SII-SWORD/CoKE huggingface dataset:
Pfam PF11887: Cholesterol uptake porter CUP1 of Mce4, putative (family)
Mce4_CUP1 is a family of putative Mce4 transporters of cholesterol.  The domain is found associated with [pfam:PF02470]. The full TCDB classification for this family in conjunction with PF02470 is TC:3.A.1.27.4.
Pfam PF06946: Bacteriophage A118-like holin, Hol118 (family)
This family consists of several Listeria bacteriophage holin proteins and related bacterial sequences. Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the build up of a holin oligomer which causes the lysis.
Pfam PF23788: EDRF1 N-terminal (domain)
This entry represents the N-terminal domain of EDRF1 (Erythroid differentiation-related factor 1), a transcription factor involved in erythroid differentiation. It is involved in transcriptional activation of the globin gene.
Pfam PF16808: Coiled-coil N-terminus of cGMP-dependent protein kinase (coiled_coil)
PKcGMP_CC is the N-terminal coiled-coil, dimerisation, domain of cGMP-protein kinases.
Pfam PF13083: KhpA/KhpB, KH domain (domain)
The K homology domain is a common RNA-binding motif present in one or multiple copies in both prokaryotic and eukaryotic regulatory proteins. These motifs may act cooperatively to bind RNA in the case of multiple motifs, or independently in the case of single KH motif proteins. The structure of the prokaryotic KH domain consists of a two-layer alpha/beta fold in the arrangement alpha/beta(2)/alpha/beta. This entry represents the KH domain from RNA-binding protein KhpA and KhpB (also known as Jag or EloR). KhpA is a single-KH domain protein while KhpB also has a Jag-N domain ([pfam:PF14804]) of unknown function and a R3H domain ([pfam:PF01424]) at the C-terminal.
Wikipedia: The K Homology (KH) domain is a protein domain that was first identified in the human heterogeneous nuclear ribonucleoprotein (hnRNP) K. An evolutionarily conserved sequence of around 70 amino acids, the KH domain is present in a wide variety of nucleic acid-binding proteins. The KH domain binds RNA, and can function in RNA recognition. It is found in multiple copies in several proteins, where they can function cooperatively or independently. For example, in the AU-rich element RNA-binding protein KSRP, which has 4 KH domains, KH domains 3 and 4 behave as independent binding modules to interact with different regions of the AU-rich RNA targets. The solution structure of the first KH domain of FMR1 and of the C-terminal KH domain of hnRNP K determined by nuclear magnetic resonance (NMR) revealed a beta-alpha-alpha-beta-beta-alpha structure. Autoantibodies to NOVA1, a KH domain protein, cause paraneoplastic opsoclonus ataxia. The KH domain is found at the N-terminus of the ribosomal protein S3. This domain is unusual in that it has a different fold compared to the normal KH domain.
Pfam PF06889: Protein of unknown function (DUF1266) (family)
This family consists of several hypothetical bacterial proteins of around 235 residues in length. Members of this family seem to be found exclusively in the Enterobacteria Salmonella typhimurium and Escherichia coli. The function of this family is unknown.
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 PF19738: Family of unknown function (DUF6227) (family)
This entry represents a member of a biosynthetic gene cluster (BGC). This BGC (BGC0000118) is described by MIBiG as an example of the following biosynthetic class, polyketide. It includes a member from the pactamycin biosynthetic gene cluster from Streptomyces pactum. This family appears to be predominantly found in Actinobacteria.
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 PF23136: Domain of unknown function (DUF7051) (repeat)
This is a domain of unknown function mostly found in organisms within the Trypanosoma genus. This domain adopt a multiple helical bundle fold.
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 PF05031: Iron Transport-associated domain (domain)
NEAT domains are heme and/or hemoprotein-binding modules highly conserved in secondary structure. They have roles in hemoprotein binding, heme extraction and  heme transfer
Pfam PF09212: Carbohydrate binding module 27 (domain)
Members of this family are carbohydrate binding modules that bind to beta-1, 4-manno-oligosaccharides, carob galactomannan, and konjac glucomannan, but not to cellulose (insoluble and soluble) or soluble birchwood xylan. They adopt a beta sandwich structure comprising 13 beta strands with a single, small alpha-helix and a single metal atom.
