MAG: hypothetical protein BZY64_00945 [SAR202 cluster bacterium Ae2-Chloro-G1]
MoaD/ThiS family protein( domain architecture ID 10091490)
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 | cd00754 | ubiquitin-like (Ubl) domain found in molybdenum cofactor biosynthesis protein D (MoaD) and ... |
8-65 | 4.84e-17 | ||
ubiquitin-like (Ubl) domain found in molybdenum cofactor biosynthesis protein D (MoaD) and similar proteins; MoaD, also termed molybdopterin synthase sulfur carrier subunit, or MPT synthase subunit 1, or MPT synthase small subunit, or molybdopterin-converting factor small subunit, or molybdopterin-converting factor subunit 1, is a conserved small sulfur carrier protein that has beta-grasp ubiquitin-like (Ubl) fold involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor of a diverse group of redox enzymes. MoaD is activated in an ATP-dependent manner by sulfurtransferases similar to the activation mechanism of ubiquitin-activating enzyme E1. : Pssm-ID: 340452 Cd Length: 79 Bit Score: 67.99 E-value: 4.84e-17
|
||||||
Name | Accession | Description | Interval | E-value | ||
Ubl_MoaD | cd00754 | ubiquitin-like (Ubl) domain found in molybdenum cofactor biosynthesis protein D (MoaD) and ... |
8-65 | 4.84e-17 | ||
ubiquitin-like (Ubl) domain found in molybdenum cofactor biosynthesis protein D (MoaD) and similar proteins; MoaD, also termed molybdopterin synthase sulfur carrier subunit, or MPT synthase subunit 1, or MPT synthase small subunit, or molybdopterin-converting factor small subunit, or molybdopterin-converting factor subunit 1, is a conserved small sulfur carrier protein that has beta-grasp ubiquitin-like (Ubl) fold involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor of a diverse group of redox enzymes. MoaD is activated in an ATP-dependent manner by sulfurtransferases similar to the activation mechanism of ubiquitin-activating enzyme E1. Pssm-ID: 340452 Cd Length: 79 Bit Score: 67.99 E-value: 4.84e-17
|
||||||
MoaD | COG1977 | Molybdopterin synthase sulfur carrier subunit MoaD [Coenzyme transport and metabolism]; ... |
8-65 | 6.60e-14 | ||
Molybdopterin synthase sulfur carrier subunit MoaD [Coenzyme transport and metabolism]; Molybdopterin synthase sulfur carrier subunit MoaD is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 441580 [Multi-domain] Cd Length: 82 Bit Score: 59.83 E-value: 6.60e-14
|
||||||
moaD | TIGR01682 | molybdopterin converting factor, subunit 1, non-archaeal; This model describes MoaD. It ... |
13-65 | 6.03e-13 | ||
molybdopterin converting factor, subunit 1, non-archaeal; This model describes MoaD. It excludes archaeal homologs, since many Archaea have two MoaD-like proteins, suggesting two different functions. pfam02597 describes both the thiamine biosynthesis protein ThiS and this protein, MoaD, a subunit (together with MoaE, pfam02391) of the molybdopterin converting factor. Both ThiS and MoaD are involved in sulfur transfer reactions. Distribution of this family appears limited to species that also have a member of pfam02391, but a number of Archaea have two different members, suggesting functionally distinct subtypes. The C-terminal Gly-Gly of this model is critical to function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin] Pssm-ID: 273753 Cd Length: 80 Bit Score: 57.69 E-value: 6.03e-13
|
||||||
PLN02799 | PLN02799 | Molybdopterin synthase sulfur carrier subunit |
2-65 | 1.25e-12 | ||
Molybdopterin synthase sulfur carrier subunit Pssm-ID: 215429 Cd Length: 82 Bit Score: 56.94 E-value: 1.25e-12
|
||||||
ThiS | pfam02597 | ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in ... |
12-65 | 9.31e-11 | ||
ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalyzed by IscS. MoaD, a protein involved sulphur transfer in molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end. Pssm-ID: 396932 [Multi-domain] Cd Length: 74 Bit Score: 51.90 E-value: 9.31e-11
|
||||||
Name | Accession | Description | Interval | E-value | ||
Ubl_MoaD | cd00754 | ubiquitin-like (Ubl) domain found in molybdenum cofactor biosynthesis protein D (MoaD) and ... |
8-65 | 4.84e-17 | ||
ubiquitin-like (Ubl) domain found in molybdenum cofactor biosynthesis protein D (MoaD) and similar proteins; MoaD, also termed molybdopterin synthase sulfur carrier subunit, or MPT synthase subunit 1, or MPT synthase small subunit, or molybdopterin-converting factor small subunit, or molybdopterin-converting factor subunit 1, is a conserved small sulfur carrier protein that has beta-grasp ubiquitin-like (Ubl) fold involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor of a diverse group of redox enzymes. MoaD is activated in an ATP-dependent manner by sulfurtransferases similar to the activation mechanism of ubiquitin-activating enzyme E1. Pssm-ID: 340452 Cd Length: 79 Bit Score: 67.99 E-value: 4.84e-17
