SII-SWORD/CoKE huggingface dataset:
Pfam PF10775: ATP synthase complex subunit h (family)
Subunit h is a component of the yeast mitochondrial F1-F0 ATP synthase. It is essential for the correct assembly and functioning of this enzyme. Subunit h occupies a central place in the peripheral stalk between the F1 sector and the membrane.
Pfam PF18325: Fatty acid synthase subunit alpha Acyl carrier domain (domain)
This is the acyl carrier domain (ACP) found in fatty acid synthase subunit alpha (FAS2) [ec:2.3.1.86] .The fungal type I fatty acid synthase (FAS) is a 2.6 MDa multienzyme complex, catalyzing all necessary steps for the synthesis of long acyl chains. To be catalytically competent, the FAS must be activated by a posttranslational modification of the central acyl carrier domain (ACP) by an intrinsic phosphopantetheine transferase (PPT).
Pfam PF00435: Spectrin repeat (domain)
Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure.  These include spectrin, alpha-actinin and dystrophin.  The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Wikipedia: Spectrin repeats are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin, dystrophin and more recently the plakin family. The spectrin repeat forms a three-helix bundle. These conform to the rules of the heptad repeat. Spectrin repeats give rise to linear proteins. This however may be due to sample bias in which linear and rigid structures are more amenable to crystallization. There are hints however, that some proteins harbouring spectrin repeats may also be flexible. This is most likely due to specifically evolved functional purposes.
Pfam PF02553: Cobalt transport protein component CbiN (family)
CbiN is part of the active cobalt transport system involved in uptake of cobalt in to the cell involved with cobalamin biosynthesis (vitamin B12).  It has been suggested that CbiN may function as the periplasmic binding protein component of the active cobalt transport  system.
Wikipedia: Cobalamin biosynthesis is the process by which bacteria and archea make cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which it is used by enzymes in both the producing organisms and other species, including humans who acquire it through their diet.
Pfam PF04906: Tweety (family)
The tweety (tty) gene has not been characterised at the protein level. However, it is thought to form a membrane protein with five potential membrane-spanning regions. A number of potential functions have been suggested in.
Pfam PF00098: Zinc knuckle (domain)
The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag  proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.
Wikipedia: A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn2+) which stabilizes the fold. It was originally coined to describe the finger-like appearance of a hypothesized structure from the African clawed frog (Xenopus laevis) transcription factor IIIA. However, it has been found to encompass a wide variety of differing protein structures in eukaryotic cells. Xenopus laevis TFIIIA was originally demonstrated to contain zinc and require the metal for function in 1983, the first such reported zinc requirement for a gene regulatory protein followed soon thereafter by the Krüppel factor in Drosophila. It often appears as a metal-binding domain in multi-domain proteins.
Pfam PF05963: Cytomegalovirus US3 protein (family)
US3 of human cytomegalovirus is an endoplasmic reticulum resident transmembrane glycoprotein that binds to major histocompatibility complex class I molecules and prevents their departure. The endoplasmic reticulum retention signal of the US3 protein is contained in the luminal domain of the protein.
Pfam PF18375: CDH1/2 SANT-Helical linker 1 (domain)
CDH1 is an ATP-dependent chromatin-remodelling factor and plays an important role in regulating nucleosome assembly and mobilization. CHD1 consists of double chromodomain, SNF2-related ATPase domain, and a C-terminal DNA-binding domain. The DNA-binding domain contains SANT (Swi3, Ada2, N-CoR, TFIIIB) and SLIDE (SANT-like ISWI) domains in its C-terminal region. SANT domains are structurally related to Myb-like domains are common motifs found in chromatin interacting proteins. Deletion of individual SANT or SLIDE domains in CDH1 does not significantly affect nucleosome binding, but combined deletion of both domains severely compromise binding, suggesting that the SANT-SLIDE motif recognizes DNA/nucleosomes as a single cooperative unit. SANT sequences of Chd1 proteins are the most distantly relation group of sequences relation to other SANT/Myb sequences, and are more diverse than other SANT proteins. The SANT and SLIDE regions are well conserved in both Chd1 and ISWI (imitation switch) remodelling enzymes. This domain comprises the SANT region and the helical linker region 1 (HL1).
Pfam PF00633: Helix-hairpin-helix motif (conserved_site)
The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.
Pfam PF10419: TFIIIC subunit triple barrel domain (domain)
This is a family of proteins subunits of TFIIIC.  TFIIIC in yeast and humans is required for transcription of tRNA and 5 S RNA genes by RNA polymerase III.  Yeast members of this family are fused to phosphoglycerate mutase domain.
