SII-SWORD/CoKE huggingface dataset:
Pfam PF03443: Auxiliary Activity family 9 (formerly GH61) (family)
Although weak endoglucanase activity has been demonstrated in several members of this family, they lack the clustered conserved catalytic acidic amino acids present in most glycoside hydrolases.  Many members of this family lack measurable cellulase activity on their own, but enhance the activity of other cellulolytic enzymes.  They are therefore unlikely to be true glycoside hydrolases. The substrate-binding surface of this family is a flat Ig-like fold. This family of enzymes were originally classified as glycoside hydrolases (GH61) and they have been reclassified as the Auxiliary Activity Family 9 (AA9) of CAZy.
Wikipedia: Auxiliary Activity family 9 is a family of lytic polysaccharide monooxygenases. The family was previously incorrectly classified as glycoside hydrolase family 61, however it was re-classified in March 2013.
Pfam PF16309: Domain of unknown function (DUF4951) (family)
This family consists of several uncharacterized proteins around 125 residues in length and is mainly found in various Acinetobacter baumannii species. The function of this family is unknown.
Pfam PF04942: CC domain (domain)
This short domain contains four conserved cysteines that probably for two disulphide bonds. The domain is named after the characteristic CC motif.
Pfam PF02308: MgtC family (family)
The MgtC protein is found in an operon with the Mg2+ transporter protein MgtB.  The function of MgtC and its homologues is not known.
Pfam PF17860: RK-1-like defensin (domain)
This family includes RK-1 a defensin like peptide from rabbit kidney. The family also includes some rat alpha defensins.
Pfam PF11022: ATP synthase subunit K (family)
This entry represents ATP synthase subunit K (Atp19) from fungi. Atp19 is the subunit k of the mitochondrial F1F0 ATP synthase, which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain.
Pfam PF17652: Glycosyl hydrolase family 81 C-terminal domain (repeat)
Family of eukaryotic beta-1,3-glucanases. Within the Aspergillus fumigatus protein [swissprot:Q9UVV0] two perfectly conserved Glu residues (E550 or E554) have been proposed as putative nucleophiles of the active site of the Engl1 endoglucanase, while the proton donor would be D475. The endo-beta-1,3-glucanase activity is essential for efficient spore release. This entry represents the helical C-terminal domain.
Wikipedia: In molecular biology, glycoside hydrolase family 81 is a family of glycoside hydrolases.
Pfam PF15042: Late cornified envelope-like proline-rich protein 1 (family)
This family of uncharacterised proteins is found in mammals.
Pfam PF13588: Type I restriction enzyme R protein N terminus (HSDR_N) (domain)
This family consists of a number of N terminal regions found in type I restriction enzyme R (HSDR) proteins. Restriction and modification (R/M) systems are found in a wide variety of prokaryotes and are thought to protect the host bacterium from the uptake of foreign DNA. Type I restriction and modification systems are encoded by three genes: hsdR, hsdM, and hsdS. The three polypeptides, HsdR, HsdM, and HsdS, often assemble to give an enzyme (R2M2S1) that modifies hemimethylated DNA and restricts unmethylated DNA.
Pfam PF11585: Insect antimicrobial peptide, stomoxyn (family)
Stomoxyn, localised in the gut epithelium, is an insect antimicrobial peptide which functions in killing a range of microorganisms, parasites and some viruses. Stomoxyn has a structure consisting of a random coil in water however in TFE it adopts a stable helical structure. Stomoxyn is thought to have a similar function to cecropin A from Hyalophora cecropia due to structural similarities.
Wikipedia: Stomoxyn is an insect antimicrobial peptide localised in the gut epithelium, which functions in killing a range of microorganisms, parasites and some viruses. In water, stomoxyn has a flexible random coil in structure, while in trifluoroethanol it adopts a stable helical structure. Structural similarities to the antimicrobial peptide cecropin A from Hyalophora cecropia suggest that it may function in a similar manner by disrupting the bacterial membrane.
Pfam PF22653: Domain of unknown function (DUF7007) (domain)
This domain is found in uncharacterised bacterial proteins. It is predicted to adopt a globular structure consisting of segregated alpha-helices and a five-stranded antiparallel beta-sheet. This domain contains two highly conserved sequence motifs TxxHGG and  YEED that may be of a functional importance.
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 PF22129: CRISPR-associated endonuclease CjCas9 wedge domain (domain)
In the type II CRISPR-Cas system, the Cas9 effector nuclease associates with dual guide RNAs (crRNA and trans-activating crRNA (tracrRNA)) and cleaves double-stranded DNA targets complementary to the crRNA guide. Cas9 is composed of multiple domains. This entry represents the so-called wedge (WED) domain that is found in Campylobacter jejuni Cas9 (CjCas9), one of the smallest Cas9 orthologues. The WED domain is involved in the recognition of PAM-containing duplex formed by the target and non-target DNA strands. The CjCas9 WED domain consists of a beta-hairpin packed with two short alpha-helices.
Pfam PF18947: HAMP domain (domain)
The HAMP domain (present in Histidine kinases, Adenyl cyclases, Methyl-accepting proteins and Phosphatases) is an approximately 50-amino acid Î±-helical region common to chemoreceptors and histidine kinases that is present in several multidomain sensor proteins that participate in a variety of signal transduction processes. It is found in bacterial sensor and chemotaxis proteins and in eukaryotic histidine kinases. The bacterial proteins are usually integral membrane proteins and part of a two-component signal transduction pathway. One or several copies of the HAMP domain can be found in association with other domains, such as the histidine kinase domain, the bacterial chemotaxis sensory transducer domain, the PAS repeat, the EAL domain, the GGDEF domain, the protein phosphatase 2C-like domain, the guanylate cyclase domain, or the response regulatory domain. It has been suggested that the HAMP domain possesses a role of regulating the phosphorylation or methylation of homodimeric receptors by transmitting the conformational changes in periplasmic ligand-binding domains to cytoplasmic signalling kinase and methyl-acceptor domains .
