SII-SWORD/CoKE huggingface dataset:
Pfam PF12553: Protein of unknown function (DUF3742) (family)
This domain family is found in bacteria, and is approximately 50 amino acids in length. There is a single completely conserved residue Y 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 PF22397: DarT1-associated NADAR antitoxin (family)
This entry, previously known as DUF6977, represents the DarT1-associated NADAR antitoxin and related proteins. The DarT-NADAR system is a TA system catalysing the specific and reversible ADP-ribosylation of guanosine bases in which DarT1-associated NADARs reverse guanine ADP-ribosylation catalysed by DarT1. DarT1-associated NADAR antitoxin adopts an alpha/beta globular structure characterised by an alpha-helical core that forms the active site flanked by two small beta sheet regions, comprising two and three strands. Its structural core is globally similar to the structure of E.coli protein YbiA, a member of the NADAR domain family.
Pfam PF17731: Family of unknown function (DUF5570) (family)
This is a family of unknown function found in chordata. Family members contain a transmembrane region in the C-terminal and have been shown to be localized to the Golgi apparatus.
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 PF17440: Thiol-activated cytolysin beta sandwich domain (domain)
This domain has an immunoglobulin like fold. It is found at the C-terminus of the thiol-activated cytolsin protein.
Wikipedia: The thiol-activated Cholesterol-dependent Cytolysin (CDC) family is a member of the MACPF superfamily. Cholesterol dependent cytolysins are a family of β-barrel pore-forming exotoxins that are secreted by gram-positive bacteria. CDCs are secreted as water-soluble monomers of 50-70 kDa, that when bound to the target cell, form a circular homo-oligomeric complex containing as many as 40 monomers. Through multiple conformational changes, the β-barrel transmembrane structure is formed and inserted into the target cell membrane. The presence of cholesterol in the target membrane is required for pore formation, though the presence of cholesterol is not required by all CDCs for binding. For example, intermedilysin secreted by Streptococcus intermedius will bind only to target membranes containing a specific protein receptor, independent of the presence of cholesterol, but cholesterol is required by intermedilysin for pore formation. While the lipid environment of cholesterol in the membrane can affect toxin binding, the exact molecular mechanism that cholesterol regulates the cytolytic activity of the CDC is not fully understood.
Pfam PF08594: Uncharacterised protein family (UPF0300) (family)
This family of proteins appear to be specific to S. pombe.
Pfam PF24501: TMEM131L fifth Ig-like domain (domain)
Transmembrane protein 131-like (TMEM131L) was identified as a negative regulator of thymocyte proliferation that acts through mixed Wnt-dependent and independent mechanisms. It has two isoforms, L and S, which have different subcellular localisation. L isoform, the membrane-associated form, inhibits canonical Wnt/beta-catenin signalling through the induction of lysosome-dependent degradation of the active phosphorylated form of the LRP6 coreceptor. This protein was firstly described as containing three conserved homology domains (CHD1, 2 and 3), a transmembrane region and a C-terminal serine-rich region. Using structure prediction models from AlphaFold, it has been possible to identify the CHDs as Ig-like domains. This entry represents the fifth Ig-like domain of TMEM131L while in TMEM131 represents the eighth one. TMEM131 is a collagen binding transmembrane protein involved in collagen secretion by recruiting the ER-to-Golgi transport complex TRAPPIII.
Pfam PF06595: Borna disease virus P24 protein (family)
This family consists of several Borna disease virus (BDV) P24 proteins. The function of this family is unknown.
Wikipedia: The Borna disease viruses 1 and 2 are members of the species Mammalian 1 orthobornavirus and cause Borna disease in mammals.
Pfam PF08728: CRT10 (family)
CRT10 is a transcriptional regulator of ribonucleotide reductase (RNR) genes.  RNR catalyses the rate limiting step in dNTP synthesis.  Mutations in CRT10 have been shown to enhance hydroxyurea resistance.
Pfam PF01338: Bacillus thuringiensis toxin (domain)
Bacillus thuringiensis produces the delta-endotoxin CytB, a membrane pore-forming protein, which is active against insects . The toxin kills the larvae of dipteran insects by making pores in the epithelial cell membrane of the insect midgut. The crystal protein is produced during sporulation and is accumulated both as an inclusion and as part of the spore coat.
Wikipedia: Delta endotoxins (δ-endotoxins) are a family of pore-forming toxins produced by Bacillus thuringiensis species of bacteria. They are useful for their insecticidal action and are the primary toxin produced by the genetically modified (GM) Bt maize/corn and other GM crops. During spore formation the bacteria produce crystals of such proteins that are also known as parasporal bodies, next to the endospores; as a result some members are known as a parasporin. The Cyt (cytolytic) toxin group is another group of delta-endotoxins formed in the cytoplasm. VIP toxins are formed at other stages of the life cycle.
