MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436   97 LSLSEADAFLVKPEYGAQAYFMGTVRSPNQGQVVEYIDYEAFAPMAEKVMREAAALARERHGELRVWIEHRTGRLTPAVA 176
Cdd:cd00756   1 FDLAELLAALRDPEAGAVVTFVGTVRDHDEGKGVEALEYEAYPPMAEKELEEIAEEARERWGLLRVAIIHRVGRLPPGEA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6460436  177 SIVIGVASPHRRPALEACDFLIEHLKIELPIWKHEADGRGEHWV 220
Cdd:cd00756  81 IVLVAVSSPHRKEAFEACEFLIDRLKHRAPIWKKEIFEGGEEWV 124

MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436   97 LSLSEADAFLVKPEYGAQAYFMGTVRSPNQGQVVEYIDYEAFAPMAEKVMREAAALARERHGELRVWIEHRTGRLTPAVA 176
Cdd:cd00756   1 FDLAELLAALRDPEAGAVVTFVGTVRDHDEGKGVEALEYEAYPPMAEKELEEIAEEARERWGLLRVAIIHRVGRLPPGEA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6460436  177 SIVIGVASPHRRPALEACDFLIEHLKIELPIWKHEADGRGEHWV 220
Cdd:cd00756  81 IVLVAVSSPHRKEAFEACEFLIDRLKHRAPIWKKEIFEGGEEWV 124

MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of molybdopterin. Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Converting factor contains the MoaE and MoaD proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436     92 VTADPLSLSEADAFLVKPEYGAQAYFMGTVRSPNQGQVVEYIDYEAFAPMAEKVMREAAALARERHGELRVWIEHRTGRL 171
Cdd:pfam02391   1 ITEEPLDVAEIAALVSDPEAGAVVTFVGTVRDHFDGKKVTALEYEAYPPMAEKELAEIAEEARERWPLLDVAIVHRVGRL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 6460436    172 TPAVASIVIGVASPHRRPALEACDFLIEHLK 202
Cdd:pfam02391  81 PVGEAIVLVAVSSPHRAEAFEACEYLIDELK 111

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436      3 VRAVFFARLRREVGLEELTLDVPDG-ADVRAVAEHLEQERG---VSLRGCMVAVNETYASPEHLLREGDEVAFLPPVAGG 78
Cdd:TIGR01682   1 IKVLYFARLREQAGTDEETLELPDEsTTVGELKEHLAKEGPelaASRGQVMVAVNEEYVTDDALLNEGDEVAFIPPVSGG 80

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6460436    3 VRAVFFARLRREVGLEELTLDVPDGADVRAVAEHLEQ---ERGVSLRGCMVAVNETYASPEHLLREGDEVAFLPPVAGG 78
Cdd:cd00754   1 VKVLYFARARELAGKSEEELELPAGTTVEELLEELAAkypALAAILKSVRVAVNQEYVDDDTELKDGDEVAFIPPVSGG 79

Molybdopterin synthase sulfur carrier subunit

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436     1 MQVRAVFFARLRREVGLEELTLDVPDGADVRA-VAEHLEQERGV-SLRGCMV-AVNETYASPEHLLREGDEVAFLPPVAG 77
Cdd:PLN02799   2 VEIKVLFFARARELTGVSDMTLELPAGSTTADcLAELVAKFPSLeEVRSCCVlALNEEYTTESAALKDGDELAIIPPISG 81

                 .
gi 6460436    78 G 78
Cdd:PLN02799  82 G 82

MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436   97 LSLSEADAFLVKPEYGAQAYFMGTVRSPNQGQVVEYIDYEAFAPMAEKVMREAAALARERHGELRVWIEHRTGRLTPAVA 176
Cdd:cd00756   1 FDLAELLAALRDPEAGAVVTFVGTVRDHDEGKGVEALEYEAYPPMAEKELEEIAEEARERWGLLRVAIIHRVGRLPPGEA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6460436  177 SIVIGVASPHRRPALEACDFLIEHLKIELPIWKHEADGRGEHWV 220
Cdd:cd00756  81 IVLVAVSSPHRKEAFEACEFLIDRLKHRAPIWKKEIFEGGEEWV 124

MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of molybdopterin. Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Converting factor contains the MoaE and MoaD proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436     92 VTADPLSLSEADAFLVKPEYGAQAYFMGTVRSPNQGQVVEYIDYEAFAPMAEKVMREAAALARERHGELRVWIEHRTGRL 171
Cdd:pfam02391   1 ITEEPLDVAEIAALVSDPEAGAVVTFVGTVRDHFDGKKVTALEYEAYPPMAEKELAEIAEEARERWPLLDVAIVHRVGRL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 6460436    172 TPAVASIVIGVASPHRRPALEACDFLIEHLK 202
Cdd:pfam02391  81 PVGEAIVLVAVSSPHRAEAFEACEYLIDELK 111

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436      3 VRAVFFARLRREVGLEELTLDVPDG-ADVRAVAEHLEQERG---VSLRGCMVAVNETYASPEHLLREGDEVAFLPPVAGG 78
Cdd:TIGR01682   1 IKVLYFARLREQAGTDEETLELPDEsTTVGELKEHLAKEGPelaASRGQVMVAVNEEYVTDDALLNEGDEVAFIPPVSGG 80

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6460436    3 VRAVFFARLRREVGLEELTLDVPDGADVRAVAEHLEQ---ERGVSLRGCMVAVNETYASPEHLLREGDEVAFLPPVAGG 78
Cdd:cd00754   1 VKVLYFARARELAGKSEEELELPAGTTVEELLEELAAkypALAAILKSVRVAVNQEYVDDDTELKDGDEVAFIPPVSGG 79

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6460436      7 FFARLRREVGLEELtldVPDGADVRAVAEHLEQERGVSLRGCMVAVNETYASPEHL---LREGDEVAFLPPVAGG 78
Cdd:pfam02597   3 LNAELRELAGKDEE---LAEGATVAELLEALGLRYPELRERVAVAVNGEIVPRLWLdtpLKDGDEVAIIPPVGGG 74

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoaE; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436   112 GAQAYFMGTVRSPNQG--QVVEYIDYEAFAPMAEKVMREAAALARERHGELRVWIEHRTGRLtPAVASIV-IGVASPHRR 188
Cdd:PRK14493 160 GAIATFTGRVRAKEDAddEPTEYLEFEKYDGVADERMAAIREELKQRDGVFEVLLHHRTGVI-EAGEDIVfVVVLAGHRQ 238

                         90       100       110
                 ....*....|....*....|....*....|..
gi 6460436   189 PALEACDFLIEHLKIELPIWKHEADGRGEHWV 220
Cdd:PRK14493 239 EAFRAVSDGIDRLKDEVPIFKKEVTVDEEFWV 270

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436    1 MQVRavFFARLRREVGlEELTLDVPDGADVRAVAEHLEQ----------ERGVSLRGCMVAVNETYASPEH---LLREGD 67
Cdd:cd17040   1 VKVR--LFGALREAGA-GEEEIEVEGGTTVRDLLDALSErypglfealdEDGELRPFILVFVNGRDVRLDDgltPLKDGD 77

                        90
                ....*....|.
gi 6460436   68 EVAFLPPVAGG 78
Cdd:cd17040  78 EVDILPPVAGG 88

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6460436      3 VRAVFFARLRREVGLEELTLDVpDGADVRAVAEHLEQERGVSLRGCM-----------VAVNETYAS--PEHLLREGDEV 69
Cdd:TIGR01687   1 VRVKYFATLRDITGKKSEEIEI-EGKTVGDLLNELMARYPKEFSELFkeglglvpnviILVNGRNVDwgLGTELKDGDVV 79

                  ....*....
gi 6460436     70 AFLPPVAGG 78
Cdd:TIGR01687  80 AIFPPVSGG 88