hypothetical protein AUH31_01870 [Armatimonadetes bacterium 13_1_40CM_64_14]
Protein Classification
MoaD/ThiS family protein( domain architecture ID 13018328)
MoaD/ThiS family protein is a ubiquitin-like protein, may be involved in sulfur transfer
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| Ubl_MoaD_like | cd17040 | ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins; Ubiquitin-like ... |
2-98 | 2.22e-11 | |||
ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins; Ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins This family includes ThiS, MoaD, CysO, QbsE, and their homologs, which are structurally homologous to ubiquitin (Ub) and may function as the sulfide donor for the biosynthesis of thiamin, molybdopterin, cysteine, thioquinolobactin, and other sulfur-containing natural products. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. Like Ub, small sulfide carrier proteins in this family are adenylated at a diglycyl C-terminus by specific activating proteins. The adenylated C-terminus is subsequently converted to a thiocarboxylate, serving as the sulfide source. Those activating proteins are diverse and show little sequence similarity. This family also includes the small archaeal modifier protein (SAMP), including SAMP1, SAMP2 and SAMP3, which are Ub-like proteins that function as protein modifiers and are required for the production of sulfur-containing biomolecules in the archaeon Haloferax volcanii. SAMP1 and SAMP2 are involved in sulfur transfer during molybdenum cofactor biosynthesis and tRNA thiolation much like MoaD and Urm1, respectively. They can form covalent conjugates with their protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. SAMP2 also forms homo-conjugates through the intermolecular isopeptide bond between the C-terminal Gly and the Lys58 side chain, a feature that likely resembles polyubiquitination. SAMP3 conjugates are dependent on the Ub-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease HvJAMM1. : Pssm-ID: 340560 [Multi-domain] Cd Length: 88 Bit Score: 54.69 E-value: 2.22e-11
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| Name | Accession | Description | Interval | E-value | |||
| Ubl_MoaD_like | cd17040 | ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins; Ubiquitin-like ... |
2-98 | 2.22e-11 | |||
ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins; Ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins This family includes ThiS, MoaD, CysO, QbsE, and their homologs, which are structurally homologous to ubiquitin (Ub) and may function as the sulfide donor for the biosynthesis of thiamin, molybdopterin, cysteine, thioquinolobactin, and other sulfur-containing natural products. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. Like Ub, small sulfide carrier proteins in this family are adenylated at a diglycyl C-terminus by specific activating proteins. The adenylated C-terminus is subsequently converted to a thiocarboxylate, serving as the sulfide source. Those activating proteins are diverse and show little sequence similarity. This family also includes the small archaeal modifier protein (SAMP), including SAMP1, SAMP2 and SAMP3, which are Ub-like proteins that function as protein modifiers and are required for the production of sulfur-containing biomolecules in the archaeon Haloferax volcanii. SAMP1 and SAMP2 are involved in sulfur transfer during molybdenum cofactor biosynthesis and tRNA thiolation much like MoaD and Urm1, respectively. They can form covalent conjugates with their protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. SAMP2 also forms homo-conjugates through the intermolecular isopeptide bond between the C-terminal Gly and the Lys58 side chain, a feature that likely resembles polyubiquitination. SAMP3 conjugates are dependent on the Ub-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease HvJAMM1. Pssm-ID: 340560 [Multi-domain] Cd Length: 88 Bit Score: 54.69 E-value: 2.22e-11
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| Name | Accession | Description | Interval | E-value | |||
| Ubl_MoaD_like | cd17040 | ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins; Ubiquitin-like ... |
2-98 | 2.22e-11 | |||
ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins; Ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins This family includes ThiS, MoaD, CysO, QbsE, and their homologs, which are structurally homologous to ubiquitin (Ub) and may function as the sulfide donor for the biosynthesis of thiamin, molybdopterin, cysteine, thioquinolobactin, and other sulfur-containing natural products. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. Like Ub, small sulfide carrier proteins in this family are adenylated at a diglycyl C-terminus by specific activating proteins. The adenylated C-terminus is subsequently converted to a thiocarboxylate, serving as the sulfide source. Those activating proteins are diverse and show little sequence similarity. This family also includes the small archaeal modifier protein (SAMP), including SAMP1, SAMP2 and SAMP3, which are Ub-like proteins that function as protein modifiers and are required for the production of sulfur-containing biomolecules in the archaeon Haloferax volcanii. SAMP1 and SAMP2 are involved in sulfur transfer during molybdenum cofactor biosynthesis and tRNA thiolation much like MoaD and Urm1, respectively. They can form covalent conjugates with their protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. SAMP2 also forms homo-conjugates through the intermolecular isopeptide bond between the C-terminal Gly and the Lys58 side chain, a feature that likely resembles polyubiquitination. SAMP3 conjugates are dependent on the Ub-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease HvJAMM1. Pssm-ID: 340560 [Multi-domain] Cd Length: 88 Bit Score: 54.69 E-value: 2.22e-11
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| Ubl_CysO_like | cd17074 | ubiquitin-like (Ubl) domain found in Mycobacterium tuberculosis CysO and similar proteins; ... |
2-98 | 7.46e-07 | |||
ubiquitin-like (Ubl) domain found in Mycobacterium tuberculosis CysO and similar proteins; CysO, also termed 9.5 kDa culture filtrate antigen cfp10A, together with CysM (Cysteine synthase M), forms a protein complex CysM-CysO that represents a new cysteine biosynthetic pathway in Mycobacterium tuberculosis. The replacement of the acetyl group of O-acetylserine by CysO thiocarboxylate to generate a protein-bound cysteine is catalyzed by CysM in a pyridoxal 5?-phosphate (PLP)-dependent manner. The family also includes QbsE that functions as the sulfide donor for the biosynthesis of thioquinolobactin in Pseudomonas fluorescens. A JAMM motif protein QbsD catalyzes removal of the carboxy-terminal dipeptide from QbsE. Both CysO and QbsE are similar to prokaryotic sulfur carrier proteins such as ThiS and MoaD, containing the beta-grasp ubiquitin-like fold. Pssm-ID: 340594 Cd Length: 89 Bit Score: 43.04 E-value: 7.46e-07
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