Wikipedia: In molecular biology, a carbohydrate-binding module (CBM) is a protein domain found in carbohydrate-active enzymes. The majority of these domains have carbohydrate-binding activity. Some of these domains are found on cellulosomal scaffoldin proteins. CBMs were previously known as cellulose-binding domains. CBMs are classified into numerous families, based on amino acid sequence similarity. There are currently 64 families of CBM in the CAZy database.
Pfam PF13300: Domain of unknown function (DUF4078) (family)
This family is found from fungi to humans, but its exact function is not known.
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 PF19950: Family of unknown function (DUF6412) (family)
This entry represents a member of a biosynthetic gene cluster (BGC). This BGC (BGC0001514) is described by MIBiG as an example of the following biosynthetic class, other (unspecified), in particular the aristeromycin biosynthetic gene cluster from Streptomyces  citricolor. This family appears to be predominantly found in  Actinobacteria.
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 PF21026: Schlafen, GTPase-like domain (domain)
This is a domain found in groups II and III of Schlafen (SLFN), protein which follows the AlbA_2 domain ([pfam:PF04326]). In group II this is the C-terminal domain, while in group III members it localizes in the central region, followed by a C-terminal helicase domain ([pfam:PF09848]). This domain has been described as a GTPase-like domain and it contains the SLFN-specific SWADL motif. SLFN proteins are involved in the control of cell proliferation, induction of immune responses, and the regulation of viral replication. Mouse and human members are regulated by interferons. In SLFN12, this is the C-terminal domain which contains crucial residues for interaction with PDE3A. By analogy with dynamin and MxB, this domain in SLFN12 may contribute to chromatin and actin cytoskeleton interactions, involved in cell differentiation. SLFN proteins share common domains and a high degree of homology, however, they have specific and sometimes, opposing effects in some cancer types.
Pfam PF07178: TraL protein (family)
This family consists of several bacterial TraL proteins. TraL is a predicted peripheral membrane protein which is thought to be involved in bacterial sex pilus assembly. The exact function of this family is unclear.
Pfam PF00056: lactate/malate dehydrogenase, NAD binding domain (domain)
L-lactate dehydrogenases are metabolic enzymes which catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family.  Malate dehydrogenases catalyse the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. N-terminus (this family) is a Rossmann NAD-binding fold. C-terminus is an unusual alpha+beta fold.
Wikipedia: Lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells. LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NAD+ to NADH and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.
Pfam PF23947: Domain of unknown function (DUF7281) (domain)
This domain is found C-terminal in uncharacterised bacterial proteins. It shares some similarity to the C-terminal domain of JetD [[pfam:PF09983]].
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 PF04247: Invasion gene expression up-regulator, SirB (family)
SirB up-regulates Salmonella typhimurium invasion gene transcription. It is, however, not essential for the expression of these genes. Its function is unknown.
Pfam PF13383: Methyltransferase domain (family)
This family appears to be a methyltransferase domain.
Pfam PF07654: Immunoglobulin C1-set domain (domain)
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulphide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three (in alpha, delta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; IPR013106), C1-set (constant-1; IPR003597), C2-set (constant-2; IPR008424) and I-set (intermediate; IPR013098) . Structural studies have shown that these domains share a common core Greek-key Î²-sandwich structure, with the types differing in the number of strands in the Î²-sheets as well as in their sequence patterns .

Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions, including cell-cell recognition, cell-surface receptors, muscle structure and the immune system .
This entry represents C1-set domains, which are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system, such as in immunoglobulin light and heavy chains, in the major histocompatibility complex (MHC) class I and II complex molecules , and in various T-cell receptors.
Wikipedia: C1-set domains are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system, such as in immunoglobulin light and heavy chains, in the major histocompatibility complex (MHC) class I and II complex molecules, and in various T-cell receptors.
Pfam PF19949: Family of unknown function (DUF6411) (family)
This entry represents a member of a biosynthetic gene cluster (BGC). This BGC (BGC0001740) is described by MIBiG as an example of the following biosynthetic classes, NRP (non-ribosomal peptide) and polyketide, in particular the phthoxazolin biosynthetic gene cluster from Streptomyces avermitilis.