Pfam PF06557: Protein of unknown function (DUF1122) (family)
This family consists of several hypothetical archaeal and bacterial proteins of unknown function, including [swissprot:O67778] from Aquifex aeolicus. The structure of this protein has been solved but its function remains unknown. Members of this family seem to have an acyl-CoA N-acyltransferase topology.
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 PF11162: Protein of unknown function (DUF2946) (family)
This family of proteins has no known function.
Wikipedia: A domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.
Pfam PF05593: RHS Repeat (repeat)
RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding (e.g.). Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain.
Pfam PF23627: WDR26 Lis-homology motif (conserved_site)
This entry represents the LisH motif present towards the N-terminal of WD repeat-containing protein 26 homolog (WDR26) from Arabidopsis thaliana and other eukaryotic proteins. WDR26 is involved in cellular signaling control of high light acclimation, defense response to biotic and abiotic stress and implicated in the regulation of hormones. This motif is often associated to CTLH and WD domains.
Pfam PF24401: iHD-CE (domain)
This entry represents an inactive HD-CE domain (iHD-CE) which acts as a sensor in the antiviral immunity systems and it is predominantly located within HSP90 systems. Specifically, it is associated with wHTH repeats located at the C-terminal.
Pfam PF23585: Domain of unknown function (DUF7137) (domain)
This domain is found in a group of uncharacterised proteins mainly from Fungi. It is predicted to adopt a beta-sandwich with Ig-like topology and is likely distantly related to the delta subunit of translocon-associated protein (TRAP-delta, [pfam:PF05404]).
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 PF22032: Hen1 N-terminal domain (domain)
This is the N-terminal domain of Hen1. The bacterial RNA repair complex composed of three proteins: Pnkp1, Rnl and Hen1, neutralises the damage inflicted by ribotoxins which is essential for cell survival. The Pnkp-Hen1 RNA repair complex carries out methylation of the 2'-OH group that is responsible for the RNA cleavage and thus the repaired RNA resists future RNA damage by the same ribotoxin. The N-terminal domain of Hen1 activates the ligase activity of Pnkp by locking the insertion domain of Pnkp into a conformation that allows access to the ligase pocket.
Pfam PF23235: Large helicase-related protein, winged-helix domain (domain)
This is a winged-helix (WH) domain found in Large helicase -related protein from Escherichia coli (Lhr), DEAD/DEAH box helicase from Mycolicibacterium smegmatis ([swissprot:A0QT91]) and similar bacterial sequences. These proteins have a C-terminal domain composed of a series of five WH modules (named WH2 to WH6) and a beta-barrel module. This entry represents WH3. It shows three alpha-helices followed by two loops or 'wings' and two beta-strands forming an antiparallel beta-sheet.
Pfam PF02811: PHP domain (family)
The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.
Pfam PF14608: RNA-binding, Nab2-type zinc finger (domain)
This is an unusual zinc-finger family, and is represented by fingers 5-7 of Nab2. Nab2 ZnF5-7 are zinc-fingers of the type C-x8-C-x5-C-x3-H. Nab2 ZnFs function in the generation of export-competent mRNPs. Mab2 is a conserved polyadenosine-RNA-binding Zn finger protein required for both mRNA export and polyadenylation regulation and becomes attached to the mRNP after splicing and during or immediately after polyadenylation. The three ZnFs, 5-7, have almost identical folds and, most unusually, associate with one another to form a single coherent structural unit. ZnF5-7 bind to eight consecutive adenines, and chemical shift perturbations identify residues on each finger that interact with RNA.
Pfam PF12828: PX-associated (domain)
This domain is associated with the PX domain.
Pfam PF17444: Uncharacterized YhdX-like (family)
This is a family of unknown function found in Bacillus.
Pfam PF14275: Domain of unknown function (DUF4362) (family)
This family of proteins is found in bacteria. Proteins in this family are typically between 93 and 146 amino acids in length. There is a conserved IRIV 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 PF02521: Putative outer membrane protein (domain)
This family consists of putative outer membrane proteins from Helicobacter pylori (campylobacter pylori).
