SII-SWORD/CoKE huggingface dataset:
Pfam PF15008: Domain of unknown function (DUF4518) (family)
The precise function of this protein family is unknown but it is thought to be involved in apoptosis regulation.
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 PF05359: Domain of Unknown Function (DUF748) (repeat)
This is a family of proteins 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 PF00642: Zinc finger C-x8-C-x5-C-x3-H type (and similar) (family)
This entry represents C-x8-C-x5-C-x3-H (CCCH) type Zinc finger (Znf) domains. Proteins containing CCCH Znf domains include Znf proteins from eukaryotes involved in cell cycle or growth phase-related regulation, e.g. human TIS11B (butyrate response factor 1, also known as mRNA decay activator protein ZFP36L1), a probable regulatory protein involved in regulating the response to growth factors, and the mouse TTP growth factor-inducible nuclear protein, which has the same function. The mouse TTP protein is induced by growth factors. Another protein containing this domain is the human splicing factor U2AF 35kDa subunit, which plays a critical role in both constitutive and enhancer-dependent splicing by mediating essential protein-protein interactions and protein-RNA interactions required for 3' splice site selection. It has been shown that different CCCH-type Znf proteins interact with the 3'-untranslated region of various mRNA . This type of Znf is very often present in two copies.
Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates . Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few . Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
Pfam PF23704: General transcription factor 3C polypeptide 1, winged-helix domain (domain)
This winged-helix (WH) domain is found at the N-terminal end of human General transcription factor 3C polypeptide 1 (GTF3C1, also known as TFIIIC220) and similar eukaryotic sequences. GTF3C1 is required for RNA polymerase III-mediated transcription. It binds to the box B promoter element.
Pfam PF18563: TubC N-terminal docking domain (domain)
This is the N-terminal docking domain found in TubC proteins from the tubulysin polyketide synthase and nonribosomal polypeptide synthetase (PKS-NRPS) system, which binds to C-terminal docking domain of TubB.
Pfam PF05598: Transposase domain (DUF772) (domain)
This presumed domain is found at the N-terminus of many proteins found in transposons.
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 PF03436: Domain of unknown function (DUF281) (family)
This family of worm domain has no known function. The boundaries of the presumed domain are rather uncertain.
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 PF07239: Outer membrane protein OpcA (family)
This family consists of several Neisseria species specific OpcA outer membrane proteins. Opc (formerly called 5C) is one of the major outer membrane proteins and has been shown to play an important role in meningococcal adhesion and invasion of both epithelial and endothelial cells.
Wikipedia: Outer membrane adhesin OpcA protein family consists of several Neisseria species specific outer membrane proteins. Neisseria meningitidis causes meningococcal meningitis and sepsis. Opc is one of the major outer membrane proteins and has been shown to play an important role in meningococcal adhesion and invasion of epithelial and endothelial cells, mediating attachment to host cells by binding proteoglycan cell-surface receptors.
Pfam PF24329: Teneurin 1-4, FN-plug domain (domain)
This entry represents the FN-plug domain found near the central region of Teneurins 1 to 4, a group of proteins involved in development and function of the nervous system. This domain forms numerous hydrogen-bonding and hydrophobic interactions with the YD-shell interior.
Pfam PF00332: Glycosyl hydrolases family 17 (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 17 GH17 comprises enzymes with several known activities; endo-1,3-beta-glucosidase (3.2.1.39); lichenase (3.2.1.73); exo-1,3-glucanase (3.2.1.58). Currently these enzymes have only been found in plants and in fungi.
Wikipedia: In molecular biology, Glycoside hydrolase family 17 is a family of glycoside hydrolases. It folds into a TIM barrel.
Pfam PF01361: Tautomerase enzyme (domain)
This family includes the enzyme 4-oxalocrotonate tautomerase [swissprot:Q01468] that catalyses the ketonisation of 2-hydroxymuconate to 2-oxo-3-hexenedioate.
