SII-SWORD/CoKE huggingface dataset:
Domain of unknown function DUF7850 (DUF7850)
Type: Domain

This domain is found in uncharacterised proteins mainly from Actinomycetes. It is predicted to adopt a β-sandwich structure with significant similarity to carbohydrate-binding modules in particular to CBM_4_9 (

).
Domain of unknown function DUF7851 (DUF7851)
Type: Domain

This domain is found in uncharacterised proteins from plants. It is predicted to adopt a structure consisting of a mixed β-sheet and α-helices packed on both sides with unique topology. It contains a highly conserved sequence motif RxKxRKG that contributes to the formation of a highly basic surface patch.
Domain of unknown function DUF7852 (DUF7852)
Type: Domain

This domain is found in uncharacterised bacterial proteins. It is predicted to adopt a β-sandwich structure with long twisted strands.
Protein of unknown function DUF7853 (DUF7853)
Type: Family

This family represents a group of uncharacterised proteins from halobacteria. Members are around 100 residues and are predicted to adopt a mainly alpha-configuration.
Protein of unknown function DUF7854 (DUF7854)
Type: Family

This family represents a group of uncharacterised proteins from halobacteria. Members are around 100 residues and are predicted to adopt an α-β configuration.
Protein of unknown function DUF7855 (DUF7855)
Type: Family

This family represents a group of uncharacterised proteins from halobacteria. Members are around 100 residues and are predicted to adopt an α-β configuration an the N-terminal and show short α-helices in the C-terminal.
Protein of unknown function DUF7856 (DUF7856)
Type: Family

This family represents a group of uncharacterised proteins from halobacteria.
Protein of unknown function DUF7857 (DUF7857)
Type: Family

This family represents a group of uncharacterised proteins from halobacteria. Members are around 284 residues and are predicted to adopt a mainly β configuration an the N-terminal and show short α-helices in the C-terminal.
Protein of unknown function DUF7858 (DUF7858)
Type: Family

This family represents a group of uncharacterised proteins from halobacteria. Members are predicted to adopt a mainly alpha configuration.
Protein of unknown function DUF7859 (DUF7859)
Type: Family

This family represents a group of very short uncharacterised sequences from halobacteria. Members are predicted to adopt an α-helical configuration.
Protein of unknown function DUF7860 (DUF7860)
Type: Family

This family represents a group of short uncharacterised proteins from halobacteria. Members are predicted to adopt an alpha configuration.
Protein of unknown function DUF7861 (DUF7861)
Type: Family

This family represents a group of uncharacterised proteins from halobacteria. Members are around 100 residues and are predicted to adopt a mainly beta configuration.
Domain of unknown function DUF7862 (DUF7862)
Type: Domain

This domain is found in uncharacterised bacterial proteins. It is predicted to adopt a β-sandwich with Ig-like topology.
Domain of unknown function DUF7863 (DUF7863)
Type: Domain

This domain is found in uncharacterised bacterial proteins. It is predicted to adopt a globular structure composed of array of helices.
Domain of unknown function DUF7864 (DUF7864)
Type: Domain

This domain is found in uncharacterised bacterial proteins. It is predicted to adopt a globular α/β structure with similarity to AAA proteins.
Domain of unknown function DUF7865 (DUF7865)
Type: Domain

This domain is found in uncharacterised plan proteins. It is predicted to contain four transmembrane helices.
Domain of unknown function DUF7866 (DUF7866)
Type: Domain

This domain is found in uncharacterised proteins from plants. It is predicted to fold into a three-stranded antiparallel twisted β-sheet. It contains several highly conserved cysteine residues that are predicted to form disulfide bonds.
Domain of unknown function DUF7867 (DUF7867)
Type: Domain

This domain is found in a group of uncharacterised proteins from alphaproteobacteria. This domain is usually found associated with

and is predicted to form a three -sided beta-helix.
Domain of unknown function DUF7868 (DUF7868)
Type: Domain

This domain is found in uncharacterised bacterial proteins. It has similarity to the C-terminal domain of Haemocyanin and it is predicted to adopt similar β-sandwich fold.
Domain of unknown function DUF7869 (DUF7869)
Type: Domain

This domain is found in uncharacterised eukaryotic proteins. It is predicted to adopt a globular structure composed of a curved β-sheet and helices packed on it. It contains conserved histidine and aspartate residues some of which cluster in space.
Domain of unknown function DUF7870 (DUF7870)
Type: Domain

