ID A0A016ST65_9BILA Unreviewed; 1243 AA.
AC A0A016ST65;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN Name=Acey_s0180.g767 {ECO:0000313|EMBL:EYB93576.1};
GN ORFNames=Y032_0180g767 {ECO:0000313|EMBL:EYB93576.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB93576.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
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:EYB93576.1}.
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DR EMBL; JARK01001516; EYB93576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016ST65; -.
DR STRING; 53326.A0A016ST65; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR CDD; cd07542; P-type_ATPase_cation; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR047821; P5B-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 272..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 441..465
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 497..515
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 979..1000
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1012..1030
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1042..1068
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1096..1115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1127..1147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1167..1192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 22..175
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 215..265
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
SQ SEQUENCE 1243 AA; 139626 MW; 650FD68E9D6023A8 CRC64;
MGEGGGGRRH HLTLESGEHL LHLYAYKSSS LRTGLFYILS IATFGLFRLI LHWKQKWHIR
FRAARSTFAF ADFVYIVDDH DVEEFHPIHT TRRSYREPPL CHLSSASDNS CLLFHQNPTN
SNNKIIKAFI GPARCQIPFT RYHWVYSGVV PREDGSMREV DEIRWFLYRK LHYLWIEKEK
KIFDDDDERD GQWITPGDIM SQSSPHVFHD TISKGTGFNE HQVSQRLATY GLNSIEINLR
PVPMLLFMEV ISPFYIFQIF SVTVWYNDEY CYYASVIVIM SVCSIIMDVL QTRGQEKRLR
AMVHSSSEVE VIRNGGSVVR ISSEQLVPGD ILLIPPHGCL LQCDAVLMNG TVIVNESMLT
GESVPVTKVA LVEDIHESNF CIEKHSKHVL FCGTQVLQTR YYRGQKVKAV VLRTGFSTMK
GQLVRSIMYP KPVDFRFTKD LFKFVGFLGC ISGCGFVYTI IIMVLRGSSL RRVIVRALDI
ITITVPPALP EFTITRLKVV TIVFAAAMSV GIINAQLRLK NKEIYCISPS TINTCGAINV
VCFDKTGTLT EDGLDFHVLR GVEEANGSDR PTFTTECNRM IREELPQQGE LVNAIATCHS
LTRINGILHG DPLDLILFQQ TGWVLEEAGA DESDHDETEM FDLVQPTVIK PPQNSNKMDE
EYSIIRQFTF SSSLQRMSVI VFNPSSDDRT MTLYCKGSPE MVHSLCDPSS VPPNYFPVVN
EYAQHGFRLI AVARRTLNLN FNKAVKVPRA TVECDLQLLG LVAMENRIKP VTLGVINQLN
RAQIRTVMVT GDNLLTAMSV ARECGIIRPN KRAFLVEHCP GEVDVRGRTK IIVKQSVSSS
GDILDDDPVL TKAERDAELG ELIQSSYHLA ISGPTFAVIT HEYPEVLDSL VSVCDVFARM
APDQKQQLVN SLQEVGYTVA MCGDGANDCA ALKAAHAGIS LSDAEASIAA PFTSKVADIR
CVPTIISEGR AALVTSFGIF KYMAGYSLTQ FVTVMLLYYI SNILTDGQFM YIDMFLITLL
AVLFGNTSAY EKLCPTPPPT RLLSVASICS VLGQLAIMGG TQLFVFLMTT SQPWFVPYNA
PRGSDIEDKR SMQGTAVFYV SVFQYITLVV VYSKGPPYRD TLFSNRPFCA SIAFVTLLSL
VIVMWAPPWL RDFMGNMDLP SVEYRSLLVL IACINAIVSF LFEKVFVERF LLDYMERQTR
RRRVEADYSD ELYAKNGGAL YERILSRIGG EPSWFLPRLS CSS
//
