Protein Family Models

SPX (Syg1, Pho81 and XPR1) and EXS (ERD1, XPR1, and SYG1) domain-containing protein similar to Homo sapiens xenotropic and polytropic retrovirus receptor 1 (XPR1) that plays a role in phosphate homeostasis

Date:

2024-01-09

primase-helicase family protein is a DUF5906 domain-containing protein and may belong to the P-loop containing NTPase superfamily

Date:

2023-11-29

adenosine deaminase family protein such as tRNA-specific adenosine deaminase 1 (TAD1), which is similar to yeast tRNA-specific adenosine deaminase that deaminates adenosine-37 to inosine in tRNA-Ala

Date:

2023-11-15

picornavirus capsid protein is a component of the capsid (protein coat) which encloses the viral genome; it may play roles in the infection cycle

Date:

2023-10-31

C-terminal domains (CTDs) of ABC-3C systems, contain distinct patterns of charged and polar residues and are not yet unifiable with known domains. These domains are found at the C-terminus of the effector component of the systems, which are upstream of the Middle Component and ABC ATPase components on the genome. Due to the typically large size of these CTDs relative to the actual effector and MC domains, the CTDs are predicted to serves as the platform on which the remaining two components assemble. Therewith, conformational changes transmitted by the ABC ATPase-mediated detection of invasive elements like DNA viruses would result in an unfurling and activation of the CTD-associated effector [1]. (from Pfam)

Date:

2023-12-12

C-terminal domains (CTDs) of ABC-3C systems, contain distinct patterns of charged and polar residues and are not yet unifiable with known domains. These domains are found at the C-terminus of the effector component of the systems, which are upstream of the Middle Component and ABC ATPase components on the genome. Due to the typically large size of these CTDs relative to the actual effector and MC domains, the CTDs are predicted to serve as the platform on which the remaining two components assemble. Therewith, conformational changes transmitted by the ABC ATPase-mediated detection of invasive elements like DNA viruses would result in an unfurling and activation of the CTD-associated effector [1]. (from Pfam)

Date:

2023-12-12

Middle Components (MCs) of the ABC-3C biological conflict systems occupy the central position between the catalytic effector and ABC ATPases of the systems. MCs are defined by distinctive patterns of conserved charged residues. As some MCs are HTH domains, they are predicted to function akin to kleisins as DNA-binding partners for the ABC ATPases, assisting in recognition and responding to invasive elements such as DNA viruses [1]. (from Pfam)

Date:

2023-12-12

This presumed domain is functionally uncharacterised. This domain family is found in Proteobacteria and viruses, and is approximately 90 amino acids in length. It contains the conserved motifs FDD and MGGW. (from Pfam)

Date:

2023-12-12

This presumed domain is functionally uncharacterised. This domain family is found in bacteria and viruses, and is approximately 80 amino acids in length. It has a conserved sequence GGLxxxGRxxY and a conserved tryptophan residue at the C-terminal. (from Pfam)

Date:

2023-12-12

This is a family of uncharacterised proteins of unknown function predominantly found in viruses. (from Pfam)

Date:

2023-12-12

This is a family of uncharacterised proteins of unknown function predominantly found in viruses. (from Pfam)

Date:

2023-12-12

This is a family of uncharacterised proteins of known function found in viruses, particularly in Conferred and Mummified. (from Pfam)

Date:

2023-12-12

This is a family of uncharacterised proteins of unknown function found in viruses. It is thought to be part of the early transcription factor large subunit. (from Pfam)

Date:

2023-12-12

This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria, archaea and viruses. Proteins in this family are typically between 89 and 148 amino acids in length. (from Pfam)

Date:

2023-12-12

This presumed domain is functionally uncharacterised. This domain family is found in bacteria and viruses, and is approximately 110 amino acids in length. This domain is predicted to contain a complex four helical bundle structure. The structure shows similarity to the single stranded binding protein DnaT. (from Pfam)

Date:

2023-12-12

Birnaviruses are dsRNA viruses. This entry corresponds to the C-terminal domain of RNA dependent RNA polymerase also known as VP1. All of the birnavirus VP1 proteins contain conserved RdRp motifs that reside in the catalytic "palm" domain of all classes of polymerases. However, the birnavirus RdRps lack the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RdRps [1]. This RdRp has the five essential RNA polymerase motifs in a permuted order of C-A-B-D-E to form a conserved catalytic active site [2,3]. This domain is mostly alpha-helical that runs across the canyon in the front of the palm, and wraps around the fingers subdomain [2], which may function to prevent back-primed RNA synthesis during protein priming. (from Pfam)

Date:

2023-12-12

This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria and viruses. Proteins in this family are typically between 115 and 155 amino acids in length. (from Pfam)

Date:

2023-12-12

Middle Components (MCs) of the ABC-3C biological conflict systems occupy the central position between the catalytic effector and ABC ATPases of the systems. MCs are defined by distinctive patterns of conserved charged residues. As some MCs are HTH domains, they are predicted to function akin to kleisins as DNA-binding partners for the ABC ATPases, assisting in recognition and responding to invasive elements such as DNA viruses. MC7 is a MC unifiable with the HTH fold [1]. (from Pfam)

Date:

2023-12-12

Middle Components (MCs) of the ABC-3C biological conflict systems occupy the central position between the catalytic effector and ABC ATPases of the systems. MCs are defined by distinctive patterns of conserved charged residues. As some MCs are HTH domains, they are predicted to function akin to kleisins as DNA-binding partners for the ABC ATPases, assisting in recognition and responding to invasive elements such as DNA viruses [1]. (from Pfam)

Date:

2023-12-12

C-terminal domains (CTDs) of ABC-3C systems, contain distinct patterns of charged and polar residues and are not yet unifiable with known domains. These domains are found at the C-terminus of the effector component of the systems, which are upstream of the Middle Component and ABC ATPase components on the genome. Due to the typically large size of these CTDs relative to the actual effector and MC domains, the CTDs are predicted to serve as the platform on which the remaining two components assemble. Therewith, conformational changes transmitted by the ABC ATPase-mediated detection of invasive elements like DNA viruses would result in an unfurling and activation of the CTD-associated effector [1]. (from Pfam)

Date:

2023-12-12