Pfam PF00052: Laminin B (Domain IV) (domain)
Laminin is a large molecular weight glycoprotein present only in basement membranes in almost every animal tissue. Each laminin is a heterotrimer assembled from alpha, beta and gamma chain subunits, secreted and incorporated into cell-associated extracellular matrices. The laminins can self-assemble, bind to other matrix macromolecules, and have unique and shared cell interactions mediated by integrins, dystroglycan, and other receptors. Through these interactions, laminins critically contribute to cell differentiation, shape and movement, maintenance of tissue phenotypes, and promotion of tissue survival .

The different laminin chains share a 600-residue domain I/II which oligomerises into a rod-like coiled-coil structure forming the long arm of laminins. The N-terminal short arms consist of rod-like elements (domain III and V) formed by tandem arrays of laminin-type EGF modules and several globular domains: domains IV and domain VI (laminin N-terminal). All alpha chains share a unique C-terminal G domain which consists of five laminin G modules . Laminin IV domain is also found in the perlecan protein, an integral component of basement membranes, which serves also as an attachment substrate for cells, but it is not found in short laminin chains (alpha4 or beta3). The function of this domain is not yet known.
Wikipedia: Laminins are a family of glycoproteins of the extracellular matrix of all animals. They are major constituents of the basement membrane, namely the basal lamina. Laminins are vital to biological activity, influencing cell differentiation, migration, and adhesion.
Pfam PF05295: Luciferase/LBP N-terminal domain (domain)
This family consists of a presumed N-terminal domain that is conserved between dinoflagellate luciferase and luciferin binding proteins. Luciferase is involved in catalysing the light emitting reaction in bioluminescence and luciferin binding protein (LBP) is known to bind to luciferin (the substrate for luciferase) to stop it reacting with the enzyme and therefore switching off the bioluminescence function. The expression of these two proteins is controlled by a circadian clock at the translational level, with synthesis and degradation occurring on a daily basis. However This domain is not the catalytic part of the protein.  It has been suggested that this region may mediate an interaction between LBP and Luciferase or their association with the vacuolar membrane.
Wikipedia: Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein. The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the substrate and enzyme, respectively. Both words are derived from the Latin word lucifer, meaning "lightbearer", which in turn is derived from the Latin words for "light" (lux) and "to bring or carry" (ferre).
Pfam PF15334: Aurora kinase A and ninein interacting protein (family)
AIB is a family of eukaryotic proteins necessary for the adequate functioning of Aurora-A, a protein involved in chromosome alignment, centrosome maturation, mitotic spindle assembly and aspects of tumourigenesis. AIB is likely to act as a regulator of Aurora-A activity.
Pfam PF01064: Activin types I and II receptor domain (domain)
This Pfam entry consists of both TGF-beta receptor types. This is an alignment of the hydrophilic cysteine-rich  ligand-binding domains, Both receptor types, (type I and II) posses a 9 amino acid cysteine box, with the the consensus CCX{4-5}CN. The type I receptors also possess 7 extracellular residues preceding the cysteine box.
Wikipedia: An Activin receptor is a receptor which binds activin. These proteins are receptor-type kinases of Ser/Thr type, which have a single transmembrane domain and a specific hydrophilic Cys-rich ligand-binding domain.
Pfam PF22970: Domain of unknown function (DUF7028) (domain)
This domain is found in a group of uncharacterised proteins mainly from plants. It is predicted to adopt a globular structure that has significant sequence and structural similarity to MBD domains.
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 PF16728: Domain of unknown function (DUF5066) (domain)
The function of DUF5066 is not clear.
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 PF20859: Hypothetical protein RHA1_ro05818, N-terminal helical domain (domain)
This domain is found at the N terminus of Hypothetical protein RHA1_ro05818 from Rhodococcus jostii ([swissprot:Q0S4E1]). This protein is thought to be a thioesterase involved in the metabolism of cholate. This protein has a 4HBT domain ([pfam:PF03061]) at the C-terminal. The N-terminal domain shows an helical fold.
Pfam PF09340: Histone acetyltransferase subunit NuA4 (family)
The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast.  NuA4 complexes are highly conserved in eukaryotes and play primary roles in transcription, cellular response to DNA damage, and cell cycle control.
