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Database: UniProt
Entry: C9SIT3_VERA1
LinkDB: C9SIT3_VERA1
Original site: C9SIT3_VERA1 
ID   C9SIT3_VERA1            Unreviewed;        95 AA.
AC   C9SIT3;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Molybdopterin synthase sulfur carrier subunit {ECO:0000256|HAMAP-Rule:MF_03051};
DE   AltName: Full=Common component for nitrate reductase and xanthine dehydrogenase protein G {ECO:0000256|HAMAP-Rule:MF_03051};
DE   AltName: Full=Molybdenum cofactor synthesis protein 2 small subunit {ECO:0000256|HAMAP-Rule:MF_03051};
DE   AltName: Full=Molybdenum cofactor synthesis protein 2A {ECO:0000256|HAMAP-Rule:MF_03051};
DE   AltName: Full=Sulfur carrier protein MOCS2A {ECO:0000256|HAMAP-Rule:MF_03051};
DE            Short=MOCS2A {ECO:0000256|HAMAP-Rule:MF_03051};
GN   Name=cnxG {ECO:0000256|HAMAP-Rule:MF_03051};
GN   ORFNames=VDBG_04965 {ECO:0000313|EMBL:EEY18856.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
CC   -!- FUNCTION: Acts as a sulfur carrier required for molybdopterin
CC       biosynthesis. Component of the molybdopterin synthase complex that
CC       catalyzes the conversion of precursor Z into molybdopterin by mediating
CC       the incorporation of 2 sulfur atoms into precursor Z to generate a
CC       dithiolene group. In the complex, serves as sulfur donor by being
CC       thiocarboxylated (-COSH) at its C-terminus by UBA4. After interaction
CC       with MOCS2B, the sulfur is then transferred to precursor Z to form
CC       molybdopterin. {ECO:0000256|HAMAP-Rule:MF_03051}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|HAMAP-Rule:MF_03051}.
CC   -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC       (MOCS2B) subunits. {ECO:0000256|HAMAP-Rule:MF_03051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03051}.
CC   -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC       adenylated (-COAMP) via the hesA/moeB/thiF part of UBA4, then
CC       thiocarboxylated (-COSH) via the rhodanese domain of UBA4.
CC       {ECO:0000256|HAMAP-Rule:MF_03051}.
CC   -!- SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03051}.
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DR   EMBL; DS985218; EEY18856.1; -; Genomic_DNA.
DR   RefSeq; XP_003005359.1; XM_003005313.1.
DR   AlphaFoldDB; C9SIT3; -.
DR   STRING; 526221.C9SIT3; -.
DR   GeneID; 9536776; -.
DR   KEGG; val:VDBG_04965; -.
DR   eggNOG; ENOG502SD3I; Eukaryota.
DR   HOGENOM; CLU_114601_6_1_1; -.
DR   OMA; IECNDEV; -.
DR   OrthoDB; 6652at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0019008; C:molybdopterin synthase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00754; Ubl_MoaD; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   HAMAP; MF_03051; MOCS2A; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR044672; MOCS2A.
DR   InterPro; IPR028887; MOCS2A_euk.
DR   InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR   InterPro; IPR003749; ThiS/MoaD-like.
DR   PANTHER; PTHR33359; MOLYBDOPTERIN SYNTHASE SULFUR CARRIER SUBUNIT; 1.
DR   PANTHER; PTHR33359:SF1; MOLYBDOPTERIN SYNTHASE SULFUR CARRIER SUBUNIT; 1.
DR   Pfam; PF02597; ThiS; 1.
DR   SUPFAM; SSF54285; MoaD/ThiS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03051};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|HAMAP-Rule:MF_03051};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03051};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_03051}; Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT   MOD_RES         95
FT                   /note="1-thioglycine; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03051"
FT   MOD_RES         95
FT                   /note="Glycyl adenylate; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03051"
SQ   SEQUENCE   95 AA;  10156 MW;  4A009E5D1F03235C CRC64;
     MNSTGRPPTG HFSILYFAGA SSYTAKDQEA LPAPLPLGRL FDTLEERYSG IKSKILDSCL
     VTINLDYVDL PKPGEDGAMI KEGDEVAIIP PVSSG
//
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