Wikipedia: In molecular biology, the HAMP domain is an approximately 50-amino acid alpha-helical region that forms a dimeric, four-helical coiled coil. It is found in bacterial sensor and chemotaxis proteins and in eukaryotic histidine kinases. The bacterial proteins are usually integral membrane proteins and part of a two-component signal transduction pathway. One or several copies of the HAMP domain can be found in association with other domains, such as the histidine kinase domain, the bacterial chemotaxis sensory transducer domain, the PAS repeat, the EAL domain, the GGDEF domain, the protein phosphatase 2C-like domain, the guanylate cyclase domain, or the response regulatory domain. In its most common setting, the HAMP domain transmits conformational changes in periplasmic ligand-binding domains to cytoplasmic signalling kinase and methyl-acceptor domains and thus regulates the phosphorylation or methylation activity of homodimeric receptors.
Pfam PF18246: Oligosaccharyltransferase Insert domain (domain)
This is a domain found in STT3 present in P. furiosus. In P. furiousus, STT3 is an Oligosaccharyltransferase which catalyzes the transfer of a heptasaccharide, containing one hexouronate and two pentose residues, onto peptides in an Asn-X-Thr/Ser-motif-dependent manner. This domain is inserted into the central core (CC) domain and hence is referred to as the Insert (IS) domain. This IS domain contains a disulphide bond.
Pfam PF08797: HIRAN domain (domain)
The HIRAN domain (HIP116, Rad5p N-terminal) is found in the N-terminal regions of the SWI2/SNF2 proteins typified by HIP116 and Rad5p. The HIRAN domain is found as a standalone protein in several bacteria and prophages, or fused to other catalytic domains, such as a nuclease of the restriction endonuclease fold and TDP1-like DNA phosphoesterases, in the eukaryotes. It has been predicted that this domain functions as a DNA-binding domain that probably recognises features associated with damaged DNA or stalled replication forks
Pfam PF07851: TMPIT-like protein (family)
A number of members of this family are annotated as being transmembrane proteins induced by tumour necrosis factor alpha, but no literature was found to support this.
Pfam PF18122: Anaphase-promoting complex sub unit 1 C-terminal domain (domain)
This is the C-terminal domain of chain A, also known as sub-unit 1, found in anaphase-promoting complex (APC/C) present in Homo sapiens. APC/C is an ubiquitin ligase that controls chromosome segregation and mitotic exit.
Pfam PF11053: Terminase DNA packaging enzyme (family)
Phage T4 terminase functions in packaging concatemeric DNA. The T4 terminase is composed of a large subunit, gp17 ad a small subunit, gp16. The role of gp16 is not well characterised however it is known that it binds to double-stranded DNA but not single stranded DNA.
Pfam PF20727: Nairovirus, mucin-like domain (domain)
This is the mucin-like domain (MLD) located at the N-terminal of the glycoprotein precursor complex (GPC), encoded in the M segment of nairoviruses genome. It contains a furin cleavage site which separates MLD from GP38 ([pfam:PF07948]).
Pfam PF22574: Sperm microtubule inner protein 8 (domain)
This domain is found in homologues of Sperm microtubule inner protein 8 (SPMIP8, also known as Testis, prostate and placenta-expressed protein TEPP). SPMIP8 is an axonemal microtubule inner protein (MIP) part of the doublet microtubules (DMTs) in flagellum axoneme. SPMIP8 is specifically expressed in testis, prostate, and placenta, and might have a role in reproductive biology.
Pfam PF10690: Myticin pre-proprotein from the mussel (family)
Myticin is a cysteine-rich peptide produced in three isoforms, A, B and C, by Mytilus galloprovincialis, the Mediterranean mussel. Some isoforms show antibacterial activity against gram-positive bacteria, while others are additionally active against the fungus Fusarium oxysporum and a gram-negative bacterium, Escherichia coli D31.  Myticin-prepro is the precursor peptide. The mature molecule, named myticin, consists of 40 residues, with four intramolecular disulfide bridges and a cysteine array in the primary structure different from that of previously characterised cysteine-rich antimicrobial peptides. The first 20 amino acids are a putative signal peptide, and the antimicrobial peptide sequence is a 36-residue C-terminal extension. Such a structure suggests that myticins are synthesised as prepro-proteins that are then processed by various proteolytic events before storage in the haemocytes as the active peptide. Myticin precursors are expressed mainly in the haemocytes. The family Mytilin has been merged into this family.
Wikipedia: Myticin is a cysteine-rich peptide produced in three isoforms, A, B and C, by Mytilus galloprovincialis, which are found primarily in marine habitats. Myticin is also produced in other species of Mytilus, though the properties of Myticin in Mytilus galloprovincialis is understood to a greater extent. Isoforms A and B show antibacterial activity against Gram-positive bacteria, while isoform C is additionally active against the fungus Fusarium oxysporum and bacterium Escherichia coli. Myticin-prepro is the precursor peptide.
Pfam PF05796: Chordopoxvirus protein G2 (family)
This family consists of several Chordopoxvirus isatin-beta-thiosemicarbazone dependent protein (protein G2) sequences. Inactivation of the gene coding for this protein renders the virus dependent upon isatin-beta-thiosemicarbazone (IBT) for growth.