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Database: UniProt
Entry: A0A139AFI5_GONPR
LinkDB: A0A139AFI5_GONPR
Original site: A0A139AFI5_GONPR 
ID   A0A139AFI5_GONPR        Unreviewed;       836 AA.
AC   A0A139AFI5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   18-JAN-2017, entry version 5.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=M427DRAFT_112217 {ECO:0000313|EMBL:KXS15185.1};
OS   Gonapodya prolifera JEL478.
OC   Eukaryota; Fungi; Chytridiomycota; Monoblepharidomycetes;
OC   Monoblepharidales; Gonapodyaceae; Gonapodya.
OX   NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS15185.1, ECO:0000313|Proteomes:UP000070544};
RN   [1] {ECO:0000313|EMBL:KXS15185.1, ECO:0000313|Proteomes:UP000070544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL478 {ECO:0000313|EMBL:KXS15185.1,
RC   ECO:0000313|Proteomes:UP000070544};
RX   PubMed=25977457; DOI=10.1093/gbe/evv090;
RA   Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A.,
RA   LaButti K.M., Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A.,
RA   Grigoriev I.V., Spatafora J.W., Berbee M.L.;
RT   "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting
RT   Cell Walls of Algal Ancestors of Land Plants.";
RL   Genome Biol. Evol. 7:1590-1601(2015).
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
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DR   EMBL; KQ965764; KXS15185.1; -; Genomic_DNA.
DR   EnsemblFungi; KXS15185; KXS15185; M427DRAFT_112217.
DR   Proteomes; UP000070544; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070544};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070544};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    412    434       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    455    474       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    534    554       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    566    586       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    627    646       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    738    763       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    769    790       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       50     77       {ECO:0000256|SAM:Coils}.
FT   COILED       89    116       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   836 AA;  94300 MW;  02283019FD103157 CRC64;
     MSLFRSALMS LTRIYVPSEI AQTTYAELGE VGLIQFRDLN PEVNAFQRAF VSEIRRLDEM
     ERKIRFLESQ LEKAGVVVQP VTESTPYARM RTQQLIDDLE SKLNEHEGRV VQMNQSQETL
     NKRYLELTEM RHVLRETGTF FDEAQSRQED LSGGAAQPDA PLLASEEGEV GGDRGSANLG
     FVAGVIPRNK MIVFERVLWR VLRGNLYMNY AEIEEPIRDP VTDEVVKKNV FIIFAHGKEL
     LGKIRKISES LGATLYPVDE HPEKRREDAM EVIARIEDLN QVLANTTSTR KAELKKVAES
     VETWNMIVKK EKAIYYAMNM ADYDPGKKAL VAEGWVPTQS LPAVQGALRT VSDRTGATVP
     PILDVVPTKK EPPTFHPVNK FTIGFQSIID AYGVARYREV NPGLYTIVTF PFLFAMMFGD
     VGHGFLMALA GIFLTVKEKS LYKYRTDEMF GMVYGGRYII LLMGLYSMYT GLIYNDVFSL
     GFEFLGGSGW HFHTTNGDKE IGLQTKVYAF GVDPAWVHAD NKLLFVNSYK MKQAVLIGVI
     HMSFGIILQV WNHLQFKRWV SIFFEFVPQF IFMEAIFGYL CILIVYKWST DWYSIGKPPP
     GLLNVLIYMF LSPGAIKNDT KVYDGQATIQ VALVAIALIC VPWMLLPKPL ILRAQHNKKM
     KAKALARVGE AGHDGHDDHN GVNGHHDDDD DDDHFEFSEI MIHQVIHTIE FCLGCISNTA
     SYLRLWALSL AHAQLSEVLW KMVMTTIFGM AANGAGLGGI LVWAAFAAWF TLTIGILLIM
     EGLSAFLHAL RLHWVEFDSK FYEGSGRIFE PFSFYRLDEG EDIVVPFDST GLGGGH
//
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