ID F1KSX7_ASCSU Unreviewed; 1214 AA.
AC F1KSX7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
DE Flags: Fragment;
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY40981.1};
RN [1] {ECO:0000313|EMBL:ADY40981.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
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}.
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DR EMBL; JI165340; ADY40981.1; -; mRNA.
DR AlphaFoldDB; F1KSX7; -.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
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; 3.
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 SMART; SM00831; Cation_ATPase_N; 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 2: Evidence at transcript level;
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 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 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 177..201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 378..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 414..435
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 930..949
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 961..990
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1010..1032
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1044..1066
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1086..1111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 132..205
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1190..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1214
FT /evidence="ECO:0000313|EMBL:ADY40981.1"
SQ SEQUENCE 1214 AA; 135335 MW; CDBAEC942D53241E CRC64;
MSSSCEHSAH ITVADETLQL WGYRINKFKT ALTWLGTVLT FGAFRLLLYW YPKLFVKCTA
SRCALATADS VLVRDDHMNI SFRPVRFMIS KPGCQVAIPS GAFHMNDVVK FRYFTYKKLT
HIWHPVEMKF MTVESMDGDI AFSRFHELAE NGLSDAEVKK RMLTYGKNVI EVKLKPILVL
LFKEVISPFY IFQIFSVSVW FSDNYELYAS IIVLMSVMSI TIDVFHTRKQ EINLRSMVHS
SDTVQVIRNG GQLKVVLSEQ LVPGDVIVIP SHGCTMQCDA VLMNGTVIVN ESMLTGESVP
VTKVALPDAE EEGSSVFSIK EHSRHTLFCG TQVLQTRYYS GRRVKAVVLR TAYSTLKGQL
VRSIMYPKPV DFRFTKDLFK FVGFLACIAA CGFVYTIAIM ILRGSNVKKI LVRSLDIITI
VVPPALPAAM SIGIISAQIR LRKKQIFCIS PSTINTCGAI NTVCFDKTGT LTEDGLDFHC
MRPVRKVEDG KQPIFDGEFL AFLSDEMSAY GELIKAISTC HSLTRIQGEL CGDPLDLILF
KHTGWSLDET VGSGVDETDR FDVIQPTVVR NVPGHFGFDS QMELAIIRQF TFSSSLQRMA
VIVHNPSEQS HSMTLYCKGS PEMVASLCRS ETVPTDYTSI VSDYAQHGYR LIAVAYRKLE
LSFAKSQKIK RELVECDLEL LGMIVMENRL KRQTVGVIHQ LNKARIRTIM VTGDNLLTAL
SVARECAIIQ PAKRAFLVET APLPEKSADK RTPLILKQSV SSSEDVIDGC SSTLDVEAGH
LVDSTYQLAI SGPTFAVVCH EYPELIEKLV TVCDVYARMS PDQKQLLVNK LQEVDYTVAM
CGDGANDCAA LKAAHAGISL SEAEASIAAP FTSKIPNIRC VPIIIREGRA ALVTSFGVFK
YMAGYSLTQF ITILHLYWLN TNLTDFQFLY IDMGLVTLIA LFFGNTPACE KLSSTPPPAR
LLSLASVLSI AGQLAIVTSF QLFIFLYTTF QPWFIPYSVP LGNEEEDKRS MQGTAIFCLS
TFQYLTLAVI YSKGFPYRKT LFSNTPLCLS LLVLAITSII ICVYPPSFAN SFMEFDPLPE
TGYRLFILVI GFICAVCAYL YETYFIDHLI LNVRERRRKA RHLRSGSSET SRFEKILHSI
GSEPSWVTLS PRGDRSPDSA IVGHVDHSET TETLLSPSCY TTPPTSPIKV AANGSAHDSS
DRCNSEKQFY DAQQ
//
