ID D6RM23_COPC7 Unreviewed; 87 AA.
AC D6RM23;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Molybdopterin synthase sulfur carrier subunit {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 Short=MOCS2A {ECO:0000256|HAMAP-Rule:MF_03051};
DE AltName: Full=Sulfur carrier protein MOCS2A {ECO:0000256|HAMAP-Rule:MF_03051};
GN ORFNames=CC1G_14412 {ECO:0000313|EMBL:EFI27921.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EFI27921.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EFI27921.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFI27921.1}.
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DR EMBL; AACS02000004; EFI27921.1; -; Genomic_DNA.
DR RefSeq; XP_002911415.1; XM_002911369.1.
DR AlphaFoldDB; D6RM23; -.
DR STRING; 240176.D6RM23; -.
DR GeneID; 9378339; -.
DR KEGG; cci:CC1G_14412; -.
DR VEuPathDB; FungiDB:CC1G_14412; -.
DR eggNOG; ENOG502SSQY; Eukaryota.
DR HOGENOM; CLU_114601_4_3_1; -.
DR InParanoid; D6RM23; -.
DR OMA; CTTECIT; -.
DR OrthoDB; 1439019at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001861; 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:UP000001861}.
FT MOD_RES 87
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03051"
FT MOD_RES 87
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03051"
SQ SEQUENCE 87 AA; 9088 MW; 8B0F59321F83B790 CRC64;
MTSITVLYFA AASTETGLTV EKVPIPTQGL ALSSLPGLLV SRHPGTNLEQ VFQTSQWSVD
AEMVEDPTTV TLRGGEEVAV ICPVSGG
//