Wikipedia: 4-Oxalocrotonate tautomerase or 4-OT is an enzyme that converts 2-hydroxymuconate to the αβ-unsaturated ketone, 2-oxo-3-hexenedioate. This enzyme forms part of a bacterial metabolic pathway that oxidatively catabolizes toluene, o-xylene, 3-ethyltoluene, and 1,2,4-trimethylbenzene into intermediates of the citric acid cycle. With a monomer size of just 62 amino acid residues, the 4-Oxalocrotonate tautomerase is one of the smallest enzyme subunits known. However, in solution, the enzyme forms a hexamer of six identical subunits, so the active site may be formed by amino acid residues from several subunits. This enzyme is also unusual in that it uses a proline residue at the amino terminus as an active site residue.
Pfam PF20087: Family of unknown function (DUF6479) (family)
This presumed domain is functionally uncharacterised. This domain family is found in bacteria, and is typically between 39 and 51 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 PF01539: Hepatitis C virus envelope glycoprotein E1 (family)
Poliovirus infection leads to drastic alterations in membrane permeability late during infection. Proteins 2B and 2BC enhance membrane permeability .
Pfam PF06810: Phage minor structural protein GP20 (family)
This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.
Pfam PF12857: TOBE-like domain (domain)
The TOBE domain (Transport-associated OB) always occurs  as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum (eg [swissprot:P46930]) and sulfate ([swissprot:P16676]). Found in ABC transporters immediately  after the ATPase domain.
Pfam PF02351: GDNF/GAS1 domain (domain)
This cysteine rich domain is found in multiple copies in GNDF and GAS1 proteins. GDNF and neurturin (NTN) receptors are potent survival factors for sympathetic, sensory and central nervous system neurons.  GDNF and neurturin promote neuronal survival by signaling through similar multicomponent receptors that consist of a common receptor tyrosine kinase and a member of a GPI-linked family of receptors that determines ligand specificity.
Wikipedia: The GDNF family receptor-α (GFRα) proteins are a group of co-receptors which form complexes with GDNF-family ligands (GFLs) to activate RET, the receptor of the GFLs. The GFRα co-receptors include the following:GFRα1 – preference for GDNF
GFRα2 – preference for neurturin
GFRα3 – preference for artemin
GFRα4 – preference for persephin
GFRAL - receptor for GDF15
Pfam PF23058: ZCCHC3, second RNA-binding domain (domain)
This entry represents the second RNA-binding domain (RBD) found in the Zinc finger CCHC domain-containing protein 3 (ZCCHC3). ZCCHC3 is a nucleic acid-binding protein crucial for the innate immune response to DNA and RNA viruses. It functions in the cytoplasm by binding to viral DNA and RNA, facilitating the recognition of these nucleic acids by key virus sensors like RIGI, IFIH1/MDA5, and CGAS.
Pfam PF02597: ThiS family (domain)
ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer [swissprot:O32583]. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalysed by IscS. MoaD, [swissprot:P30748] a protein involved sulphur transfer in molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end.
Pfam PF15563: Immunity protein 19 (family)
A predicted immunity protein with an alpha+beta fold and a conserved HxxRN motif. Proteins containing this domain are present in heterogeneous poly-immunity loci in polymorphic toxin systems.
Pfam PF00514: Armadillo/beta-catenin-like repeat (repeat)
Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.
Wikipedia: An armadillo repeat is a characteristic, repetitive amino acid sequence of about 42 residues in length that is found in many proteins. Proteins that contain armadillo repeats typically contain several tandemly repeated copies. Each armadillo repeat is composed of a pair of alpha helices that form a hairpin structure. Multiple copies of the repeat form what is known as an alpha solenoid structure.
Pfam PF16839: Nematode antimicrobial peptide (domain)
This family of antimicrobial peptides is found in nematodes.
Pfam PF14802: TMEM192 family (family)
The function of this family of transmembrane proteins is unknown. In vertebrates, proteins in this family are located in the lysosomal membrane and late endosome. In Arabidopsis, a member of this family has been found to weakly interact with FRIGIDA, a determinant of flowering time.