Wikipedia: The NuA4 histone acetyltransferase complex is a protein complex that has histone acetylase activity on chromatin, as well as ATPase, DNA helicase and structural DNA binding activities. The complex is thought to be involved in double-strand DNA break repair. Subunits of the human complex include HTATIP/TIP60, TRRAP, RUVBL1, RUVBL2, beta-actin and BAF53/ACTL6A. In yeast, the complex has 13 subunits, including the catalytic subunit Esa1.
Pfam PF09409: PUB domain (domain)
The PUB (also known as PUG) domain is found in peptide N-glycanase where it functions as a AAA ATPase binding domain. This domain is also found on other proteins linked to the ubiquitin-proteasome system.
Pfam PF20790: Reovirus VP3 protein, guanylyltransferase (GTase) (domain)
This domain family is found at the N-terminal end of Turret protein (TP), also known as VP3, from Reovirus. This GTase domain, responsible for the catalysis of the first step of RNA capping, consists of two subdomains, which form a deep and narrow cleft. This domain is rich in beta strands and adopts a pentameric assembly.
Pfam PF24954: Domain of unknown function (DUF7763) (domain)
This domain is found in uncharacterised proteins mainly from Streptococcus. It is predicted to adopt globular structure consisting of four alpha-helices.
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 PF16227: Domain of unknown function (DUF4886) (domain)
This domain is mainly found in uncharacterized proteins around 290 residues in length and is mainly found in various Bacteroides species. It has a curved central beta sheet flanked by helices. Distant homolog analysis showed it has a similarity with GDSL-like  Lipase/Acylhydrolase family. The function of this domain is still unknown.
Pfam PF21770: MGTC/SAPB C-terminal domain (domain)
This domain is found at the C-terminus of proteins that are members of MGTC/SAPB family. It adopts a ferredoxin-like fold and has a significant structural similarity to ACT-like domains. In contrast to the canonical ACT-like domains, this domain doesn't dimerize or bind to small molecules. It is probably involved in protein-protein interactions.
Pfam PF05667: CCDC22 protein coiled-coil region (coiled_coil)
Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the COMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologues from animals and plants.
Pfam PF21445: ADDB, N-terminal (domain)
ATP-dependent helicase/deoxyribonuclease subunit B (ADDB) forms a heterodimer with ADDA which acts as both an ATP-dependent DNA helicase and an ATP-dependent single-stranded exonuclease, acting in both directions. This entry represents the N-terminal domain of ADDB, which contains the Walker A motif involved in ATP binding.
Pfam PF09099: Quinohemoprotein amine dehydrogenase, alpha subunit domain III (domain)
Members of this family, which are predominantly found in the prokaryotic protein quinohemoprotein amine dehydrogenase, adopt an immunoglobulin-like beta-sandwich fold, with seven strands arranged into two beta sheets; the fold is possibly related to the immunoglobulin and/or fibronectin type III superfamilies. The precise function of this domain has not, as yet, been defined.
Pfam PF08005: PHR domain (domain)
This domain is called PHR as it was original found in the proteins PAM ([swissprot:O75592]), highwire ([swissprot:Q9NB71]) and RPM ([swissprot:Q17551]).  This domain can be duplicated in the highwire, PFAM and PRM sequence.                 The C-terminal region of the protein BTBD1 includes the PHR domain and is known to interact with Topoisomerase I, an enzyme which relaxes DNA supercoils.
Pfam PF20184: Family of unknown function (DUF6547) (family)
This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are typically between 116 and 127 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 PF21695: Transcription regulator GlnR, N-terminal domain (domain)
This domain is found at the N-terminal end of Transcription regulator GlnR from Amycolatopsis mediterranei and similar sequences predominantly found in actinobacteria. GlnR plays a key role in the global regulation of nitrogen metabolism. It belongs to the OmpR/PhoB subfamily. This domain shows five alternating beta-strands and alpha- helices that form a five-stranded parallel beta-sheet in the middle surrounded by two alpha-helices on one side and three on the other, showing great structure similarity with most of the known structures of the typical RR receiver domains. This domain is usually found associated with [pfam:PF00486].
Pfam PF15499: Ubiquitin-specific peptidase-like, SUMO isopeptidase (family)
Peptidase_C98 is a small family of SUMO - small ubiquitin-related modifier - isopeptidases found in eukaryotes. Reversible attachment of SUMO is an essential protein modification in all eukaryotic cells, The family neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase, and the invariant residues required for SUMO binding and cleavage, in UniProtKB:Q5W0Q7, are Cys-236, His-456 and Asp-472, all of which are fully conserved in the family. Member proteins are low-abundance proteins that colocalise with coilin in Cajal bodies. Peptidase_C98 depletion does not affect global sumoylation, but causes striking coilin mis-localisation and impairs cell proliferation, functions that are not dependent on the catalytic activity. Thus, Peptidase_C98 represents a third type of SUMO protease, with essential functions in Cajal body biology.
