Molybdopterin synthase sulfur carrier subunit MoaD [Coenzyme transport and metabolism]; Molybdopterin synthase sulfur carrier subunit MoaD is part of the Pathway/BioSystem: Molybdopterin biosynthesis

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142661215  3 INLELMGPLVDFLpnsDRGKAVFNLTNNSTIADMLDELK----------IKQKVVVAVNGdEEKGLDHVLSDGDEVLVFS 72
Cdd:COG1977   2 VTVRYFAALREAA---GKSEEEVELPEGATVGDLLEALAarypglaerlLRRRVRVAVNG-EDVRLDTPLKDGDEVALFP 77

                ....*
gi 142661215 73 LVSGG 77
Cdd:COG1977  78 PVAGG 82

thiamine biosynthesis protein ThiS; This model represents ThiS, a small, ubiquitin-like thiamine biosynthesis protein related to MoaD, a molybdenum cofactor biosynthesis protein. Both proteins are involved in sulfur transfer. ThiS has a conserved Gly-Gly C-terminus that is modified, in reactions requiring ThiI, ThiF, IscS, and a sulfur atom from Cys, into the thiocarboxylate that provides the sulfur for thiazole biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 142661215  30 NSTIADMLDELKIKQK-VVVAVNGD---EEKGLDHVLSDGDEVLVFSLVSGG 77
Cdd:TIGR01683 13 GTTLAALLESLGLDPRrVAVAVNGEivpRSEWDDTILKEGDRIEIVTFVGGG 64

Molybdopterin synthase sulfur carrier subunit MoaD [Coenzyme transport and metabolism]; Molybdopterin synthase sulfur carrier subunit MoaD is part of the Pathway/BioSystem: Molybdopterin biosynthesis

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142661215  3 INLELMGPLVDFLpnsDRGKAVFNLTNNSTIADMLDELK----------IKQKVVVAVNGdEEKGLDHVLSDGDEVLVFS 72
Cdd:COG1977   2 VTVRYFAALREAA---GKSEEEVELPEGATVGDLLEALAarypglaerlLRRRVRVAVNG-EDVRLDTPLKDGDEVALFP 77

                ....*
gi 142661215 73 LVSGG 77
Cdd:COG1977  78 PVAGG 82

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 142661215 25 FNLTNNSTIADMLDELKI-KQKVVVAVNGD---EEKGLDHVLSDGDEVLVFSLVSGG 77
Cdd:cd00565   8 REVDEGLTLAELLEELGFtPKGVAVELNGEivpRSEWAETILKDGDRIEIVTFVGGG 64

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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142661215  3 INLELMGPLVDFlpnsDRGKAVFNLTNNSTIADMLDEL---------------KIKQKVVVAVNGDEEKGLDH--VLSDG 65
Cdd:cd17040   1 VKVRLFGALREA----GAGEEEIEVEGGTTVRDLLDALserypglfealdedgELRPFILVFVNGRDVRLDDGltPLKDG 76

                        90
                ....*....|..
gi 142661215 66 DEVLVFSLVSGG 77
Cdd:cd17040  77 DEVDILPPVAGG 88

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.

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                ....*....|....*....|....*....|....*....|....*....|....*
gi 142661215 31 STIADMLDELKIK--------QKVVVAVNgDEEKGLDHVLSDGDEVLVFSLVSGG 77
Cdd:cd00754  26 TTVEELLEELAAKypalaailKSVRVAVN-QEYVDDDTELKDGDEVAFIPPVSGG 79

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 142661215 29 NNSTIADMLDELKIKQKVVVAVNGDEEKGLDHVLSDGDEVLVFSLVSGG 77
Cdd:cd17506  19 GGATVRDLLRTLSLPPEEVIVVVNGEVVPEDDPLKDGDIIRLIPVVSGG 67