Pfam PF11927: Haem-dependent oxidative N-demethylase, alpha subunit-like (family)
This protein family is found in fungi and bacteria, including the alpha subunit of an haem-dependent oxidative N-demethylase (HODM) from Pseudomonas mendocina. This protein, catalytically active, is responsible for haem, oxygen and NADPH-dependent dimethylamine (DMA) binding. It shows structural similarity to the to the Aer2 PAS domain, but lacks the core PAS-domain alpha-helix that forms the Aer2 haem pocket, and displays extended beta-strands and a longer loop. The structure of [swissprot:A4XXY9], PDBe:5lte, shows that it is an haem-binding PAS domain, similar in structure to PAS gas sensors.
Pfam PF22624: 4'-phosphopantetheinyl transferase, N-terminal (domain)
This domain is found at the N-terminal end of human 4'-phosphopantetheinyl transferase (also known as L-aminoadipate -semialdehyde dehydrogenase-phosphopantetheinyl transferase, AASDHPPT), which catalyses the post-translational modification of target proteins by phosphopantetheine. This protein consists of two nearly identical domains (this entry and [pfam:PF01648]) connected by a short linker region. Both domains show a pair of beta-sheets connected by a loop region.
Pfam PF11492: Cricket paralysis virus, VP4 (family)
This is a family of minor capsid proteins, known as VP4, from the dicistroviridae. The dicistroviridae is a group of small, RNA-containing viruses that are closely structurally related to the picornaviridae. VP4 is a short, extended polypeptide chain found within the viral capsid, at the interface between the external protein shell and packaged RNA genome.
Pfam PF01157: Ribosomal protein L21e (family)
The eL21 family contains proteins from a number of eukaryotic and archaebacterial organisms which include mammalian eL21, Entamoeba histolytica eL21, Caenorhabditis elegans eL21 (C14B9.7), Saccharomyces cerevisiae (Baker's yeast) eL21 (URP1) and Haloarcula marismortui eL21 (HL31).
Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites . About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits.

Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome .
Pfam PF05752: Calicivirus minor structural protein (family)
This family consists of minor structural proteins largely from human calicivirus isolates. Human calicivirus causes gastroenteritis. The function of this family is unknown.
Pfam PF07826: IMP cyclohydrolase-like protein (domain)
This enzyme ([swissprot:O27099]) is may catalyse the cyclization of 5-formylamidoimidazole-4-carboxamide ribonucleotide to inosine monophosphate (IMP), a reaction which is important in de novo purine biosynthesis in archaeal species. This single domain protein is arranged to form an overall fold that consists of a four-layered alpha-beta-beta-alpha core structure. The two antiparallel beta-sheets pack against each other and are covered by alpha-helices on one face of the molecule. The protein is structurally similar to members of the N-terminal nucleophile (NTN) hydrolase superfamily.  A deep pocket was in fact found on the surface of IMP cyclohydrolase in a position equivalent to that of active sites of NTN-hydrolases, but an N-terminal nucleophile could not be found. Therefore, it is thought that this enzyme is structurally but not functionally similar to members of the NTN-hydrolase family.
Wikipedia: In enzymology, an IMP cyclohydrolase (EC 3.5.4.10) is an enzyme that catalyzes the chemical reactionIMP + H2O  5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Pfam PF20973: Vitamin uptake-like sensor (domain)
This is an integral membrane sensory domain related to the Putative vitamin uptake transporter Vut_1 ([pfam:PF02592], found in YhhQ protein from E. coli). This domain, named Vitamin uptake-like sensor (VUPS), is found in a variety of bacteria in combination with PAS (PF13188), GGDEF ([pfam:PF00990]), and EAL ([pfam:PF00563]) domains, and with histidine sensor kinases.