This domain is found in uncharacterised plant proteins. It has detectable similarity to methyltransferases and it is predicted to adopt similar structure. It contains two highly conserved cysteines and a histidine.
Domain of unknown function DUF7871 (DUF7871)
Type: Domain

This domain is found in uncharacterised fungal proteins. It contains a number of highly conserved cysteine residues some of which may be involved in metal coordination.
Domain of unknown function DUF7872 (DUF7872)
Type: Domain

This domain is found in uncharacterised fungal proteins. It contains highly conserved cysteine residues that are predicted to form disulfide bonds. This domain is predicted to fold into an α/β structure with an unique topology.
Protein of unknown function DUF7873 (DUF7873)
Type: Family

This entry represents a family of uncharacterised actinobacterial proteins.
Protein of unknown function DUF7874 (DUF7874)
Type: Family

This entry represents a group of uncharacterised plant proteins. They are predicted to adopt a non-compact structure composed of α-helices.
Domain of unknown function DUF7875 (DUF7875)
Type: Domain

This entry represents a group of uncharacterised plant proteins. They are predicted to adopt a helical hairpin structure.
Domain of unknown function DUF7876 (DUF7876)
Type: Domain

This entry represents a domain found in a group of uncharacterised plant proteins. It is predicted to fold into an array of α-helices.
Domain of unknown function DUF7877 (DUF7877)
Type: Domain

This is a presumed domain found in a group of uncharacterised fungal sequences.
Domain of unknown function DUF7878 (DUF7878)
Type: Domain

This domain is found in uncharacterised bacterial proteins. It is predicted to contain two structural β(3)-α repeats that swap their α-helix in a similar way as observed in the known ssDNA-binding transcriptional regulator domains. It is likely that this domain is distantly related to them and probably represents the minimal two repeat containing fold.
Protein of unknown function DUF7879 (DUF7879)
Type: Family

This entry represents a family of virus proteins that is likely zinc binding. It shows structural similarity to

. The function of these proteins is unknown.
Domain of unknown function DUF7880 (DUF7880)
Type: Domain

This entry represents a four helical bundle domain found in a range of uncharacterised proteins. This domain is sometimes found in proteins that also contain

. Shows similarity to the PsbQ superfamily.
Domain of unknown function DUF7881 (DUF7881)
Type: Domain

This entry represents a ubiquitin-like fold domain found in a range of bacterial proteins. These proteins usually have an adjacent HNH domain to the C terminus (

). The function of this domain is unknown.
Domain of unknown function DUF7882 (DUF7882)
Type: Domain

This entry represents a family of uncharacterised proteins that are about 100 amino acids in length. These proteins are predicted to form homopentameric complexes. These proteins are found in actinomycete as well as a few phage genomes.
Domain of unknown function DUF7883 (DUF7883)
Type: Domain

This entry represents a domain of unknown function identified in Trypanosoma. Based on structural predictions, this domain is hypothesised to adopt a winged helix-turn-helix (HTH) fold. Winged helix DNA-binding proteins share a characteristic winged helix-turn-helix DNA-binding motif, in which the "wings", or loops, are small β-sheets .
Domain of unknown function DUF7884 (DUF7884)
Type: Domain

This domain is found in a group of uncharacterised bacterial proteins. It is usually found associated with methyltransferase domains such as

and

and is predicted to adopt an α-β configuration. It has a conserved motif F/YWDG.
Domain of unknown function DUF7885 (DUF7885)
Type: Domain

This domain is found in a group of uncharacterised plant proteins that are predicted to have an F-box domain.
Domain of unknown function DUF7886 (DUF7886)
Type: Domain

This domain is found in uncharacterised proteins from animals and plants. It is predicted to adopt an unique complex α/β structure.
Domain of unknown function DUF7887 (DUF7887)
Type: Domain

This domain is found in uncharacterised plant proteins. It is predicted to contain two transmembrane helices.
Domain of unknown function DUF7888 (DUF7888)
Type: Domain

This domain is found in uncharacterised fungal proteins. It is predicted to fold into α-β-β sandwich. It has two pairs of conserved cysteine residues that are predicted to form disulfide bonds.
Domain of unknown function DUF7889 (DUF7889)
Type: Domain

This presumed domain is found in a group of fungal uncharacterised proteins that also contain

and

. It has highly conserved E and L residues.
Domain of unknown function DUF7890 (DUF7890)
Type: Domain

This domain is found in uncharacterised plant proteins. It is predicted to contain two short α-helices. At the N terminus, it contains a number of highly conserved positively charged residues.
Domain of unknown function DUF7891 (DUF7891)
Type: Domain

