, based on sequence similarity, has led to the definition of &gt;100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
Pfam PF22544: HYDIN/CFA65/VesB-like, Ig-like domain (domain)
VesB is a serine protease that is secreted by the type II secretion system (T2S) in Vibrio cholerae ([swissprot:Q9KSQ6]). It efficiently cleaves a trypsin substrate, but not chymotrypsin and elastase substrates. It has been suggested to contribute to intestinal growth or pathogenesis, although is not the only factor required for intestinal survival. VesB can cleave the A subunit of cholera toxin, a process important for cholera toxin activation. It consists of a protease domain ([pfam:PF00089]) followed by a Ig-like domain, represented in this entry, which may be involved in one or more different functions such as stabilizing the protease domain, co-defining substrate specificity, binding to the bacterial surface and being part of a yet undefined secretion motif of the T2S system. This protein belongs to the chymotrypsin subfamily A (which includes mostly eukaryotic proteases), having a structure and specificity profile resembling that of eukaryotic trypsin-like proteases. This domain is also found in some eukaryotic proteins, such as HYDIN and CFA65 from human (which contain repeated Ig-like domains).
Pfam PF20126: Toxin TumE (family)
This entry represents a family of proteins found in archaea and bacteria. These proteins have been recently described as the toxin component TumE from the novel toxin-antitoxin system TumA, which constitutes a translation-targeting toxic effector. These proteins are predicted to adopt a conserved alpha+beta fold, where two alpha-helices pack against an antiparallel beta-sheet with seven strands.
Pfam PF17292: POB3-like N-terminal PH domain (domain)
This domain is found at the N-terminus of POB3 and related proteins.
Pfam PF02622: AlgH-like (family)
This entry represents a group of bacterial proteins, including AlgH from Pseudomonas aeruginosa, which is involved in the transcriptional regulation of alginate biosynthesis.
Pfam PF22223: ATR1 N-terminal domain (domain)
Host-adapted plant pathogens secrete numerous effectors into the host extracellular spaces or inside cells. The A. thaliana TNL receptor RPP1 confers strain-specific immunity through recognition of H.arabidopsidis effector ATR1. ATR1 consists of two alpha-helical domains that are involved in interactions with the receptor. The ATR1 N-terminal domain interacts with both, the C-terminal jelly roll/Ig-like domain (C-JID) and the LRRs of the RPP1 receptor.
Pfam PF18013: Phage tail lysozyme (domain)
This domain has a lysozyme like fold.  It is found in the tail protein of various phages probably giving them the ability to degrade the host cell wall peptidoglycan layer.
Pfam PF07884: Vitamin K epoxide reductase family (domain)
Vitamin K epoxide reductase (VKOR) recycles reduced vitamin K, which is used subsequently as a co-factor in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. VKORC1 is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea. Four cysteine residues and one residue, which is either serine or threonine, are identified as likely active-site residues. In some plant and bacterial homologues the VKORC1 homologous domain is fused with domains of the thioredoxin family of oxidoreductases.
Wikipedia: Vitamin K epoxide reductase (VKOR) is an enzyme that reduces vitamin K after it has been oxidised in the carboxylation of glutamic acid residues in blood coagulation enzymes. VKOR is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea. In some plant and bacterial homologues, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases.
Pfam PF19508: Family of unknown function (DUF6042) (family)
This entry represents a member of a biosynthetic gene cluster (BGC). This BGC (BGC0000291) is described by MIBiG as an example of the following biosynthetic class, NRP (non-ribosomal peptide). This family includes a protein from the A54145 biosynthetic gene cluster  from Streptomyces fradiae.
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 PF11361: Protein of unknown function (DUF3159) (family)
Some members in this family of proteins with unknown function are annotated as membrane proteins however this cannot be confirmed. Currently this family of proteins has no known function.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF17311: Family of unknown function (DUF5358) (family)
This family of unknown function is found in 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 PF15590: Immunity protein 27 (family)
A predicted immunity protein with an alpha+beta fold and a conserved aspartate and GGxP motif. Proteins containing this domain are present in bacterial polymorphic toxin systems as an immediate gene neighbour of the toxin gene, usually containing a domain of the Ntox10 or Tox-ParB families.
Pfam PF01639: Viral family 110 (family)
This family of viral proteins is known as the 110 family. The function of members of this family is unknown. The family contains a central cysteine rich region with eight conserved cysteines. Some members of the family contains two copies of the cysteine rich region [swissprot:P18560].
Pfam PF05791: Bacillus haemolytic enterotoxin (HBL) (family)
This family consists of several Bacillus haemolytic enterotoxins (HblC, HblD, HblA, NheA, and NheB) which can cause food poisoning in humans.
Wikipedia: In molecular biology, the Bacillus haemolytic enterotoxin family of proteins consists of several Bacillus haemolytic enterotoxins, which can cause food poisoning in humans. Haemolysin BL and non-haemolytic enterotoxin, represent the major enterotoxins produced by Bacillus cereus. Most of the cytotoxic activity of B. cereus isolates has been attributed to the level of Nhe, which may indicate a highly diarrheic potential. The exact mechanism by which B. cereus causes diarrhoea is unknown. Hbl, cytotoxin K (CytK) and Nhe are all putative causes.