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 PF01311: Bacterial export proteins, family 1 (family)
This family includes the following members;     FliR, MopE, SsaT, YopT, Hrp, HrcT and SpaR All of these members export proteins, that do not possess signal  peptides, through the membrane.  Although the proteins that these exporters move may be different, the exporters are thought to  function in similar ways.
Pfam PF21138: Helicase SMUBP-2/HCS1, 1B domain (domain)
Proteins in this entry belong to the DNA2/NAM7 helicase family and includes SMUBP-2 (also known as IGHMBP2) from mammals and HCS1 (also known as DNA polymerase alpha-associated DNA helicase A) from yeasts. This entry represents the 1B domain consisting of a short alpha-helix and a beta-barrel. This domain forms the RNA-binding channel together with 1A, 2A and 1C domains. Domains 1B and 1C directly interact with the 3'-end of RNA.
Pfam PF22292: Domain of unknown function (DUF6965) (domain)
This entry represents a family of uncharacterised proteins which are predicted to form a small three helical bundle containing a beta hairpin between helices 1 and 2.
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 PF16798: Domain of unknown function (DUF5069) (domain)
The function of DUF5069 is not known.
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 PF13910: Domain of unknown function (DUF4209) (domain)
This short domain is found in bacteria and eukaryotes, though not in yeasts or Archaea. It carries a highly conserved RNxxxHG 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 PF00752: XPG N-terminal domain (family)
Xeroderma pigmentosum (XP)  is a human autosomal recessive disease, characterised by a high incidence of sunlight-induced skin cancer. People's skin cells with this condition are hypersensitive to ultraviolet light, due to defects in the incision step of DNA excision repair. There are a minimum of seven genetic complementation groups involved in this pathway: XP-A to XP-G. XP-G is one of the most rare and phenotypically heterogeneous of XP, showing anything from slight to extreme dysfunction in DNA excision repair . XP-G can be corrected by a 133 Kd nuclear protein, XPGC . XPGC is an acidic protein that confers normal UV resistance in expressing cells . It is a magnesium-dependent, single-strand DNA endonuclease that makes structure-specific endonucleolytic incisions in a DNA substrate containing a duplex region and single-stranded arms . XPGC cleaves one strand of the duplex at the border with the single-stranded region .

XPG (ERCC-5) belongs to a family of proteins that includes RAD2 from Saccharomyces cerevisiae (Baker's yeast) and rad13 from Schizosaccharomyces pombe (Fission yeast), which are single-stranded DNA endonucleases ; mouse and human FEN-1, a structure-specific endonuclease; RAD2 from fission yeast and RAD27 from budding yeast; fission yeast exo1, a 5'-3' double-stranded DNA exonuclease that may act in a pathway that corrects mismatched base pairs; yeast DHS1, and yeast DIN7. Sequence alignment of this family of proteins reveals that similarities are largely confined to two regions. The first is located at the N-terminal extremity (N-region) and corresponds to the first 95 to 105 amino acids. The second region is internal (I-region) and found towards the C terminus; it spans about 140 residues and contains a highly conserved core of 27 amino acids that includes a conserved pentapeptide (E-A-[DE]-A-[QS]). It is possible that the conserved acidic residues are involved in the catalytic mechanism of DNA excision repair in XPG. The amino acids linking the N-and I-regions are not conserved.
This entry represents the N-terminal of XPG.
Wikipedia: In molecular biology the protein domain XPG refers to, in this case, the N-terminus of XPG. The XPG protein can be corrected by a 133 kDa nuclear protein, XPGC. XPGC is an acidic protein that confers normal ultraviolet (UV) light resistance. It is a magnesium-dependent, single-strand DNA endonuclease that makes structure-specific endonucleolytic incisions in a DNA substrate containing a duplex region and single-stranded arms. XPGC cleaves one strand of the duplex at the border with the single-stranded region.
