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Database: UniProt
Entry: G4TRL2_SERID
LinkDB: G4TRL2_SERID
Original site: G4TRL2_SERID 
ID   G4TRL2_SERID            Unreviewed;       621 AA.
AC   G4TRL2;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   22-FEB-2023, entry version 42.
DE   SubName: Full=Related to Gephyrin {ECO:0000313|EMBL:CCA73955.1};
GN   ORFNames=PIIN_07909 {ECO:0000313|EMBL:CCA73955.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA73955.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA73955.1, ECO:0000313|Proteomes:UP000007148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA73955.1,
RC   ECO:0000313|Proteomes:UP000007148};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA   Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA   Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT   the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(2011).
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}.
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:CCA73955.1}.
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DR   EMBL; CAFZ01000266; CCA73955.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4TRL2; -.
DR   STRING; 1109443.G4TRL2; -.
DR   eggNOG; KOG2371; Eukaryota.
DR   HOGENOM; CLU_010186_2_2_1; -.
DR   InParanoid; G4TRL2; -.
DR   OMA; RHRESPY; -.
DR   OrthoDB; 275356at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000007148; 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; PS01078; MOCF_BIOSYNTHESIS_1; 1.
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:UP000007148};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          1..119
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          382..529
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   621 AA;  66207 MW;  9CC1B504192E4132 CRC64;
     MKISETRLTV VESLIVPDES GVITSTIKSL VELKSIDLII TTGGTGFGIR DVTPEAIGPL
     LQKQAPGLVH LLLSSSPKAV LSRPVAGICD QTLIITLPGS PKAVDECLEA LLSGGILDHA
     LALSRGADSR HLHENSAALT GAGVQTRHVH SHCGHHAPKP RTGGKMEMIP SSTFLGRLDI
     PSYLIVPLRA RNSPFPLISL QEACQLIIKN IHHLPPITLP VNPSLRGYIL AEPIYAQNDL
     PRYPSSNVDG YAIQASKGPG VYKVVHPGTH PRSLPVPEDS IYRINTGAPL PLGTDAVIMV
     EDTELVSPAP NGSGEVPSEE LEVRTLAQVE VGENIRKPGS DLRKGDLIFE KGAAIGNTGG
     DLGALAFIGR REVVVYRKPR VAIMSTGDEL ADLADESDQQ GEWRHWDTNR PILRGALEAQ
     GYDVVDLGIV RDSLGAHVQA LSSGLEQADI FISTGGSSMG TTDHIRPMLQ EMNATVLFGR
     VKVKPGKPTI FAQVPCKSGE GTKPFFGLPG NPASALVTFN LFVRPALRLL GGFSIKDCQL
     QPVKVKLADD MPLDPRPEFH RVLVKANNEG QLEAHSTGGQ RSSRASSLNS SNALVALPAL
     VEEGPKQLLK GDMADALLID L
//
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