Pfam PF06355: Aegerolysin (family)
This family consists of several bacterial and fungal Aegerolysin-like proteins. It has been found that aegerolysin and ostreolysin are expressed during formation of primordia and fruiting bodies. It has been suggested that these haemolysins play an important role in initial phase of fungal fruiting. The bacterial members of this family are expressed during sporulation.  Ostreolysin was found cytolytic to various erythrocytes and tumour cells. It forms transmembrane pores 4 nm in diameter. The activity is inhibited by total membrane lipids, and modulated by lysophosphatides. The potential use of aegerolysins is reviewed with special emphasis on their properties which would allow their use in therapeutics. Aegerolysin is part of the pleurotolysin pore-forming (Pleurotolysin) transporter superfamily. Member proteins assemble into a transmembrane pore complex.
Pfam PF02386: Cation transport protein (family)
This family consists of various cation transport proteins (Trk) and  V-type sodium ATP synthase subunit J or translocating ATPase J [ec:3.6.1.34]. These proteins are involved in active sodium up-take utilising ATP in the process.  TrkH a member of the family [swissprot:P76769] from E. coli is a  hydrophobic membrane protein and determines the specificity and kinetics  of cation transport by the TrK system in E. coli.
Wikipedia: This protein family consists of various potassium transport proteins (Trk) and V-type sodium ATP synthase subunit J or translocating ATPase J. These proteins are involved in active sodium uptake utilizing ATP in the process. TrkH from Escherichia coli is a transmembrane protein and determines the specificity and kinetics of cation transport by the TrK system in this organism. This protein interacts with TrkA and requires TrkE for transport activity.
Pfam PF17484: N-Lobe handle Tf-binding protein B (domain)
Bacterial lipoproteins represent a large group of specialized membrane proteins that perform a variety of functions including maintenance and stabilization of the cell envelope, protein targeting and transit to the outer membrane, membrane biogenesis, and cell adherence. Pathogenic Gram-negative bacteria within the Neisseriaceae and Pasteurellaceae families rely on a specialized uptake system, characterized by an essential surface receptor complex that acquires iron from host transferrin (Tf) and transports the iron across the outer membrane. They have an iron uptake system composed of surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), that together function to extract iron from the host iron binding glycoprotein (Tf). TbpB is a bilobed (N and C lobe) lipid-anchored protein with each lobe consisting of an eight-stranded beta barrel flanked by a 'handle' domain made up of four (N lobe) or eight (C lobe) beta strands. TbpB extends from the outer membrane surface by virtue of an N-terminal peptide region that is anchored to the outer membrane by fatty acyl chains on the N-terminal cysteine and is involved in the initial capture of iron-loaded Tf. The 4-residue conserved LSAC motif found at the amino terminus of TbpB represents a prototypical lipobox, with the cysteine residue serving as the first amino acid in the mature protein which is subsequently modified by the addition of a diacyl glycerol. A second conserved motif of interest is located two amino acids downstream of the LSAC site. This region consists of four glycine residues in tandem. Deletion of the conserved polyglycine motif has significant negative effects on growth in certain conditions, while mutational analysis revealed that the LSAC motif constituting the lipobox of TbpB is necessary for lipidation and hence tethering of TbpB to the bacterial surface. This domain family is found on the N-terminal region of TbpB proteins, which comprises the N lobe handle consisting of a four-stranded antiparallel beta sheets held together by a short surface-exposed alpha helix. Tf-binding activity primarily resides in the TbpB N lobe.
Pfam PF15081: Domain of unknown function (DUF4548) (family)
This family of proteins is found in eukaryotes. Proteins in this family are typically between and 178 amino acids in length. The human member of this family is C1orf105.
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 PF20870: FAM186A/B, N-terminal (domain)
This is a helical region found at the N-terminal of FAM186A/B from human and similar proteins. The function of members in this entry is not clear.
Pfam PF00322: Endothelin family (family)
Endothelins (ET's) are the most potent vasoconstrictors known . They stimulate cardiac contraction, regulate release of vasoactive substances, and stimulate mitogenesis in blood vessels in primary culture. They also stimulate contraction in almost all other smooth muscles (e.g., uterus, bronchus, vas deferensa and stomach) and stimulate secretion in several tissues (e.g., kidney, liver and adrenals). Endothelin receptors have also been found in the brain, e.g. cerebral cortex, cerebellum and glial cells. Endothelins have been implicated in a variety of pathophysiological conditions associated with stress, including hypertension, myocardial infarction, subarachnoid haemorrhage and renal failure.

Endothelins are synthesised by proteolysis of large preproendothelins, which are cleaved to 'big endothelins' before being processed to the mature peptide.

Sarafotoxins (SRTX) and bibrotoxin (BTX) are cardiotoxins from the venom of snakes of the Atractaspis family, structurally and functionally  similar to endothelin.

