ID A0A024UWN8_9STRA Unreviewed; 184 AA.
AC A0A024UWN8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=V-type ATPase, C subunit {ECO:0000313|EMBL:ETW10375.1};
GN ORFNames=H310_00693 {ECO:0000313|EMBL:ETW10375.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW10375.1};
RN [1] {ECO:0000313|EMBL:ETW10375.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW10375.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU363060}.
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DR EMBL; KI913952; ETW10375.1; -; Genomic_DNA.
DR RefSeq; XP_008861786.1; XM_008863564.1.
DR AlphaFoldDB; A0A024UWN8; -.
DR STRING; 157072.A0A024UWN8; -.
DR EnsemblFungi; H310_00693-t26_1; H310_00693-t26_1-p1; H310_00693.
DR EnsemblProtists; ETW10375; ETW10375; H310_00693.
DR GeneID; 20077743; -.
DR VEuPathDB; FungiDB:H310_00693; -.
DR eggNOG; KOG0233; Eukaryota.
DR OrthoDB; 1112183at2759; -.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd18177; ATP-synt_Vo_c_ATP6F_rpt1; 1.
DR CDD; cd18178; ATP-synt_Vo_c_ATP6F_rpt2; 1.
DR Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR10263:SF18; V-TYPE PROTON ATPASE 21 KDA PROTEOLIPID SUBUNIT C; 1.
DR PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 2.
PE 3: Inferred from homology;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU363060};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363060};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363060};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363060};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363060}.
FT TRANSMEM 23..46
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 67..89
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 109..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 149..176
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT DOMAIN 28..87
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 117..175
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 184 AA; 18844 MW; E5F59BD32F1DF9F0 CRC64;
MSIATDALFN QGWGDILTNI SPYAWGSLGI AVGLGFSVVG AAWGIFLTGS SLLGASVKAP
RIRTKNLVSI IFCEATAIYG VIISIILLNK MDVPAVRLPT DPVLSMDQMF FAGYAVFGSG
LAVGLTNIAS GVSVGIAGSS CALADAQNAA LYVKILIVEI FASALGIFGV IVGIIVSNNA
AFPK
//
