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Database: UniProt
Entry: B0X8H8_CULQU
LinkDB: B0X8H8_CULQU
Original site: B0X8H8_CULQU 
ID   B0X8H8_CULQU            Unreviewed;      1310 AA.
AC   B0X8H8;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE            EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN   Name=6049144 {ECO:0000313|EnsemblMetazoa:CPIJ015651-PA};
GN   ORFNames=CpipJ_CPIJ015651 {ECO:0000313|EMBL:EDS42514.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS42514.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS42514.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ015651-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ015651-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) to UniProtKB.
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; DS232489; EDS42514.1; -; Genomic_DNA.
DR   RefSeq; XP_001865950.1; XM_001865915.1.
DR   STRING; 7176.B0X8H8; -.
DR   EnsemblMetazoa; CPIJ015651-RA; CPIJ015651-PA; CPIJ015651.
DR   GeneID; 6049144; -.
DR   KEGG; cqu:CpipJ_CPIJ015651; -.
DR   VEuPathDB; VectorBase:CPIJ015651; -.
DR   VEuPathDB; VectorBase:CQUJHB014172; -.
DR   eggNOG; KOG0208; Eukaryota.
DR   HOGENOM; CLU_001828_0_0_1; -.
DR   InParanoid; B0X8H8; -.
DR   OMA; KLRYRWH; -.
DR   OrthoDB; 6047at2759; -.
DR   Proteomes; UP000002320; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF12409; P5-ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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.
PE   3: Inferred from homology;
KW   ATP-binding {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|RuleBase:RU362082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320};
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        93..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        282..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        481..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        519..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1042..1066
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1078..1094
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1115..1139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1165..1183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1195..1215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1235..1258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   DOMAIN          79..231
FT                   /note="P5B-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12409"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..26
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1310 AA;  147084 MW;  DEAF8A0AA0B39C84 CRC64;
     MPLETSDLHP EPVPPAHPPP PPDVPDQANG GYKSQMAAAI RSSNRRVEEK HHPEGHSTLV
     ELLTETSQAS VHDILNDGEE DQMFVTGYEK SSVRTFFCYV GFALTLGIMR LVMHWWQHWL
     LLATHRKCSL EVAQKVLVHE RYQDKHDAYY VKNVITMNAE AISEVTSTSK RLSTNGQCIV
     KELQQNGITN RVAFFNECNP FQVAFHRTGG RFEHFDSIRF FCCKKLRYIW SPETKQFVKL
     RGMDVDVPSV TIHHNKGLST YEQNIRRLVY GSNEILIPLR GVVTLLFLEV LNPFYVFQIF
     SVILWFAYDY YYYATVIMLM SGFGITVSII QTQKNQKALY STVKSSDTAT VIRENCESEQ
     IETRLLVPGD VLEIPATGCT MQCDAVLISG NCILDESMLT GESVPVTKTP LPLKRDLNYD
     NKEHARHTLF CGTKVIQTRY IGSEKVLVKV INTGNITAKG GLIRSILYPP PVDYKFEKDS
     YKFIMVLAFL AGCGFLYTVT TKILRGVGAL KIIVESLDLI TIAVPPALPA AMTVGRMYAQ
     KRLQKNNIYC VSPRAINVSG SIDCVCFDKT GTLTEDGLDM WGVLPKDSTN NFQIPLTQIN
     RLPMSEHLLS GMLTCHSITF VNGEMRGDPL DLKIFESTGW ILEEANVSDE TKYDLLFPTI
     VKPPRTDSKD NLNLELDVAY DNSNDIGIVR EFSFTSALQR MSVITRKLSD NHFNVYCKGS
     PEMISSLCKP ESIPEDFTNK LGFYAQQGYR IIAIAYKSLD KKMNYSKVQK VSREKIESDL
     QFLGFVILEN RLKTDTEEVI ESLNAANIRC IMVTGDNLLT AASVAHDCGM VMPGQSLVTV
     TAHVDKSGSN KYFLSYDITG QPQLTQSDII NDNSVSDEKR NGNYTLMTQS NSVSSCETID
     TCTLSTQVSA FEKEAHRITI EGEGEKTIAA GKGGSFRFAL TGKTWAIIKE HFVDLVPTII
     TFGTVFARMS PDQKQHLISD LQNLGYYVAM CGDGANDCGA LKAAHTGISL SEAESSVASP
     FTSKNPTIAC VPKVIKEGRA ALVTSFGIFK YMAAYSLVQF ASVLILYSID SNLTDLEFLY
     IDLFIISVTA FFFGKTSSYD GPLVKQTPSN SLISLSPLLS LALHLIVALG FQVAGWYHIQ
     AQPWFVPFNY TDELALNDLG CYENYAVFCI STFQYIILAI VFSKGAPYRK SIISNYGFLV
     AIIFNTCLSI LLTLYPPVWL QDLFQLVIPQ DDMIFRAYLV GYGVANFILA LFIEKYIIDE
     IAFKKLRYRW HNIAKSRRKY LMIEHSFRKE VQHPSDFKTV LGWSSEKYDY
//
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