SII-SWORD/CoKE huggingface dataset:
Pfam PF15362: Enamelin (disordered)
ENAMELIN is involved in the mineralisation and structural organisation of enamel. It is necessary for the extension of enamel during the secretory stage of dental enamel formation. The proteins are expressed in teeth, particularly in odontoblasts, ameloblasts and cementoblasts.
Wikipedia: Enamelin is an enamel matrix protein (EMPs), that in humans is encoded by the ENAM gene. It is part of the non-amelogenins, which comprise 10% of the total enamel matrix proteins. It is one of the key proteins thought to be involved in amelogenesis. The formation of enamel's intricate architecture is thought to be rigorously controlled in ameloblasts through interactions of various organic matrix protein molecules that include: enamelin, amelogenin, ameloblastin, tuftelin, dentine sialophosphoprotein, and a variety of enzymes. Enamelin is the largest protein (~168kDa) in the enamel matrix of developing teeth and is the least abundant of total enamel matrix proteins. It is present predominantly at the growing enamel surface.
Pfam PF13889: Chromosome segregation during meiosis (family)
The proteins come from eukaryotes, plants and animals, and are necessary for chromosome segregation during meiosis.
Pfam PF08561: Mitochondrial ribosomal protein L37 (family)
This family includes yeast MRPL37 a mitochondrial ribosomal protein.
Pfam PF01783: Ribosomal L32p protein family (family)
This entry represents the 50S large ribosomal subunit protein bL32 family. This family is found in prokaryotes and eukaryotic organelles. Structurally well characterised protein as a part of ribosome particle .
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 PF10327: Serpentine type 7TM GPCR chemoreceptor Sri (family)
Chemoreception is mediated in Caenorhabditis elegans by members of the seven-transmembrane G-protein-coupled receptor class (7TM GPCRs) of proteins which are of the serpentine type. Sri is part of the Str superfamily of chemoreceptors. Chemoperception is one of the central senses of soil nematodes like C. elegans which are otherwise 'blind' and 'deaf'.
Pfam PF22585: Sialidase-like, CBM domain (domain)
This entry represents a carbohydrate binding module (CBM) found in a group of uncharacterised bacterial proteins.
Pfam PF16788: ATF-interacting protein binding domain (family)
ATF7IP-BD is a short conserved region of activating transcription factor 7-interacting protein 1 found in higher eukaryotes. This domain appears to bind several key proteins such as TFIIE-alpha and TFIIE-beta as well the transcriptional regulator Sp1 which are part of the transcriptional machinery.
Pfam PF20431: E motif (repeat)
This entry represents the E motif found in plant pentatricopeptide repeat (PPR) proteins which contain a DYW deaminase domain. The DYW domain is required for RNA editing, a process that deaminates specific cytidines to uridines. This motif, together with the E+ motif, precedes the DYW domain and, although their role is not clear, they are essential in the RNA editing reaction. The E/E+ motifs may contain two degenerate PPR motifs that could be involved in RNA or protein binding.
Pfam PF20072: Domain of unknown function (DUF6468) (domain)
This domain of unknown function is found in uncharacterised proteins predominantly from Alphaproteobacteria but it is also present in some sequences from eukaryotes. This domain is approximately 75 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 PF12847: Methyltransferase domain (domain)
Protein in this family function as methyltransferases.
Pfam PF21529: Gloven 1/2 (family)
This entry represents a group of plant proteins, including GLV1 and GLV22 (also known as RGF9) from Arabidopsis. GLV2 is a signalling peptide (root growth factor) that regulates the pattern of root growth and lateral root development by modulating the length and the number of cortical cells in the root apical meristem (RAM), and the anticlinal asymmetric cell divisions in lateral root initiation cells. It is also involved in the regulation of hypocotyl bending and root gravitropism, probably by influencing the formation of auxin gradients. In general, RGFs are required for maintenance of the root stem cell niche and transit amplifying cell proliferation in Arabidopsis.
