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Database: UniProt
Entry: B8MRE0_TALSN
LinkDB: B8MRE0_TALSN
Original site: B8MRE0_TALSN 
ID   B8MRE0_TALSN            Unreviewed;       718 AA.
AC   B8MRE0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   22-FEB-2023, entry version 63.
DE   SubName: Full=Molybdenum cofactor biosynthesis protein Gephyrin, putative {ECO:0000313|EMBL:EED13035.1};
GN   ORFNames=TSTA_055390 {ECO:0000313|EMBL:EED13035.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED13035.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum
CC       cofactor. In the first step, molybdopterin is adenylated. Subsequently,
CC       molybdate is inserted into adenylated molybdopterin and AMP is
CC       released. {ECO:0000256|RuleBase:RU365090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC         diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC         ChEBI:CHEBI:62727; Evidence={ECO:0000256|RuleBase:RU365090};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC         molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC         ChEBI:CHEBI:71302, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family.
CC       {ECO:0000256|RuleBase:RU365090}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC       {ECO:0000256|ARBA:ARBA00008339}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC       {ECO:0000256|ARBA:ARBA00007589}.
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DR   EMBL; EQ962659; EED13035.1; -; Genomic_DNA.
DR   RefSeq; XP_002487146.1; XM_002487101.1.
DR   AlphaFoldDB; B8MRE0; -.
DR   STRING; 441959.B8MRE0; -.
DR   GeneID; 8102232; -.
DR   VEuPathDB; FungiDB:TSTA_055390; -.
DR   eggNOG; KOG2371; Eukaryota.
DR   HOGENOM; CLU_010186_2_2_1; -.
DR   InParanoid; B8MRE0; -.
DR   OMA; RHRESPY; -.
DR   OrthoDB; 275356at2759; -.
DR   PhylomeDB; B8MRE0; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00887; MoeA; 1.
DR   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
DR   Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   InterPro; IPR038987; MoeA-like.
DR   InterPro; IPR005111; MoeA_C_domain_IV.
DR   InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   InterPro; IPR036135; MoeA_linker/N_sf.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00994; MoCF_biosynth; 2.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 2.
DR   SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR   SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 2.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU365090};
KW   Metal-binding {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          9..159
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          440..610
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          189..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..217
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   718 AA;  75764 MW;  941578C7C9904CA9 CRC64;
     MSTDILRPAI LIISDTASIN PQSDKTGPIL TEIFTSPQHS KTWSSPIVKI VPDDFDRIQN
     AVKEWADNQE DGFNLILTSG GTGFAVRDGT PEAVSPLIHR HAPGLIHGMI AASLKVTPFA
     MMARPVAGTR NASLVITLPG SPKGAKENLE AVINLLPHAC IQAAGADSRS IHAKGIKKLE
     QDAGLLSTGT ESTTAKDHSH NNHHHHHHHH HHDHGHAVPK AHTSPEDRPQ SNDPNAGPTR
     RYRSSPYPML SVDEALKIIA KETPEPTIIE APVTTDLVGS VLAEDVYASE AVPAYRASIV
     DGYAIIVPDD STPGPRTKGV FPVASVSHAQ ASSMPPPLEP GNIARITTGA PLPPNANAVV
     MVEDTILAST TPDGKEEAAV EILTDDVKIG ENVRDPGSDV TKGSKILSRG DLISAIGGEI
     GLLASTGTKT VKIFKKPTVG VMSTGDELVP HDDPSALHGG QIRDSNRPSL ISCLRAWGFE
     TVDLGIARDT PAGELENALR GALRGISVSQ PAVDVIITTG GVSMGELDLL KPTIERTLGG
     TIHFGRVSMK PGKPTTFASV PYKPSSSPIA SSEQQQQQQE RERRLIFSLP GNPASALVTL
     NLFVLPSLHK LMGLSTRNTP TTPPGSGLGL PLITATLTHS IKLDPKRTEY HRAIVTASRR
     DGRLYATSTG TAGVGQRSSR VGSLAKANAL LVLYPGLGVV GDGQVVEALL MGPLMAED
//
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