ID A0A177DJI4_ALTAL Unreviewed; 892 AA.
AC A0A177DJI4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Gephyrin {ECO:0000313|EMBL:OAG20104.1};
GN ORFNames=CC77DRAFT_963373 {ECO:0000313|EMBL:OAG20104.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG20104.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG20104.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG20104.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441479; OAG20104.1; -; Genomic_DNA.
DR RefSeq; XP_018385525.1; XM_018535664.1.
DR AlphaFoldDB; A0A177DJI4; -.
DR STRING; 5599.A0A177DJI4; -.
DR GeneID; 29121258; -.
DR KEGG; aalt:CC77DRAFT_963373; -.
DR VEuPathDB; FungiDB:CC77DRAFT_963373; -.
DR OMA; ESPYPMI; -.
DR OrthoDB; 275356at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000077248; 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; 2.
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:UP000077248};
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..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..378
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 649..799
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 400..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 94476 MW; 2BB74D6F189B3C64 CRC64;
MSLTYGTGGA TAALGVVGLY MLFNNEGEAF NVGAFLESIS PYTFASVGIA LCIGLSVVGS
AWGIWTTGVS IVGGGVKAPR IRTKNLISII FCEVVAIYGV IMAIIFSSKM NQLSDPELLY
SGSNYFTGYA LFWAGITVGM CNLICGVCVG INGSSAALAD AADPAMFVKI LTIEIFAAIL
GLFGLIIGLL MQSNAKDFHE YRQWHVRTTP PVLNLTSIKM ATTNPKLKSA VLVVSETASQ
DPSTDKCIPV LKKVFGDLGN DQWHVSETEI VPDNALAIQK TIRTWTDGPD PINLIVTSGG
TGFATKDVTP EAVTPLIDRH APGLIHGMLT TSYAVTPFAL MARPVAGLRK KTLILTLPGS
PKGAKENLEA VLKLLPHACI QAAGAESRPL HAGGVEKLEK DAGVSSAGTT TGTGCGHHHH
GHSHGHGGHA GPRAHTNPEE RPQSNDPSAG PTRRYRSSPY PMLAVDNALK LIAEQTPAPV
VERVPVDMRL SGSVLAEDVK ATESVPAFRA SIVDGYAVKI PSTGKFEKGV YPVTIVSHAQ
AGEVKELREG EIARITTGAP LPPGADSVVM VEDTVLKSLT DDGKEEKEIE ILTDEIKPNE
NVREVGSDVK EGETILKKGE GVTVVGGEFG LLASVGTKEV SVYKKPVVGV LSTGDEIIPH
NREGSLRLGE VRDTNRPTLI TAARSHRFEV IDLGIVSDKP GSLEQTLRDA MRKCDVIITS
GGVSMGELDL LKPTIERSLG GTIHFGRVNM KPGKPTTFAT VPVKDNSGNP VTKSVFSLPG
NPASAVVCFH LFVLPALHQQ AGIKPLGLPR IKVILDEDVK MDKGRPEYHR ALVVTKEDGL
LYASSTGGQR SSRIGSFRGA NALLAMPQGE GSLKKGEKVE ALLMGKLGEV ER
//