Pfam PF14709: double strand RNA binding domain from DEAD END PROTEIN 1 (domain)
A C-terminal domain in human dead end protein 1 (DND1_HUMAN) homologous to double strand RNA binding domains (PF00035, PF00333)
Wikipedia: 
RNA-binding proteins are proteins that bind to the double or single stranded RNA in cells and participate in forming ribonucleoprotein complexes.
RBPs contain various structural motifs, such as RNA recognition motif (RRM), dsRNA binding domain, zinc finger and others.
They are cytoplasmic and nuclear proteins. However, since most mature RNA is exported from the nucleus relatively quickly, most RBPs in the nucleus exist as complexes of protein and pre-mRNA called heterogeneous ribonucleoprotein particles (hnRNPs).
RBPs have crucial roles in various cellular processes such as: cellular function, transport and localization. They especially play a major role in post-transcriptional control of RNAs, such as: splicing, polyadenylation, mRNA stabilization, mRNA localization and translation. Eukaryotic cells express diverse RBPs with unique RNA-binding activity and protein–protein interaction. According to the Eukaryotic RBP Database (EuRBPDB), there are 2961 genes encoding RBPs in humans. During evolution, the diversity of RBPs greatly increased with the increase in the number of introns. Diversity enabled eukaryotic cells to utilize RNA exons in various arrangements, giving rise to a unique RNP (ribonucleoprotein) for each RNA. Although RBPs have a crucial role in post-transcriptional regulation in gene expression, relatively few RBPs have been studied systematically. It has now become clear that RNA–RBP interactions play important roles in many biological processes among organisms.
Pfam PF12322: T4 bacteriophage base plate protein (family)
The Baseplate Hub Assembly Protein family consists of chaperones that play a crucial role in the assembly of the baseplate's central hub during bacteriophage tail formation. These proteins are essential for the proper construction of the baseplate, which is a complex structure at the base of the bacteriophage tail. It serves as a platform for tail assembly and is critical for the phage's ability to attach to host bacteria and inject its genetic material. Members of the Baseplate Hub Assembly Protein family facilitate the correct folding and assembly of baseplate components, ensuring the formation of a functional viral structure.
Pfam PF22654: Domain of unknown function (DUF7008) (domain)
This domain is found in uncharacterised bacterial proteins. It contains a number of highly conserved positively charged residues that may have functional role.
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 PF16868: NMT1-like family (family)
Substrate-binding proteins (SBPs) are extracytoplasmic proteins involved in substrate recognition for several different bacterial transporters. This entry represents the TAXI family of the substrate-binding proteins. They are part of the TAXI-TRAP (tripartite ATP-independent periplasmic) transporter. Proteins in this family have been proposed to function as glutamine/glutamate specific uptake systems and a role in glutamate transport .
The tripartite ATP-independent periplasmic (TRAP) transporters are substrate-binding protein (SBP)-dependent secondary transporters found in prokaryotes. They consist of a substrate-binding protein (SBP) of the DctP or TAXI families and two integral membrane proteins that form the DctQ and DctM protein families .
Pfam PF22038: Polycomb protein EED insertion domain (domain)
EED is one of the core subunits of Polycomb Repressive Complex 2 (PRC2) that is involved in histone methylation. EED consists of two domains: a seven-bladed beta-propeller and a small alpha/beta domain that is inserted into the sixth blade. EED specifically binds to histone tails carrying trimethyl-lysine residues associated with repressive chromatin marks, and this leads to the allosteric activation of the methyltransferase activity of PRC2.
Pfam PF17456: Toxin-coregulated pilus protein S (family)
The toxin-coregulated pilus (TCP) and cholera toxin (CT) are two main virulence factors produced by V. cholerae, which allows the bacterium to colonize and establish an infection in a host and to cause the physical symptoms of the disease, respectively. Increased expression of the TCP, a type IV pilus expressed by the tcp operon (tcpABQCRDSTEF) located on the Vibrio pathogenicity island (VPI), has been associated with enhanced attachment and is essential for colonization of the intestinal epithelium. This domain of unknown function is found in TcpS proteins in Vibrionaceae such as Vibrio choleae.
Pfam PF22835: Testis-expressed protein 13B-like, middle domain (domain)
This entry represents the middle region of human Testis-expressed protein 13B, which is predicted to show a disordered structure.