Pfam PF02161: Progesterone receptor (family)
Steroid or nuclear hormone receptors (NRs) constitute an important superfamily of transcription regulators that are involved in widely diverse physiological functions, including control of embryonic development, cell differentiation and homeostasis. Members of the superfamily include the steroid hormone receptors and receptors for thyroid hormone, retinoids, 1,25-dihydroxy-vitamin D3 and a variety of other ligands. The proteins function as dimeric molecules in nuclei to regulate the transcription of target genes in a ligand-responsive manner . In addition to C-terminal ligand-binding domains, these nuclear receptors contain a highly-conserved, N-terminal zinc-finger that mediates specific binding to target DNA sequences, termed ligand-responsive elements. In the absence of ligand, steroid hormone receptors are thought to be weakly associated with nuclear components; hormone binding greatly increases receptor affinity.

NRs are extremely important in medical research, a large number of them being implicated in diseases such as cancer, diabetes, hormone resistance syndromes, etc. While several NRs act as ligand-inducible transcription factors, many do not yet have a defined ligand and are accordingly termed "orphan" receptors. During the last decade, more than 300 NRs have been described, many of which are orphans, which cannot easily be named due to current nomenclature has recently been introduced in an attempt to rationalise the increasingly complex set of names used to describe superfamily members.

The progesterone receptor consists of 3 functional and structural domains: an N-terminal (modulatory) domain; a DNA binding domain that mediates specific binding to target DNA sequences (ligand-responsive elements); and a hormone binding domain. The N-terminal domain is unique to the progesterone receptors and spans approximately the first 500 residues; the highly-conserved DNA-binding domain is smaller (around 65 residues) and occupies the central portion of the protein; and the hormone binding domain lies at the receptor C terminus.
Wikipedia: The progesterone receptor (PR), also known as NR3C3 or nuclear receptor subfamily 3, group C, member 3, is a protein found inside cells. It is activated by the steroid hormone progesterone.
Pfam PF02547: Queuosine biosynthesis protein (family)
Queuosine (Q) biosynthesis protein, or S-adenosylmethionine:tRNA -ribosyltransferase-isomerase, is required for the synthesis of the queuosine precursor (oQ). It catalyses the transfer and isomerisation of the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to form epoxyqueuosine (oQ-tRNA).  Q is a hypermodified nucleoside usually found at the first position of the anticodon of asparagine, aspartate, histidine, and tyrosine tRNAs. In Streptococcus gordonii , QueA has been shown to play a role in the regulation of arginine deiminase genes.
Pfam PF01156: Inosine-uridine preferring nucleoside hydrolase (domain)
Inosine-uridine preferring nucleoside hydrolase (3.2.2.1) (IU-nucleoside hydrolase or IUNH) is an enzyme first identified in protozoan  that catalyses the hydrolysis of all of the commonly occuring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substrates. This enzyme is important for these parasitic organisms, which are deficient inde novosynthesis of purines, to salvage the host purine nucleosides. IUNH from Crithidia fasciculata has been sequenced and characterised, it is an homotetrameric enzyme of subunits of 34 Kd. An histidine has been shown to be important for the catalytic mechanism, it acts as a proton donor to activate the hypoxanthine leaving group.

A highly conserved region located in the N-terminal extremity contains four conserved aspartates that have been shown  to be located in the active site cavity.

IUNH is evolutionary related to a number of uncharacterised proteins from various biological sources.
This entry represents the structural domain of IUNH.
Pfam PF16561: Glycogen recognition site of AMP-activated protein kinase (family)
AMPK1_CBM is a family found in close association with AMPKBI [pfam:PF04739]. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.
Pfam PF17713: Family of unknown function (DUF5558) (family)
This is a family of unknown function found in Homo sapiens.
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 PF22552: T3SS (YopN, CesT) and YbjN peptide-binding chaperone 3 (domain)
This circularly-permuted TY-Chap domain is observed in host systems predicted to counter viral ribosylating toxins. They are predicted to function as peptide-binding chaperone domains that target proteins modified by ADPr and potentially misfolded as a consequence.