This domain is found in a group of uncharacterised fungal sequences that also contain

. It has a conserved I/LWG motif.
Domain of unknown function DUF7892 (DUF7892)
Type: Domain

This predicted domain is found in a group of uncharacterised fungal proteins that also contain an F-box domain. This domain is predicted to adopt a winged helix fold.
Domain of unknown function DUF7893 (DUF7893)
Type: Domain

This predicted winged helix domain is found in a group of uncharacterised fungal proteins. It is often found associated with

.
Domain of unknown function DUF7894 (DUF7894)
Type: Domain

This domain is found in uncharacterised plant proteins. It is predicted to fold into a α/β structure with a central mixed β-sheet and α-helices packed on both sides. The predicted structure has a topological similarity to PACT family domains members of

.
Domain of unknown function DUF7895 (DUF7895)
Type: Domain

This domain is found in uncharacterised plant proteins. It contains four pairs of highly conserved cysteine residues that may be involved in metal coordination. It also contains a highly conserved CxxCxGxG sequence motif.
Domain of unknown function DUF7896 (DUF7896)
Type: Domain

This domain is found in uncharacterised proteins from fungi. It contains two pairs of conserved cysteine and histidine residues that may be involved in metal coordination.
Domain of unknown function DUF7897 (DUF7897)
Type: Domain

This domain is found in uncharacterised proteins predominantly from bacteria. It is predicted to adopt a complex α/β structure.
Domain of unknown function DUF7898 (DUF7898)
Type: Domain

This entry describes the N-terminal domain of unknown function of DNA polymerase theta subunit (PolQ) majoritarily from fungal and and yeast proteins. Structural predictions suggest that this family adopts Helix-Helix-Helix (HHH) motifs. Proteins containing HHH motifs are typically associated with DNA-binding functions. These structural elements are often found in enzymes involved in DNA metabolism, such as DNA polymerases and helicases .
Repeat of unknown function DUF7899 (DUF7899)
Type: Repeat

This domain is found in uncharacterised plant proteins. It is predicted to adopt an eight-bladed β-propeller.
Domain of unknown function DUF7900 (DUF7900)
Type: Domain

This domain is found at the C-terminal end of a group of uncharacterised plant proteins. It is often found associated to

. It has a conserved motif GWQK.
Domain of unknown function DUF7901 (DUF7901)
Type: Domain

This domain is found in uncharacterised bacterial proteins. It is predicted to adopt a β-sandwich structure with significant topological similarity to known galactose-binding domains, in particular to lectin-like domain of the Cwp84, a surface layer associated protein of Clostridium difficile. It is likely that this domain is involved carbohydrate binding.
Domain of unknown function DUF7902 (DUF7902)
Type: Domain

This domain is found in uncharacterised bacterial proteins. It is predicted to adopt a three-helical bundle with some topological similarity to spectrin.
Domain of unknown function DUF7903 (DUF7903)
Type: Domain

This domain is found in uncharacterised plant proteins. It has detectable similarity to members of the CYTH-like phosphatase superfamily and it is predicted to adopt similar structure.
Domain of unknown function DUF7904 (DUF7904)
Type: Domain

This gelsolin-like domain is found in a group of uncharacterised fungal proteins. Its function is unknown.
Domain of unknown function DUF7905 (DUF7905)
Type: Domain

This domain is found in the Uncharacterized protein C582.04c from Schizosaccharomyces pombe and related proteins. It has detectable similarity to domains members of the CYTH-like phosphatase superfamily and it is predicted to adopt a similar structure.
Domain of unknown function DUF7906 (DUF7906)
Type: Domain

This domain is found in uncharacterised plant proteins. It is predicted to adopt a globular α/β structure.
Domain of unknown function DUF7907 (DUF7907)
Type: Domain

This domain is found in uncharacterised fungal proteins. It is predicted to adopt beta-Trefoil fold. It is probably distantly related to domains members of

.
Domain of unknown function DUF7908 (DUF7908)
Type: Domain

This domain is found in uncharacterised fungal proteins. It is predicted to adopt beta-Trefoil fold.
Domain of unknown function DUF7909 (DUF7909)
Type: Domain

This domain is found in uncharacterised fungal proteins. It is predicted to adopt beta-Trefoil fold.
Domain of unknown function DUF7910 (DUF7910)
Type: Domain

This domain is found in uncharacterised plant proteins. It is predicted to adopt beta-Trefoil fold. It is closely related to members of Fascin