Pfam PF10093: Elongation-Factor P (EF-P) rhamnosyltransferase EarP (family)
This entry includes family members such as EarP enzymes which are essential for post-translational activation of elongation factor P(EF-P). It was identified as EF-P arginine R32 specific rhamnosyl transferase in Shewanella oneidensis using dTDP-beta-L-rhamnose as donor substrate. This was further confirmed for Pseudomonas aeruginosa, Pseudomonas putida and Neisseria meningitidis. As for S. oneidensis and P. aeruginosa, EarP enzyme acts as an inverting glycosyltransferase, thus mediating the formation of an alpha-L-rhamnosidic linkage. Structural analysis show that EarP is composed of two opposing domains with Rossmann folds, thus constituting a B pattern-type glycosyltransferase (GT-B) and provide basis for arginine glycosylation by EarP. Mutational analysis of efp and earP genes, resulted in a substantial decrease in the production of rhamnolipids and pyocyanin (important factors for colonization and invasion during infection) of P. aeruginosa. Collectively this indicates that EarP and EF-P are essential for P. aeruginosa pathogenicity.The protein family is also annotated in the CaZy Database as GT104.
Pfam PF09994: T6SS, Phospholipase effector Tle1-like, catalytic domain (domain)
This domain is found in the type VI secretion system (T6SS) protein Phospholipase effector Tle1 from Pseudomonas aeruginosa ([swissprot:Q9HYV3]), which hydrolyse membrane phospholipids. Tle1 is organised into two distinct parts, the phospholipase catalytic module (this entry) and the putative membrane-anchoring module ([pfam:PF22137]). This domain adopts a compact conformation with a classical mixed alpha/beta-hydrolase fold that shows of seven central parallel beta-sheets and 13 alpha-helices.
Pfam PF05241: EXPERA (EXPanded EBP superfamily) (family)
The EXPERA (EXPanded EBP superfamily) domain is conserved among the  following protein families: TM6SF1 (Transmembrane 6 Superfamily Member 1), TM6SF2 (Transmembrane 6 Superfamily Member 2), MAC30  (Meningioma-associated protein 30 also known as TMEM97, or  Transmembrane protein 97), and EBP (Emopamil binding protein). EBP is an enzyme with a D8, D7 sterol isomerase activity that catalyzes the  transposition of a double bond from C8=C9 to C7=C8 in the sterol  B-ring. Mutations of EBP are known to cause the genetic disorder of X-linked dominant chondrodysplasia punctata (CDPX2). This syndrome of humans is lethal in most males, and affected females display asymmetric hyperkeratotic skin and skeletal abnormalities.
Pfam PF00649: Copper fist DNA binding domain (domain)
Some fungal transcription factors contain an N-terminal domain, the copper fist, which seems to be involved in copper-dependent DNA-binding . These proteins activate the transcription of the metallothionein gene in response to copper. Metallothionein maintains copper levels in yeast . The copper fist domain, which is similar in structure to metallothionein itself, undergoes a large conformational change on copper-binding that allows DNA-binding. The domain contains a conserved array of zinc-binding residues (Cys-X2-Cys-X8-Cys-X-His) and forms a three-stranded antiparallel Î²-sheet with two short helical segments that project from one end of the Î²-sheet . Conserved residues form a basic patch that may be important for DNA binding.
Wikipedia: Copper fist is an N-terminal domain involved in copper-dependent DNA binding. It is named for its resemblance to a fist closed around a penny. Functionally, the "penny" is a collection of copper ions and the "knuckles" of the fist are proteins that interact with the promoter of the metallothionein gene, enhancing its transcription by creating a more stable binding site for RNA polymerase during transcription, an essential step in DNA replication.
Pfam PF17136: Ribosomal proteins 50S L24/mitochondrial 39S L24 (family)
This is the family of bacterial 50S ribosomal subunit proteins L24. It also carries some mitochondrial 39S L24 proteins.
Pfam PF21297: Mitochondrial dynamics protein MID51-like, C-terminal domain (domain)
This domain is found in Mitochondrial dynamics protein MID51 from humans and similar proteins predominantly found in vertebrates. MID51 promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface to drive mitochondrial fission. This entry represents the C-terminal domain of this protein, which adopts a nucleotidyltransferase fold with a mixed alpha-beta topology configured into two lobes separated by a deep cleft.
Pfam PF11619: Transcription factor P53 - C terminal domain (family)
This family of proteins is the C terminal domain of the transcription factor P53. While the rest of the protein is quite conserved between the different transcription factors such as p53 and p73, the C terminal domain is highly divergent. The DM-p53 structure is characterized by an additional N-terminal beta-strand and a C-terminal helix.
Wikipedia: 
p53, also known as Tumor protein P53, cellular tumor antigen p53, or transformation-related protein 53 (TRP53) is a regulatory protein that is often mutated in human cancers. The p53 proteins are crucial in vertebrates, where they prevent cancer formation. As such, p53 has been described as "the guardian of the genome" because of its role in conserving stability by preventing genome mutation. Hence TP53 is classified as a tumor suppressor gene.
