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MOC2A_DROME
ID   MOC2A_DROME             Reviewed;          90 AA.
AC   P0C919; E1JIW5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Molybdopterin synthase sulfur carrier subunit {ECO:0000255|HAMAP-Rule:MF_03051};
DE   AltName: Full=Molybdenum cofactor synthesis protein 2 small subunit {ECO:0000255|HAMAP-Rule:MF_03051};
DE   AltName: Full=Molybdenum cofactor synthesis protein 2A {ECO:0000255|HAMAP-Rule:MF_03051};
DE            Short=MOCS2A {ECO:0000255|HAMAP-Rule:MF_03051};
DE   AltName: Full=Sulfur carrier protein MOCS2A {ECO:0000255|HAMAP-Rule:MF_03051};
GN   Name=Mocs2A {ECO:0000312|FlyBase:FBgn0260229};
GN   Synonyms=Mocs2 {ECO:0000255|HAMAP-Rule:MF_03051};
GN   ORFNames=CG42503 {ECO:0000312|FlyBase:FBgn0260229};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=18237443; DOI=10.1186/1471-2164-9-61;
RA   Hayden C.A., Bosco G.;
RT   "Comparative genomic analysis of novel conserved peptide upstream open
RT   reading frames in Drosophila melanogaster and other dipteran species.";
RL   BMC Genomics 9:61-61(2008).
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 MOCS3. After interaction
CC       with Mocs2B, the sulfur is then transferred to precursor Z to form
CC       molybdopterin. {ECO:0000255|HAMAP-Rule:MF_03051}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03051}.
CC   -!- SUBUNIT: Heterotetramer; composed of 2 small (Mocs2A) and 2 large
CC       (Mocs2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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 MOCS3, then
CC       thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
CC       {ECO:0000255|HAMAP-Rule:MF_03051}.
CC   -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC       also produces the large subunit (Mocs2B).
CC   -!- SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03051}.
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DR   EMBL; AE014297; ACZ95014.1; -; Genomic_DNA.
DR   RefSeq; NP_001163720.1; NM_001170249.1.
DR   AlphaFoldDB; P0C919; -.
DR   SMR; P0C919; -.
DR   BioGRID; 1073035; 1.
DR   STRING; 7227.FBpp0289862; -.
DR   PaxDb; P0C919; -.
DR   EnsemblMetazoa; FBtr0300637; FBpp0289862; FBgn0260229.
DR   GeneID; 8674021; -.
DR   KEGG; dme:Dmel_CG42503; -.
DR   CTD; 8674021; -.
DR   FlyBase; FBgn0260229; Mocs2A.
DR   VEuPathDB; VectorBase:FBgn0260229; -.
DR   eggNOG; KOG3474; Eukaryota.
DR   HOGENOM; CLU_114601_4_3_1; -.
DR   OMA; HVLFFAK; -.
DR   PhylomeDB; P0C919; -.
DR   UniPathway; UPA00344; -.
DR   BioGRID-ORCS; 8674021; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 8674021; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0260229; Expressed in midgut and 12 other tissues.
DR   Genevisible; P0C919; DM.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0019008; C:molybdopterin synthase complex; ISS:FlyBase.
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; ISS:UniProtKB.
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; PTHR33359; 1.
DR   Pfam; PF02597; ThiS; 1.
DR   SUPFAM; SSF54285; SSF54285; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..90
FT                   /note="Molybdopterin synthase sulfur carrier subunit"
FT                   /id="PRO_0000369312"
FT   MOD_RES         90
FT                   /note="1-thioglycine; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03051"
FT   MOD_RES         90
FT                   /note="Glycyl adenylate; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03051"
SQ   SEQUENCE   90 AA;  9858 MW;  1D75801A952AB2E6 CRC64;
     MNADGPVVNV HVLFFAKSRE LANTPRSTVE VPTEITATEL LDHLVSKFGL TSIRDNLILA
     HNESYIDNLS DRILFKEGDE LAIIPPLSGG
 
 
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