.
Repeat of unknown function DUF7911 (DUF7911)
Type: Repeat

This domain is found in uncharacterised nematode proteins. It is predicted to fold into a five-bladed β-propeller.
Domain of unknown function DUF7912 (DUF7912)
Type: Domain

This domain is found in uncharacterised plant proteins. It is predicted to adopt an SH3-like fold.
Domain of unknown function DUF7913 (DUF7913)
Type: Domain

This domain is found in uncharacterised plant proteins. It is predicted to fold into an array of four α-helices.
Repeat of unknown function DUF7914 (DUF7914)
Type: Repeat

This domain is found in uncharacterised proteins mainly from Trypanosomes. It is predicted to fold into a seven-bladed β-propeller.
Domain of unknown function DUF7915 (DUF7915)
Type: Domain

This domain is found in uncharacterised plant proteins. It is predicted to fold into an α/β structure consisting of a central mixed β-sheet and α-helices packed on both sides. It is usually found C-terminal to

.
Domain of unknown function DUF7916 (DUF7916)
Type: Domain

This domain is found in uncharacterised bacterial proteins. It is predicted to adopt a TIM-barrel structure. It shares detectable similarity with Mycobacterium tuberculosis Indole-3-glycerol phosphate synthase (TrpC).
PAR-amplifying and CtIP-maintaining micropeptide (PACMP)
Type: Family

This protein family includes PAR-amplifying and CtIP-maintaining micropeptide (also known as Poly-ADP-ribosylation-amplifying and CtIP-maintaining micropeptide, PACMP). PACMP is recruited to DNA damage sites and acts as a regulator via association with poly-ADP-ribose chains, and enhances the poly-ADP-ribosyltransferase activity of PARP1 . This protein sequence is 44-residues long.
ParB, C-terminal dimerisation domain (ParB_dimer_C)
Type: Domain

This entry represents the C-terminal dimerisation domain found in ParB proteins. The dimerisation domain tightly links the two subunits of the ParB dimer . Structural analysis of the C-terminal domain reveals a dimer with a lysine-rich surface that binds DNA non-specifically and is essential for DNA condensation in vitro .

ParB plays a vital role in chromosome partitioning and nucleoid occlusion. These proteins are essential for ensuring proper chromosome segregation during cell division by binding to the DNA origin of replication and localising to both poles of the predivisional cell following DNA replication. ParB proteins share significant sequence and structural similarity with Sulfiredoxin (Srx), a sulfinic acid reductase identified in eukaryotes. Sequence comparison and phylogenetic analysis of the Srx and ParB protein families suggest that Srx evolved via truncation of ParB, resulting in the removal of the entire C-terminal half of the protein including the HTH domain . ParB comprises three highly conserved domains: an N-terminal nucleotide-binding domain (NBD)

, a central helix-turn-helix parS-binding domain

, non-structured linker region, and a C-terminal dimerisation domain

that tightly links the two subunits of the ParB dimer .
ParB-like, catalytic effector domain (Parb-CE)
Type: Domain

This entry represents a ParB-like domain predicted to act as a catalytic effector (CE) in multiple antiviral immunity systems and predicted to target nucleotides along with Calcineurin-CE, HD-CE and PRTase-CE .

ParB plays a vital role in chromosome partitioning and nucleoid occlusion. These proteins are essential for ensuring proper chromosome segregation during cell division by binding to the DNA origin of replication and localising to both poles of the predivisional cell following DNA replication. ParB proteins share significant sequence and structural similarity with Sulfiredoxin (Srx), a sulfinic acid reductase identified in eukaryotes. Sequence comparison and phylogenetic analysis of the Srx and ParB protein families suggest that Srx evolved via truncation of ParB, resulting in the removal of the entire C-terminal half of the protein including the HTH domain . ParB comprises three highly conserved domains: an N-terminal nucleotide-binding domain (NBD)

, a central helix-turn-helix parS-binding domain

, non-structured linker region, and a C-terminal dimerisation domain

that tightly links the two subunits of the ParB dimer .
PCFS4-like, zinc finger domain (PCFS4-like)
Type: Domain

This zinc finger domain is found in the homologues of polyadenylation and cleavage factor homolog 4 (PCFS4) including PCFS1, PCFS5 and other RNA-binding proteins in eukaryotes. This domain contains three highly conserved cysteine residues and histidine. Its structure is predicted to be similar to known Treble clef zinc finger domains.

