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
//