|
||||||
MoaD | COG1977 | Molybdopterin synthase sulfur carrier subunit MoaD [Coenzyme transport and metabolism]; ... |
8-65 | 6.60e-14 | ||
Molybdopterin synthase sulfur carrier subunit MoaD [Coenzyme transport and metabolism]; Molybdopterin synthase sulfur carrier subunit MoaD is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 441580 [Multi-domain] Cd Length: 82 Bit Score: 59.83 E-value: 6.60e-14
|
||||||
moaD | TIGR01682 | molybdopterin converting factor, subunit 1, non-archaeal; This model describes MoaD. It ... |
13-65 | 6.03e-13 | ||
molybdopterin converting factor, subunit 1, non-archaeal; This model describes MoaD. It excludes archaeal homologs, since many Archaea have two MoaD-like proteins, suggesting two different functions. pfam02597 describes both the thiamine biosynthesis protein ThiS and this protein, MoaD, a subunit (together with MoaE, pfam02391) of the molybdopterin converting factor. Both ThiS and MoaD are involved in sulfur transfer reactions. Distribution of this family appears limited to species that also have a member of pfam02391, but a number of Archaea have two different members, suggesting functionally distinct subtypes. The C-terminal Gly-Gly of this model is critical to function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin] Pssm-ID: 273753 Cd Length: 80 Bit Score: 57.69 E-value: 6.03e-13
|
||||||
PLN02799 | PLN02799 | Molybdopterin synthase sulfur carrier subunit |
2-65 | 1.25e-12 | ||
Molybdopterin synthase sulfur carrier subunit Pssm-ID: 215429 Cd Length: 82 Bit Score: 56.94 E-value: 1.25e-12
|
||||||
ThiS | pfam02597 | ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in ... |
12-65 | 9.31e-11 | ||
ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalyzed by IscS. MoaD, a protein involved sulphur transfer in molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end. Pssm-ID: 396932 [Multi-domain] Cd Length: 74 Bit Score: 51.90 E-value: 9.31e-11
|
||||||
Ubl_MoaD_like | cd17040 | ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins; Ubiquitin-like ... |
13-65 | 1.48e-05 | ||
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: 38.90 E-value: 1.48e-05
|
||||||
moaD | PRK11130 | molybdopterin synthase small subunit; Provisional |
37-65 | 1.02e-04 | ||
molybdopterin synthase small subunit; Provisional Pssm-ID: 182985 Cd Length: 81 Bit Score: 36.48 E-value: 1.02e-04
|
||||||
Ubl_SAMP2_like | cd17506 | ubiquitin-like (Ubl) domain found in small archaeal modifier protein (SAMP2); Ubiquitin-like ... |
13-65 | 3.46e-04 | ||
ubiquitin-like (Ubl) domain found in small archaeal modifier protein (SAMP2); Ubiquitin-like small archaeal modifier protein 2 (SAMP2) shows a beta-grasp fold of Ub, suggesting that this archaeal Ubl molecule is more closely related to eukaryotic Ub and Ubls than to its prokaryotic counterpart. Several Ub-like structural features such as an N-terminal single lysine residue and di-glycine motif at the C-terminus, spatially isolated, implicate formation of a poly-SAMPylated chainpoly-SAMPylation. SAMP2 can form covalent conjugates with its protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. It 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. SAMP2 is involved in sulfur transfer during tRNA thiolation much like Urm1. This family also includes uncharacterized proteins such as Methanothermococcus thermolithotrophicus Mth1743, Pyrococcus furiosus PF1061 and others, all closely related to proteins MoaD. Pssm-ID: 340763 Cd Length: 67 Bit Score: 35.00 E-value: 3.46e-04
|
||||||
moaD_arch | TIGR01687 | MoaD family protein, archaeal; Members of this family appear to be archaeal versions of MoaD, ... |
9-65 | 4.00e-04 | ||
MoaD family protein, archaeal; Members of this family appear to be archaeal versions of MoaD, subunit 1 of molybdopterin converting factor. This model has been split from the bacterial/eukaryotic equivalog model TIGR01682 because the presence of two members of this family in a substantial number of archaeal species suggests that roles might not be interchangeable. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin] Pssm-ID: 273758 Cd Length: 88 Bit Score: 35.11 E-value: 4.00e-04
|
||||||
Blast search parameters | ||||
|