PCFS4 is known to promote flowering by suppressing FLC-mediated inhibition of flowering through the regulation of FCA pre-mRNA alternative processing . This protein regulates mRNA maturation, including alternative polyadenylation, splicing or transcription initiation of stress-associated genes .
Integrins beta, I-EGF domain, conserved site (Integrin_I-EGF_CS)
Type: Conserved_site

This entry represents a conserved region of the I-EGF domain that includes five of the conserved cysteines.

The C terminus of the extracellular region of all the integrin beta chains has four cysteine-rich tandem repeats of forty amino acids, which are variants of the EGF-like domain, termed integrin- or I-EGF domains. The I-EGF domain is a small globular domain mainly composed by loops with a small anti-parallel β-sheet constituted of two β-strands (see

). The structure is stabilised by four disulfide bonds between the first and fifth, second and fourth, third and sixth, and seventh and eighth Cys residues. Three disulfide bonds are shared with classical EGF-like domains. The disulfide unique to I-EGF domains links the N terminus to the turn between the two β-strands. Compared to classical EGF-like modules with three disulfide bonds, the I-EGF module is less elongated, with a nosecone-like shape. The anti parallel sheet between the two β-strands is shortened because four highly conserved residues among classical EGF-like modules are deleted in I-EGF modules. I-EGF repeats in the integrin beta subunit stalk region relay activation signals to the ligand-binding headpiece .

Integrins are the major metazoan receptors for cell adhesion to extracellular matrix proteins and, in vertebrates, also play important roles in certain cell-cell adhesions, make transmembrane connections to the cytoskeleton, and activate many intracellular signalling pathways . An integrin receptor is a heterodimer composed of alpha and beta subunits. Each subunit crosses the membrane once, with most of the polypeptide residing in the extracellular space, and has two short cytoplasmic domains. Some members of this family have EGF repeats at the C terminus and also have a VWA domain inserted within the integrin domain at the N-terminal.

Most integrins recognise relatively short peptide motifs and, in general, require an acidic amino acid to be present. Ligand specificity depends upon both the alpha and beta subunits . There are at least 18 types of alpha and 8 types of beta subunits recognised in humans . Each alpha subunit tends to associate only with one type of beta subunit, but there are exceptions to this rule . Each association of alpha and beta subunits has its binding specificity and signalling properties. Many integrins require activation on the cell surface before they can bind ligands. Integrins frequently intercommunicate, and binding at one integrin receptor activates or inhibits another.
Zinc carboxypeptidases, zinc-binding region 1 (CARBOXYPEPT_ZN_1)
Type: Binding_site

There are conserved sites matching these three zinc-ligands - this entry and

. If a protein includes both signatures, the probability of it being a eukaryotic zinc carboxypeptidase is very high.

There are a number of different types of zinc-dependent carboxypeptidases (EC 3.4.17.-) . All these enzymes seem to be structurally and functionally related. Some enzymes that belong to this family are listed below.

Carboxypeptidase A1 (EC 3.4.17.1), a pancreatic digestive enzyme that can remove all C-terminal amino acids with the exception of Arg, Lys and Pro.

Carboxypeptidase A2 (EC 3.4.17.15), a pancreatic digestive enzyme with a specificity similar to that of carboxypeptidase A1, but with a preference for bulkier C-terminal residues.

Carboxypeptidase B (EC 3.4.17.2), also a pancreatic digestive enzyme, but that preferentially removes C-terminal Arg and Lys.

Carboxypeptidase N (EC 3.4.17.3) (also known as arginine carboxypeptidase), a plasma enzyme which protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation.

Carboxypeptidase H (EC 3.4.17.10) (also known as enkephalin convertase or carboxypeptidase E), an enzyme located in secretory granules of pancreatic islets, adrenal gland, pituitary and brain. This enzyme removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing.

Carboxypeptidase M (EC 3.4.17.12), a membrane bound Arg and Lys specific
enzyme.

Mast cell carboxypeptidase (EC 3.4.17.1), an enzyme with a specificity to carboxypeptidase A, but found in the secretory granules of mast cells.

Streptomyces griseus carboxypeptidase (Cpase SG) (EC 3.4.17.-) , which combines the specificities of mammalian carboxypeptidases A and B.

Thermoactinomyces vulgaris carboxypeptidase T (EC 3.4.17.18) (CPT) , which also combines the specificities of carboxypeptidases A and B.

All of these enzymes bind an atom of zinc. Three conserved residues are implicated in the binding of the zinc atom: two histidines and a glutamic acid.