ID A0A0M8ZZJ9_9HYME Unreviewed; 1233 AA.
AC A0A0M8ZZJ9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=WN51_00223 {ECO:0000313|EMBL:KOX74320.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX74320.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX74320.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX74320.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX74320.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ435791; KOX74320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8ZZJ9; -.
DR STRING; 166423.A0A0M8ZZJ9; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000053105; 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:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
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; IPR004014; ATPase_P-typ_cation-transptr_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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 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 PROSITE; PS00154; ATPASE_E1_E2; 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:UP000053105};
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 246..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 417..434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 446..469
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 910..934
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 946..962
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 983..1007
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1030..1048
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1060..1079
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1099..1126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 55..181
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 197..256
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1233 AA; 140559 MW; 23474FB57A190E26 CRC64;
MRSIGKLYCG KSEQSPIGKQ RGDKFVHQST RDTEWHRIKN AQTSAVQWQK IHTGQDEDMC
VYGFEKSRLK SILTYVSYIL SIGWVRLFFH WYPQLHLYAT HNKCSLSCAT KLLITDNYQG
KYKSLFQQRI SENLLKDLGN DKQLAEKIRY KKLMINLENG TQCQIYEYKA FWCKKQCYIW
DVTQNTFSRL VGLDKYTLCS DLNLNKNRGL SKEEQCLRRI VYGSNEIIVP VQSIGVLLLL
EVLNPFYIFQ VFTLCVWFAE GYLYYTVAIN QINLRGTVAS TETVRVYRNS KVAENIPSND
LVPGDVIELP KHQATIVCDA VLLTGQCILN ESMLTGESVP VTKTPLPSHH VLYDSKECSH
HTMYSGTTII QTRSYNGRPV LARVIRTGFH TSKGSLVAAI LYPPPADFKF DQDSYKFIGI
LAVIATCGFI YTIVTKASRG ITAGDIAIKA LDIITIVIPP ALPAAMTVGK LYAQVRLKRA
QIYCINNRVI NVSGSINCVC FDKTGTLTED GLDMWGIVPC TNGILGEAER TISKLNDHPL
FEGMLVCHSL TLIDSALCGD PLDVKMFEST GWILEEFNNE HSNKYDLIAS TIMKPPKNNN
FTQNMNKISE IGIMQQYQFS SSLQRMSVII RVLGSNMFKA YTKGSPEMGY RVIAMGRTEL
PENTNKITKL PRDAVEQNLE FLGLIIMENR LKSPTIPVIK ELRTANIHVL MITGDNIQTA
VSVAKECGIL SSQEYVIDVT VVMEENKLQP EIYFNAQEMS PKLFNSIRKL ICRKIKKELT
ISLNKKLNIP NLKDIERNID STNYRFALTG QSWQLLREYY PDIVAKICVR GAIFARMTSD
QKQQLVLELM QLGYYVAMCG DGANDCGALR AAHVGISLSE AESSVASPFT SKIPDITCVP
KVIREGRAAL VTSFGIFKFM VTYSLTEFLS VVILYSIDSN LTDLEFLFID ICLIVNFASF
FGKTQAYEKQ LVKKPPMTSL LSFTSIFSLS VHMLIMTIFQ AVAYHAVRTF PWFTPFIYND
ENSYMCYENY SVYCVSMFQY ITMAIIFSRG KPYRKAIYTN ISFIFSIILL IIVCTYITIY
PANWIINMLQ LLVPPVYNWR IIILILAFAN FVLCFFVEMF VIEYLIEKKF KLKFYKLEKS
KKKYLRIEHE LKNNLSWPTL SKELPTLPLS PSVENIINVT NSKERSYNNK TKNNLESNKT
VELIKSNNRL CVFDNYSFVD DESLRNINMI TKV
//