As shown in the following schematic representation, these peptides which are 21 residues long contain two intramolecular disulphide bonds.

                        +-------------+
                        |             |
                        CxCxxxxxxxCxxxCxxxxxx
                          |       |
                          +-------+
'C': conserved cysteine involved in a disulphide bond.
Wikipedia: Endothelins are peptides with receptors and effects in many body organs. Endothelin constricts blood vessels and raises blood pressure. The endothelins are normally kept in balance by other mechanisms, but when overexpressed, they contribute to high blood pressure (hypertension), heart disease, and potentially other diseases.
Pfam PF05757: Oxygen evolving enhancer protein 3 (family)
This family consists of the plant specific oxygen evolving enhancer protein 3 (PsbQ). Photosystem II (PSII)1 is a pigment-protein complex, which consists of at least 25 different protein subunits, at present denoted PsbA-Z according to the genes that encode them. PsbQ plays an important role in the lumenal oxygen-evolving activity of PSII from higher plants and green algae.
Pfam PF13968: Domain of unknown function (DUF4220) (family)
This family is found in plants and is often associated with DUF294, [pfam:PF04578].
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 PF05041: Pecanex protein (C-terminus) (family)
This family consists of C terminal region of the pecanex protein homologues. The pecanex protein is a maternal-effect neurogenic gene found in Drosophila.
Pfam PF05194: UreE urease accessory protein, C-terminal domain (domain)
UreE is a urease accessory protein. Urease [pfam:PF00449] hydrolyses  urea into ammonia and carbamic acid. The C-terminal region of members of this family contains a His rich Nickel binding site.
Pfam PF16197: Ketoacyl-synthetase C-terminal extension (family)
KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pfam PF16748: Inscuteable LGN-binding domain (domain)
This is the LGN-binding domain (LBD) of the inscuteable homologue protein. It interacts with the TPR motifs of G-protein-signaling modulator 2 (GPSM2) (LGN) and stabilises LGN.
Pfam PF13039: Protein of unknown function (DUF3900) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are approximately 360 amino acids in length.
Pfam PF23145: IFT121, second zinc finger domain (domain)
This domain is found C-terminal in the homologues of Intraflagellar transport protein 121 (IFT121). IFT121 is a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors. This protein plays a role in cilia assembly and maintenance. IFT121 is predicted to contain a tandem of zinc fingers with rubredoxin-like fold. This entry represents the second rubredoxin-like zinc finger.
Pfam PF16208: Keratin type II head (family)
All intermediate filament proteins feature a central Î±-helical rod domain and variable nonhelical domains located at the N-terminal (head) and C-terminal (tail). The central rod domain is the main driver of self-assembly into filaments, whereas the N- and C-terminal domains are involved in post-translational modifications and interactions with other proteins . Type I and type II keratin form heteropolymeric intermediate filaments providing vital mechanical support in epithelia . This entry represents the N-terminal domain (head) of type II keratins.
Pfam PF08357: SEFIR domain (family)
This family comprises IL17 receptors (IL17Rs, e.g. [swissprot:Q60943]) and SEF proteins (e.g. [swissprot:Q8QHJ9]). The latter are feedback inhibitors of FGF signalling and are also thought to be receptors. Due to its similarity to the TIR domain ([pfam:PF01582]), the SEFIR region is thought to be involved in homotypic interactions with other SEFIR/TIR-domain-containing proteins. Thus, SEFs and IL17Rs may be involved in TOLL/IL1R-like signalling pathways.
Wikipedia: Interleukin-17 receptor (IL-17R) is a cytokine receptor which belongs to new subfamily of receptors binding proinflammatory cytokine interleukin 17A, a member of IL-17 family ligands produced by T helper 17 cells (Th17). IL-17R family consists of 5 members: IL-17RA, IL-17RB, IL-17RC, IL-17RD and IL-17RE. Functional IL-17R is a transmembrane receptor complex usually consisting of one IL-17RA, which is a founding member of the family, and second other family subunit, thus forming heteromeric receptor binding different ligands. IL-17A, a founding member of IL-17 ligand family binds to heteromeric IL-17RA/RC receptor complex. IL-17RB binds preferentially IL-17B and IL-17E and heteromeric IL-17RA/RE complex binds IL-17C. However, there is still unknown ligand for IL-17RD. The first identified member IL-17RA is located on human chromosome 22, whereas other subunits IL-17RB to IL-17RD are encoded within human chromosome 3.
Pfam PF16299: Domain of unknown function (DUF4941) (family)
This family consists of several uncharacterized proteins around 300 residues in length and is mainly found in various Thermotoga species. The function of this family is unknown.
Pfam PF22374: Clospo_01618-like (domain)
This domain is found in Lipoprotein from Clostridium sporogenes (Clospo_01618) and similar bacterial proteins. It shows a two -layered alpha/beta configuration, displaying structural similarity to the N-terminal domain of YycH, which plays a role in signal transduction.