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Database: UniProt
Entry: B2WGC2_PYRTR
LinkDB: B2WGC2_PYRTR
Original site: B2WGC2_PYRTR 
ID   B2WGC2_PYRTR            Unreviewed;       878 AA.
AC   B2WGC2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   SubName: Full=Gephyrin {ECO:0000313|EMBL:EDU42029.1};
GN   ORFNames=PTRG_08978 {ECO:0000313|EMBL:EDU42029.1};
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU42029.1, ECO:0000313|Proteomes:UP000001471};
RN   [1] {ECO:0000313|Proteomes:UP000001471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000256|ARBA:ARBA00007296}.
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; DS231624; EDU42029.1; -; Genomic_DNA.
DR   RefSeq; XP_001939310.1; XM_001939275.1.
DR   AlphaFoldDB; B2WGC2; -.
DR   STRING; 426418.B2WGC2; -.
DR   EnsemblFungi; EDU42029; EDU42029; PTRG_08978.
DR   GeneID; 6347264; -.
DR   eggNOG; KOG0233; Eukaryota.
DR   eggNOG; KOG2371; Eukaryota.
DR   HOGENOM; CLU_010186_2_2_1; -.
DR   InParanoid; B2WGC2; -.
DR   OMA; RHRESPY; -.
DR   OrthoDB; 275356at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProt.
DR   GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd18177; ATP-synt_Vo_c_ATP6F_rpt1; 1.
DR   CDD; cd18178; ATP-synt_Vo_c_ATP6F_rpt2; 1.
DR   CDD; cd00887; MoeA; 1.
DR   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 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; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR000245; ATPase_proteolipid_csu.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
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; 1.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00137; ATP-synt_C; 2.
DR   Pfam; PF00994; MoCF_biosynth; 2.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   PRINTS; PR00122; VACATPASE.
DR   SMART; SM00852; MoCF_biosynth; 2.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        5..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        43..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          232..365
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          635..785
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          388..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   878 AA;  93103 MW;  F569D80F1426C8EC CRC64;
     MSLSYGTGGA TAALAVVGLY MLFNDEGEAF NVGAFLETVS PYTFASIGIA LCIGLSVVGS
     AWGIWTTGVS ILGGGVKAPR IRTKNLISII FCEVVAIYGV IMAIIFSSKM NQLGDAELLY
     SGSNYFTGYA LFWAGITVGM CNLICGVCVG INGSSAALAD AADPALFVKI LTIEIFAAIL
     GLFGLIIGLL MQSNAKDFES YTWWDVSFTP PRSASFSQTL NMSTISSKLK AAILIVSETA
     AQDPSTDKCI PILKHVFGSL GNDQWEVSET EIVPDNSLTI QKTIRNWSDS ADPMNLIVTS
     GGTGFATKDV TPEAVTPLID RHAPVALMAR PVAGLRKQTL ILTLPGSPKG AKENLEAVLK
     LLPHACIQAA GAESRPLHVG GVKKLEKDAG VTPSGASVGT TCGHNHGHSH GHGSHTAPRA
     HTKPEERPQS NDPSAGPTQR YRSSPYPMLA VEDALNVIKE QTPAPIVEKV PVDMRIGGSV
     LAEDVKATES VPAFRASIVD GYAVKIPSSG KFQKGVYPVS IISHAQAGEV AELKEGEIAR
     ITTGAPLPPG ADAVIMVEDT VLKSLTEDGH EEKEIEILTD EIKPNENVRE VGSDVKEGET
     ILKKGEGVTV VGGEFGLLAS VGTREVSVYR RPLIGVLSTG DEIIQHNREG PLHLGEVRDT
     NRPTIITAAR SHRFEVIDLG IVSDKPGTLE QTLRDAFRKC DVIITSGGVS MGELDLLKPT
     IERSLGGTIH FGRVNMKPGK PTTFATVPVK DNAGNHVTKS IFSLPGNPAS AVVCFHLFVL
     PALHQQAGIK PVGLPRVTVV LEEDIRMDKG RPEYHRALVV TKEDGLLYAS STGGQRSSRI
     GSFRGANALL CMPQGDGSIK KGEKVIALLM GKLGELER
//
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