ID   A0A368GNP5_ANCCA        Unreviewed;       459 AA.
AC   A0A368GNP5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Vacuolar ATP synthase subunit S1 {ECO:0000313|EMBL:RCN45986.1};
GN   ORFNames=ANCCAN_08023 {ECO:0000313|EMBL:RCN45986.1};
OS   Ancylostoma caninum (Dog hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN45986.1, ECO:0000313|Proteomes:UP000252519};
RN   [1] {ECO:0000313|EMBL:RCN45986.1, ECO:0000313|Proteomes:UP000252519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Baltimore {ECO:0000313|EMBL:RCN45986.1,
RC   ECO:0000313|Proteomes:UP000252519};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Ancylostoma caninum.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the vacuolar ATPase subunit S1 family.
CC       {ECO:0000256|ARBA:ARBA00009037}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCN45986.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JOJR01000089; RCN45986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368GNP5; -.
DR   STRING; 29170.A0A368GNP5; -.
DR   Proteomes; UP000252519; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008388; Ac45_acc_su.
DR   InterPro; IPR046756; VAS1/VOA1_TM.
DR   PANTHER; PTHR12471:SF7; V-TYPE PROTON ATPASE SUBUNIT S1; 1.
DR   PANTHER; PTHR12471; VACUOLAR ATP SYNTHASE SUBUNIT S1; 1.
DR   Pfam; PF20520; Ac45-VOA1_TM; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252519};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..459
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016860015"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          409..447
FT                   /note="V-type proton ATPase subunit S1/VOA1 transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF20520"
FT   REGION          166..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   459 AA;  49537 MW;  E9BF4DB0B20A6479 CRC64;
     MRVLIAVLLT VSSVKAYDAV VFSSEQKITK DYPTIENLLS TASSKSPVVF IVNPDFTLGQ
     FSREANAYSS NKEVSGLPAT VKSAAHHVSR HLTESVYAPG AVTVTSMDNF TPGADIYILA
     GEEWKSMQSL AEAVLPKLGE KYTAVITATE AVSADKSRVK RVVTSEMEHE AANPSGNPSN
     AGGPEVSMPM TLPPYNRSQY PDVKPGKPEL GSCLLYLEGV NIVVQNSKKA FATIPIRSLT
     NTTSWSYADG DVKCNNATNG TYSFIVRLNL KGDVLDSTQK LVKISSGSQV VFKLIFTGAL
     GWWKLTDVVA DSISVQGLDS HGGTSFISGT ATAQSKVISQ TSVNNVGFVS VPGYAFACSD
     SQAAFFKTNQ DGVLIGISLY NTEVQTLGVW PDKKTQQMYF TRQVEDCIGT FSVGSWMGII
     SALILFGGFI FGFLMLNSVQ TMDRFDDPKH KQIVINVRE
//