Pfam PF20418: Alphaherpesvirus glycoprotein E N-terminal (domain)
Glycoprotein E (gE) of Alphaherpesvirus forms a complex with glycoprotein I (gI) ([pfam:PF01688]), functioning as an immunoglobulin G (IgG) Fc binding protein. gE is involved in virus spread but is not essential for propagation. This entry represents the N-terminal domain of gE, which interacts with gI.
Pfam PF00362: Integrin beta chain VWA domain (domain)
Integrins have been found in animals and their homologues have also been found in cyanobacteria, probably due to horizontal gene transfer. This domain corresponds to the integrin beta VWA domain.
Wikipedia: Integrins are transmembrane receptors that help cell–cell and cell–extracellular matrix (ECM) adhesion. Upon ligand binding, integrins activate signal transduction pathways that mediate cellular signals such as regulation of the cell cycle, organization of the intracellular cytoskeleton, and movement of new receptors to the cell membrane. The presence of integrins allows rapid and flexible responses to events at the cell surface.
Pfam PF12302: Protein of unknown function (DUF3629) (family)
This family of proteins is found in eukaryotes. Proteins in this family are typically between 256 and 292 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 PF18703: MALT1 Ig-like domain (domain)
This is an Immunoglobulin like domain which can be found in the mucosa-associated lymphoid tissue lymphoma translocation 1 (MALT1) paracaspase. Malt1 is a key component of the Carma1/Bcl10/MALT1 signalosome and is critical for NF-kB signaling in multiple contexts. The MALT1 C-terminal Ig domain is suggested to recruit key factors to promote NF-kB activation. The It is also proposed to undergo Lys63-linked ubiquitylation via TRAF6 in potentially nine different lysines to recruit the IKK complex.
Pfam PF11614: IG-like fold at C-terminal of FixG, putative oxidoreductase (domain)
This domain is part of a transmembrane protein, FixG, itself part of the FixGHIS operon closely associated with the FixNOPQ operon that is the symbiotically essential cbb3-type haem-copper oxidase complex. FixG expression is induced by oxygen-deprivation. This C-terminal domain adopts an E-set Ig-like fold.
Pfam PF21576: T6SS, Immunity protein Tgi2PP (family)
This protein family includes Immunity protein Tgi2PP from Pseudomonas fluorescens (PFL_3036), the immunity component of a effector immunity pair secreted by the type VI secretion system (T6SS) of this bacteria. Its structure consists of a short N-terminal 3-10 helix and a central five-stranded beta-sheet flanked by three alpha- helices.
Pfam PF09414: RNA ligase (family)
This is a family of RNA ligases. The enzyme repairs RNA strand breaks in nicked DNA:RNA and RNA:RNA but not in DNA:DNA duplexes.
Pfam PF16660: PHD finger protein 20-like protein 1 (disordered)
PHD20L1_u1 is a region of natively unstructured but highly conserved sequence on a set of higher eukaryotic PHD finger protein 20-like protein 1 like proteins.  The function is not known.
Pfam PF06369: Sea anemone cytotoxic protein (family)
Sea anemones are a rich source of cytotoxic proteins. Cytolysins comprise a group of more than 30 highly basic proteins with molecular masses of about 20 kDa. Cytolysins isolated from the sea anemone, Heteractis magnifica, include magnificalysin I (HMg I), magnificalysin II (HMg II) and Heteractis magnifica toxin (HMgtxn). These are highly homologous at their N-terminals. HMg I and II have molecular masses of approximately 19 kDa, and pI values of 9.4 and 10.0, respectively. Cytolysins isolated from other sea anemones Actinia tenebrosa (Tenebrosin-C, TN-C), Actinia equina (Equinatoxin, EqT) and Stichodactyla helianthus (ShC) exhibit pore-forming, haemolytic, cytotoxic, and heart stimulatory activities.
Wikipedia: In molecular biology, the sea anemone cytotoxic proteins are lethal pore-forming proteins, known collectively as actinoporins, a sub-class of cytolysins. There are several different groups of cytolysins based on their structure and function. This entry represents the most numerous group, the 20kDa highly basic peptides. These cytolysins form cation-selective pores in sphingomyelin-containing membranes. Examples include equinatoxins, sticholysins, magnificalysins, and tenebrosins, which exhibit pore-forming, haemolytic, cytotoxic, and heart stimulatory activities.