Pfam PF16913: Purine nucleobase transmembrane transport (family)
PUNUT is a family of largely plant and fungal purine transporters.  Most members are 10-pass transmembrane proteins, and they belong to the drug/metabolite transporter (dmt) superfamily. The plant vascular system transports nucleobases and their derivatives such as cytokinins and caffeine by a common H+-coupled high-affinity purine transport system; the PUNUT family members carry out this transport.
Pfam PF12398: Receptor serine/threonine kinase (family)
This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with [pfam:PF00954], [pfam:PF01453], [pfam:PF00069], [pfam:PF08276]. There is a conserved ELPL 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 PF12292: Protein of unknown function (DUF3624) (family)
This family of proteins is found in bacteria. Proteins in this family are approximately 90 amino acids in length. There is a conserved GRC 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 PF16283: Domain of unknown function (DUF4929) (family)
This family consists of uncharacterized proteins around 400 residues in length and is mainly found in various species, such as Bacteroides, Capnocytophaga and Prevotella. The function of this family is unknown.
Pfam PF05458: Cd27 binding protein (Siva) (family)
Siva binds to the CD27 cytoplasmic tail. It has a DD homology region, a box-B-like ring finger, and a zinc finger-like domain. Overexpression of Siva in various cell lines induces apoptosis, suggesting an important role for Siva in the CD27-transduced apoptotic pathway. Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosis. Indeed, the unique amphipathic helical region (SAH) present in Siva-1 is required for its binding to BCL-X(L) and sensitising cells to UV radiation. Natural complexes of Siva-1/BCL-X(L) are detected in HUT78 and murine thymocyte, suggesting a potential role for Siva-1 in regulating T cell homeostasis. This family contains both Siva-1 and the shorter Siva-2 lacking the sequence coded by exon 2. It has been suggested that Siva-2 could regulate the function of Siva-1.
Pfam PF23469: KH-domain (domain)
This entry represents a likely RNA-binding KH domain.
Pfam PF24777: Domain of unknown function (DUF7700) (domain)
This domain is usually found in tandem in uncharacterised bacterial proteins. It is predicted to adopt a globular structure consisting of a curved anti-parallel beta-sheet and alpha helices packed on one side of it. It contains highly conserved aspartate and histidine residues that may constitute a metal binding site.
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 PF20264: DUF4784 N-terminal Ig-like domain (domain)
This is a family of uncharacterised proteins from Bacteroidetes. This domain is found to the N-terminus of a WD40-like domain in DUF4784 family protein.
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 PF18689: Primase X (domain)
This domain is found in non-catalytic subunit of the archaeal eukaryotic-type primase, PriX. Detailed sequence analysis combined with structural analysis of a truncated PriX protein from the hyperthermophilic archaeon Sulfolobus solfataricus shows that, PriX is essential for the survival of the organism and that it is homologous to the C-terminal domain of archaeal and eukaryotic large primase subunits PriL. Highly conserved PriX homologues are present in many members of the phylum Crenarchaeota.
Pfam PF14132: Domain of unknown function (DUF4299) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are typically between 275 and 313 amino acids in length. There are two conserved sequence motifs: RGF and DAY. There are two completely conserved residues (P and D) that may be functionally important.
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 PF18166: Predicted pPIWI-associating nuclease (domain)
Predicted nuclease effector domain associating with prokaryotic PIWI-centered conflict systems.
Pfam PF22920: UvrC Ribonuclease H-like domain (domain)
This entry represents an RNaseH-like domain found in the UvrC protein. Nucleotide excision repair (NER) is a conserved DNA repair pathway that enables the repair of chemically and structurally distinct DNA lesions. In prokaryotes, the UvrA, UvrB and UvrC proteins mediate NER in a multistep, ATP-dependent reaction. UvrC catalyses the first incision on the fourth or fifth phosphodiester bond 3' and on the eighth phosphodiester bond 5' from the damage that is to be excised.
Pfam PF13189: Cytidylate kinase-like family (domain)
This family includes enzymes related to cytidylate kinase.
Pfam PF11646: Protein of unknown function DUF3258 (family)
This viral family are possible phage integrase proteins 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 PF10244: Mitochondrial ribosomal subunit (family)
MRP-L51 is a family of small proteins from the intact 55 S mitochondrial ribosome. It has otherwise been referred to as bMRP-64. The exact function of this family is not known.
Pfam PF13809: Tubulin like (family)
Many of the residues conserved in Tubulin, [pfam:PF00091], are also highly conserved in this family.
Pfam PF16792: Phage tail base-plate attachment protein N-terminal barrel domain (domain)
Caudo_bapla16 is a family of ORF16 tail-phage P2-like proteins that forms part of the base-plate at the tip of the phage tail. The whole base-plate complex is involved in host recognition and attachment, and consists of several proteins derived from consecutive open-reading-frames.  This entry represents the N-terminal RIFT barrel domain.
Pfam PF21687: Type II secretion system (T2SS), protein K (domain)
Members of this family are involved in the Type II protein secretion system. The T2SK family includes proteins such as ExeK, PulK, OutX and XcpX. They consist of two tandem SAM-like domains, this entry represents the first one.
Pfam PF15446: PHD/FYVE-zinc-finger like domain (domain)
This family appears to be a combination domain of several consecutive zinc-binding regions.
Wikipedia: The PHD finger was discovered in 1993 as a Cys4-His-Cys3 motif in the plant homeodomain proteins HAT3.1 in Arabidopsis and maize ZmHox1a. 
The PHD zinc finger motif resembles the metal binding RING domain (Cys3-His-Cys4) and FYVE domain. It occurs as a single finger, but often in clusters of two or three, and it also occurs together with other domains, such as the chromodomain and the bromodomain.
Pfam PF12590: Acyl-ATP thioesterase (family)
This domain family is found in bacteria and eukaryotes, and is typically between 120 and 131 amino acids in length. The family is found in association with [pfam:PF01643]. The plant acyl-acyl carrier protein (ACP) thioesterases (TEs) have roles in fatty acid synthesis.
Pfam PF01367: 5'-3' exonuclease, C-terminal SAM fold (domain)
This entry represents the H3TH (helix-3-turn-helix) domain of the 5'-3' exonuclease (53EXO) of mutli-domain DNA polymerase I and single domain protein homologues. Taq (Thermus aquaticus) DNA polymerase I contains a polymerase domain for synthesizing a new DNA strand and a 53EXO domain for cleaving RNA primers or damaged DNA strands . Taq's 53EXO recognizes and endonucleolytically cleaves a structure-specific DNA substrate that has a bifurcated downstream duplex and an upstream template-primer duplex that overlaps the downstream duplex by 1 bp .
Pfam PF06793: Uncharacterised protein family (UPF0262) (family)
This protein family is functionally uncharacterised.
Pfam PF12203: Glutamine rich N terminal domain of histone deacetylase 4 (family)
This domain is found in eukaryotes, and is approximately 90 amino acids in length. The family is found in association with [pfam:PF00850]. The domain forms an alpha helix which complexes to form a tetramer. The glutamine rich domains have many intra- and inter-helical interactions which are thought to be involved in reversible assembly and disassembly of proteins. The domain is part of histone deacetylase 4 (HDAC4) which removes acetyl groups from histones. This restores their positive charge to allow stronger DNA binding thus restricting transcriptional activity.
Pfam PF11125: Bacteriophage MS2, lysis protein (family)
This entry represents putative lysis proteins from Bacteriophage MS2 and Bacteriophage BZ13. The bacteriophage MS2 lysin protein swiss:C0M1L5 was identified as an overlapping cistron in the bacteriophage MS2 RNA. This proteins induces the formation of specific membrane adhesion sites between the inner and outer membranes, apparently leading to host cell lysis. Lysis may be performed via activation of host murein hydrolases.
Pfam PF16565: Phospholipase D-like domain at C-terminus of MIT (domain)
MIT_C is the C-terminal domain of MIT-containing proteins, [pfam:PF04212]. It contains an unanticipated phospholipase d fold (PLD fold) that binds avidly to phosphoinositide-containing membranes. It is conserved in eukaryotes, though not fungi and plants, and some bacteria.
Pfam PF00507: NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 (family)
This family contains chain 3 of the NADH-ubiquinone / plastoquinone oxidoreductase.
Wikipedia: Respiratory complex I, EC 7.1.1.2 is the first large protein complex of the respiratory chains of many organisms from bacteria to humans. It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10) and translocates protons across the inner mitochondrial membrane in eukaryotes or the plasma membrane of bacteria.
Pfam PF06209: Cofactor of BRCA1 (COBRA1) (family)
This family consists of several cofactor of BRCA1 (COBRA1) like proteins. It is thought that COBRA1 along with BRCA1 is involved in chromatin unfolding. COBRA1 is recruited to the chromosome site by the first BRCT repeat of BRCA1, and is itself sufficient to induce chromatin unfolding. BRCA1 mutations that enhance chromatin unfolding also increase its affinity for, and recruitment of, COBRA1. It is thought that that reorganisation of higher levels of chromatin structure is an important regulated step in BRCA1-mediated nuclear functions.
Pfam PF13122: Protein of unknown function (DUF3977) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are approximately 80 amino acids in length.
Pfam PF11721: Malectin domain (domain)
Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186.  NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan.
Pfam PF08703: PLC-beta C terminal (domain)
This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.
Pfam PF16637: Putative zinc-finger between two C2H2 zinc-fingers on Patz (disordered)
zf-C2H2_assoc3 is a partially unstructured region on Patz or POZ-, AT hook-, and zinc finger-containing proteins of higher eukaryotes. It lies between the two C2H2-type zinc-fingers towards the C-terminus of these proteins and may well be an unusual zinc-finger itself.
Pfam PF08164: Apoptosis-antagonizing transcription factor, C-terminal (domain)
This C terminal domain is found in traube proteins. This is the domain of the AATF proteins that interacts with BLOS2 or Ceap, that functions as an adaptor in processes such as protein and vesicle processing and transport, and perhaps transcription.
Pfam PF00268: Ribonucleotide reductase, small chain (domain)
Ribonucleotide reductase (RNR), also known as ribonucleoside diphosphate reductase, (1.17.4.1)  catalyses the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides: 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O = ribonucleoside diphosphate + reduced thioredoxin

RNR provides the precursors necessary for DNA synthesis. RNRs divide into three classes on the basis of their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, bacteriophage and viruses, use a diiron-tyrosyl radical, Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria and bacteriophage, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes.
Wikipedia: Ribonucleotide reductase (RNR), also known as ribonucleoside diphosphate reductase, is an enzyme that catalyzes the formation of deoxyribonucleotides from ribonucleotides. It catalyzes this formation by removing the 2'-hydroxyl group of the ribose ring of nucleoside diphosphates. This reduction produces deoxyribonucleotides. Deoxyribonucleotides in turn are used in the synthesis of DNA. The reaction catalyzed by RNR is strictly conserved in all living organisms. Furthermore, RNR plays a critical role in regulating the total rate of DNA synthesis so that DNA to cell mass is maintained at a constant ratio during cell division and DNA repair. A somewhat unusual feature of the RNR enzyme is that it catalyzes a reaction that proceeds via a free radical mechanism of action. The substrates for RNR are ADP, GDP, CDP and UDP. dTDP is synthesized by another enzyme from dTMP.
Pfam PF13057: Protein of unknown function (DUF3919) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are typically between 251 and 262 amino acids in length. There is a conserved YLNG sequence motif.
Pfam PF00604: Influenza RNA polymerase PB2 CAP binding domain (domain)
Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding and endonuclease domains required for transcription initiation by cap-snatching. This entry represents the CAP binding domain.