ID A0A182FR38_ANOAL Unreviewed; 90 AA.
AC A0A182FR38;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 Name=Mocs2 {ECO:0000256|HAMAP-Rule:MF_03051};
OS Anopheles albimanus (New world malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB009013-PA, ECO:0000313|Proteomes:UP000069272};
RN [1] {ECO:0000313|EnsemblMetazoa:AALB009013-PA}
RP IDENTIFICATION.
RC STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB009013-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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: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 MOCS3, then
CC thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
CC {ECO:0000256|HAMAP-Rule:MF_03051}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the large subunit (MOCS2B). {ECO:0000256|HAMAP-
CC Rule:MF_03051}.
CC -!- SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03051}.
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DR AlphaFoldDB; A0A182FR38; -.
DR STRING; 7167.A0A182FR38; -.
DR EnsemblMetazoa; AALB009013-RA; AALB009013-PA; AALB009013.
DR VEuPathDB; VectorBase:AALB009013; -.
DR VEuPathDB; VectorBase:AALB20_033133; -.
DR OrthoDB; 1204809at2759; -.
DR Proteomes; UP000069272; Chromosome 2R.
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}.
FT MOD_RES 90
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03051"
FT MOD_RES 90
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03051"
SQ SEQUENCE 90 AA; 10111 MW; 083CA84129071B1B CRC64;
MSSSSVRVRL LFFAKSRELA GKSNVEDFLV PRAEIRCSEL LDLICNQFNL SIIRHNLILA
HNEQYCDDLS ETIRIHNGDE LAVIPPISGG
//