Pfam PF15211: VEGF co-regulated chemokine 1 (family)
C-X-C chemokine 17 (CXCL17) or dendritic cell and monocyte chemokine-like protein (DMC), is a cytokine-like protein that regulates recruitment of nonactivated blood monocytes and immature dendritic cells into tissues . It may play a role in the innate defense against infections . It also plays a role in angiogenesis and possibly in the development of tumours .
Wikipedia: Chemokine ligand 17 (CXCL17) is a small cytokine belonging to the CXC chemokine family that has been identified in humans and mice. CXCL17 attracts dendritic cells and monocytes and is regulated in tumors. It is also known as VEGF co-regulated chemokine 1 (VCC-1) and dendritic cell- and monocyte-attracting chemokine-like protein (DMC). This chemokine is constitutively expressed in the lung. The gene for human CXCL17 is located on chromosome 19.
Pfam PF16287: Domain of unknown function (DUF4933) (repeat)
This family consists of uncharacterized proteins around 450 residues in length and is mainly found in various species, such as Bacteroides and Parabacteroides. Several members are annotated as putative transmembrane proteins, but the specific function of this family is unknown.
Pfam PF22736: NACHT N-terminal Helical domain 5 (domain)
This entry represents the helical domain found at the N-terminus of bacterial NACHT conflict systems. This position is frequently occupied by an effector domain.
Pfam PF21502: Oxalate biosynthetic component 1, cap domain (domain)
This domain is found in a group of proteins from proteobacteria and fungi, including the bifunctional enzyme Oxalate biosynthetic component 1 from Burkholderia pseudomallei (Obc1, [swissprot:Q63KK6]). This entry represents the cap domain of Obc1, which adopts an alpha- helical fold, with two layers of anti-parallel helices.
Pfam PF05239: PRC-barrel domain (domain)
The PRC-barrel is an all beta barrel domain found in photosystem reaction centre subunit H of the purple bacteria and RNA metabolism proteins of the RimM group. PRC-barrels are approximately 80 residues long, and found widely represented in bacteria, archaea and plants.  This domain is also present at the carboxyl terminus of the pan-bacterial protein RimM, which is involved in ribosomal maturation and processing of 16S rRNA. A family of small proteins conserved in all known euryarchaea are composed entirely of a single stand-alone copy of the domain.
Pfam PF10789: Phage RNA polymerase binding, RpbA (family)
Upon infection the RpbA encode phage protein binds to the ADP-ribosylated core RNA polymerase and modulates function to preferentially bind T4 promoters.                 This is a non-essential protein to the phage life cycle.
Pfam PF24729: Acb2/Tad1, hairpin domain (domain)
This domain, previously known as DUF7681, is found in phage proteins including Anti-CBASS protein 2 (Acb2) and Thoeris anti-defense 1 (Tad1). It folds into an alpha-helical hairpin that is found either standalone (in Acb2) or in combination with a four-stranded antiparallel beta-sheet domain (in Tad1). Prokaryotic anti-phage immune systems use TIR and cGAS-like enzymes to produce 1-3-glycocyclic ADP-ribose; and cyclic dinucleotide and trinucleotide signalling molecules, respectively, which limit phage replication. The Thoeris anti-defence proteins Tad1 and Tad2 are both pronged inhibitors and antagonise immunity alongside Anti-CBASS protein 2. These proteins achieve anti-cyclic-oligonucleotide-based anti-phage signalling system (anti-CBASS) activity by sequestering a considerable amount of cyclic nucleotides. Each of these proteins is using distinct binding pockets. The residues conserved in Tad1 and Acb2 are located near these binding sites.
Pfam PF19756: Family of unknown function (DUF6243) (family)
This entry represents a member of a biosynthetic gene cluster (BGC). This BGC (BGC0001931) is described by MIBiG as an example of the following biosynthetic class, polyketide. It includes a member from the carrimycin biosynthetic gene cluster from unidentified  unclassified sequences. 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 PF15431: Transmembrane protein 190 (family)
This entry represents the transmembrane protein 190 (TMEM190) family. In mice, this protein may play an indirect role in sperm-oocyte fusion .
Pfam PF16479: Domain of unknown function (DUF5056) (family)
This family consists of uncharacterized proteins around 360 residues in length and is mainly found in various  Bacteroides species. 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 PF00006: ATP synthase alpha/beta family, nucleotide-binding domain (domain)
This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Wikipedia: The alpha and beta subunits are found in the F1, V1, and A1 complexes of F-, V- and A-ATPases, respectively, as well as flagellar (T3SS) ATPase and the termination factor Rho. The subunits make up a ring that contains the ATP-hydrolyzing catalytic core. The F-ATPases, V-ATPases and A-ATPases are composed of two linked complexes: the F1, V1 or A1 complex containsthat synthesizes/hydrolyses ATP, and the Fo, Vo or Ao complex that forms the membrane-spanning pore. The F-, V- and A-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis.