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Conserved domains on  [gi|616689193|gb|KAE86798|]
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molybdopterin synthase sulfur carrier subunit [Staphylococcus aureus VET0402R]

Protein Classification

MoaD/ThiS family protein( domain architecture ID 10091490)

MoaD/ThiS family protein is a ubiquitin-like protein, may be involved in sulfur transfer

Graphical summary

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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 ...
1-77 1.33e-23

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: 84.55  E-value: 1.33e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616689193  1 MKVLYFAEIKDILQKAQEDIVLEQALTVQQFEILLFERYPQINN--KKFQVAVNEEFVQKSDFIQPNDTVALIPPVSGG 77
Cdd:cd00754   1 VKVLYFARARELAGKSEEELELPAGTTVEELLEELAAKYPALAAilKSVRVAVNQEYVDDDTELKDGDEVAFIPPVSGG 79
 
Name Accession Description Interval E-value
Ubl_MoaD cd00754
ubiquitin-like (Ubl) domain found in molybdenum cofactor biosynthesis protein D (MoaD) and ...
1-77 1.33e-23

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: 84.55  E-value: 1.33e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616689193  1 MKVLYFAEIKDILQKAQEDIVLEQALTVQQFEILLFERYPQINN--KKFQVAVNEEFVQKSDFIQPNDTVALIPPVSGG 77
Cdd:cd00754   1 VKVLYFARARELAGKSEEELELPAGTTVEELLEELAAKYPALAAilKSVRVAVNQEYVDDDTELKDGDEVAFIPPVSGG 79
MoaD COG1977
Molybdopterin synthase sulfur carrier subunit MoaD [Coenzyme transport and metabolism]; ...
1-77 1.69e-20

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: 76.78  E-value: 1.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616689193  1 MKVLYFAEIKDILQKAQEDIVLEQALTVQQFEILLFERYPQ----INNKKFQVAVNEEFVQKSDFIQPNDTVALIPPVSG 76
Cdd:COG1977   2 VTVRYFAALREAAGKSEEEVELPEGATVGDLLEALAARYPGlaerLLRRRVRVAVNGEDVRLDTPLKDGDEVALFPPVAG 81

                .
gi 616689193 77 G 77
Cdd:COG1977  82 G 82
moaD TIGR01682
molybdopterin converting factor, subunit 1, non-archaeal; This model describes MoaD. It ...
1-77 1.06e-17

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: 69.63  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616689193   1 MKVLYFAEIKDILQKAQEDIVLEQAL-TVQQFEILLFERYPQIN--NKKFQVAVNEEFVQKSDFIQPNDTVALIPPVSGG 77
Cdd:TIGR01682  1 IKVLYFARLREQAGTDEETLELPDEStTVGELKEHLAKEGPELAasRGQVMVAVNEEYVTDDALLNEGDEVAFIPPVSGG 80
ThiS pfam02597
ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in ...
3-77 3.66e-13

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: 58.07  E-value: 3.66e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616689193   3 VLYFAEIKDILQKAQEDivlEQALTVQQFEILLFERYPQiNNKKFQVAVNEEFVQKSDF---IQPNDTVALIPPVSGG 77
Cdd:pfam02597  1 VLLNAELRELAGKDEEL---AEGATVAELLEALGLRYPE-LRERVAVAVNGEIVPRLWLdtpLKDGDEVAIIPPVGGG 74
PLN02799 PLN02799
Molybdopterin synthase sulfur carrier subunit
2-77 2.11e-11

Molybdopterin synthase sulfur carrier subunit


Pssm-ID: 215429  Cd Length: 82  Bit Score: 53.86  E-value: 2.11e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616689193  2 KVLYFAEIKDILQKAQEDIVLEQALTVQQFEILLFERYPQINN--KKFQVAVNEEFVQKSDFIQPNDTVALIPPVSGG 77
Cdd:PLN02799  5 KVLFFARARELTGVSDMTLELPAGSTTADCLAELVAKFPSLEEvrSCCVLALNEEYTTESAALKDGDELAIIPPISGG 82
 
Name Accession Description Interval E-value
Ubl_MoaD cd00754
ubiquitin-like (Ubl) domain found in molybdenum cofactor biosynthesis protein D (MoaD) and ...
1-77 1.33e-23

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: 84.55  E-value: 1.33e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616689193  1 MKVLYFAEIKDILQKAQEDIVLEQALTVQQFEILLFERYPQINN--KKFQVAVNEEFVQKSDFIQPNDTVALIPPVSGG 77
Cdd:cd00754   1 VKVLYFARARELAGKSEEELELPAGTTVEELLEELAAKYPALAAilKSVRVAVNQEYVDDDTELKDGDEVAFIPPVSGG 79
MoaD COG1977
Molybdopterin synthase sulfur carrier subunit MoaD [Coenzyme transport and metabolism]; ...
1-77 1.69e-20

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: 76.78  E-value: 1.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616689193  1 MKVLYFAEIKDILQKAQEDIVLEQALTVQQFEILLFERYPQ----INNKKFQVAVNEEFVQKSDFIQPNDTVALIPPVSG 76
Cdd:COG1977   2 VTVRYFAALREAAGKSEEEVELPEGATVGDLLEALAARYPGlaerLLRRRVRVAVNGEDVRLDTPLKDGDEVALFPPVAG 81

                .
gi 616689193 77 G 77
Cdd:COG1977  82 G 82
moaD TIGR01682
molybdopterin converting factor, subunit 1, non-archaeal; This model describes MoaD. It ...
1-77 1.06e-17

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: 69.63  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616689193   1 MKVLYFAEIKDILQKAQEDIVLEQAL-TVQQFEILLFERYPQIN--NKKFQVAVNEEFVQKSDFIQPNDTVALIPPVSGG 77
Cdd:TIGR01682  1 IKVLYFARLREQAGTDEETLELPDEStTVGELKEHLAKEGPELAasRGQVMVAVNEEYVTDDALLNEGDEVAFIPPVSGG 80
ThiS pfam02597
ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in ...
3-77 3.66e-13

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: 58.07  E-value: 3.66e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616689193   3 VLYFAEIKDILQKAQEDivlEQALTVQQFEILLFERYPQiNNKKFQVAVNEEFVQKSDF---IQPNDTVALIPPVSGG 77
Cdd:pfam02597  1 VLLNAELRELAGKDEEL---AEGATVAELLEALGLRYPE-LRERVAVAVNGEIVPRLWLdtpLKDGDEVAIIPPVGGG 74
PLN02799 PLN02799
Molybdopterin synthase sulfur carrier subunit
2-77 2.11e-11

Molybdopterin synthase sulfur carrier subunit


Pssm-ID: 215429  Cd Length: 82  Bit Score: 53.86  E-value: 2.11e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616689193  2 KVLYFAEIKDILQKAQEDIVLEQALTVQQFEILLFERYPQINN--KKFQVAVNEEFVQKSDFIQPNDTVALIPPVSGG 77
Cdd:PLN02799  5 KVLFFARARELTGVSDMTLELPAGSTTADCLAELVAKFPSLEEvrSCCVLALNEEYTTESAALKDGDELAIIPPISGG 82
Ubl_MoaD_like cd17040
ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins; Ubiquitin-like ...
1-77 1.76e-08

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: 46.60  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616689193  1 MKVLYFAEIKDiLQKAQEDIVLEQALTVQqfEIL--LFERYPQIN---------NKKFQVAVNEEFVQKSDF---IQPND 66
Cdd:cd17040   1 VKVRLFGALRE-AGAGEEEIEVEGGTTVR--DLLdaLSERYPGLFealdedgelRPFILVFVNGRDVRLDDGltpLKDGD 77
                        90
                ....*....|.
gi 616689193 67 TVALIPPVSGG 77
Cdd:cd17040  78 EVDILPPVAGG 88
ThiS COG2104
Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]; ...
17-77 1.03e-06

Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]; Sulfur carrier protein ThiS (thiamine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 441707 [Multi-domain]  Cd Length: 66  Bit Score: 41.60  E-value: 1.03e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616689193 17 QEDIVLEQALTVQQFEILLferypQINNKKFQVAVNEEFVQKSDF----IQPNDTVALIPPVSGG 77
Cdd:COG2104   7 GEPREVPEGTTLADLLEEL-----GLDPKGVAVAVNGEIVPRSQWastvLKEGDRVEIVTAVGGG 66
moaD_arch TIGR01687
MoaD family protein, archaeal; Members of this family appear to be archaeal versions of MoaD, ...
2-77 2.72e-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: 35.88  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616689193   2 KVLYFAEIKDILQKAQEDIVLEQAlTVQQFEILLFERYPQINNKKFQ----------VAVNEEFVQKSDF--IQPNDTVA 69
Cdd:TIGR01687  2 RVKYFATLRDITGKKSEEIEIEGK-TVGDLLNELMARYPKEFSELFKeglglvpnviILVNGRNVDWGLGteLKDGDVVA 80

                 ....*...
gi 616689193  70 LIPPVSGG 77
Cdd:TIGR01687 81 IFPPVSGG 88
Ubl_SAMP2_like cd17506
ubiquitin-like (Ubl) domain found in small archaeal modifier protein (SAMP2); Ubiquitin-like ...
42-77 1.01e-03

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: 33.85  E-value: 1.01e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 616689193 42 INNKKFQVAVNEEFVQKSDFIQPNDTVALIPPVSGG 77
Cdd:cd17506  32 LPPEEVIVVVNGEVVPEDDPLKDGDIIRLIPVVSGG 67
moaD PRK11130
molybdopterin synthase small subunit; Provisional
2-77 2.16e-03

molybdopterin synthase small subunit; Provisional


Pssm-ID: 182985  Cd Length: 81  Bit Score: 33.40  E-value: 2.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616689193  2 KVLYFAEIKDILqkAQEDIVLEQAL-TVQQFEILLFERYPQ----INNKKFQVAVNEEFVQKSDFIQPNDTVALIPPVSG 76
Cdd:PRK11130  3 KVLFFAQVRELV--GTDALELAADFpTVEALRQHLAQKGDRwalaLEDGKLLAAVNQTLVSFDHPLTDGDEVAFFPPVTG 80

                .
gi 616689193 77 G 77
Cdd:PRK11130 81 G 81
Ubl_ThiS cd00565
ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS; ThiS, also termed Thiamine ...
17-77 2.94e-03

ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS; ThiS, also termed Thiamine biosynthesis protein (ThiaminS), is a sulfur carrier protein involved in thiamin biosynthesis in prokaryotes. It has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub), and is activated in an ATP-dependent manner by sulfurtransferases, similar to the activation mechanism of Ub-activating enzyme E1. ThiS has common evolutionary origin with Ub-related protein modifiers in eukaryotes, a beta-grasp fold as Ub, and is closely related to proteins MoaD and Urm1.


Pssm-ID: 340451 [Multi-domain]  Cd Length: 64  Bit Score: 32.48  E-value: 2.94e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616689193 17 QEDIVLEQALTVQQFeiLLFERYPQinnKKFQVAVNEEFVQKSDF----IQPNDTVALIPPVSGG 77
Cdd:cd00565   5 GEPREVDEGLTLAEL--LEELGFTP---KGVAVELNGEIVPRSEWaetiLKDGDRIEIVTFVGGG 64
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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