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Database: UniProt
Entry: A0A168K3Z4_CORDF
LinkDB: A0A168K3Z4_CORDF
Original site: A0A168K3Z4_CORDF 
ID   A0A168K3Z4_CORDF        Unreviewed;       686 AA.
AC   A0A168K3Z4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   SubName: Full=Gephyrin {ECO:0000313|EMBL:OAA81201.1};
GN   ORFNames=LEL_00746 {ECO:0000313|EMBL:OAA81201.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA81201.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA81201.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA81201.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:OAA81201.1}.
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DR   EMBL; AZHF01000001; OAA81201.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168K3Z4; -.
DR   STRING; 1081108.A0A168K3Z4; -.
DR   OrthoDB; 275356at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000076881; 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   NCBIfam; TIGR00177; molyb_syn; 2.
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:UP000076881};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..686
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007898343"
FT   DOMAIN          8..156
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          446..596
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          187..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..232
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   686 AA;  72547 MW;  C0681E0F5A3C70D3 CRC64;
     MDSSLTAAIL IVSTTAALDP STDASAAVLR EVLDIDGAGK WTVADEKIVS DNVIDIQKQI
     MQWTDGPDAP NFIITTGGTG FAVSDATPEA VASLLHKQAP GLVHAMLSTS LAVTPFAMMS
     RPAAGVRNRT VIVTLPGSPK GAKENLQAII KTLPHACLQS AGANSRQLHA GGTKKLEKEA
     GIIEHEHSHT HDHSHAIEHD HGHDHSHSHS HSHSHSHSHS HGHGHGHGNL VRHTKPSSKT
     LSNDPTLGPT RRHRESPYPM VSVDDALAMI DEFTPQPEIV HSKVDQDIIG SVLAEEVKAH
     EHVPAFRASI VDGYAVVAPK DGKLKGVFPV VGVSHAAPGE IGALKEGQTA RITTGAPLPP
     GATSVIMVED TVLKSMTDDG KEEKEVEIQA EGVKEGENVR EVGSDVKQGT TILSKGEQIS
     GVGGEIGLLA SVGVAEANVY KRPVIGILST GDEIIEYNRP GALKLGEVRD TNRITLISAA
     KEWGYDVVDL GIAKDKSNSL EETLRSGLRQ ADLLITTGGV SMGELDLLKP TIERSLGGTI
     HFGRVAMKPG KPTTFATVPV KDNAGKRVHK VIFSLPGNPA SALVTFHLFV LPSLHKQSGI
     YPVGLPKVPV VLGHDFPMDP RPEYHRAVLT VGEDGQLTAN STGGQRSSRV GSLRSANALL
     CMPSGKGKME KGSKVHALLL NPVRSS
//
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