ID A0A1I7S407_BURXY Unreviewed; 1349 AA.
AC A0A1I7S407;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=BXYJ_LOCUS9540 {ECO:0000313|EMBL:CAD5226995.1};
OS Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS xylophilus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC Bursaphelenchus.
OX NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0773900.1};
RN [1] {ECO:0000313|WBParaSite:BXY_0773900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:CAG9116608.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ka4C1 {ECO:0000313|EMBL:CAD5226995.1};
RA Kikuchi T.;
RL Submitted (AUG-2020) 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; CAJFDI010000004; CAD5226995.1; -; Genomic_DNA.
DR EMBL; CAJFCV020000004; CAG9116608.1; -; Genomic_DNA.
DR WBParaSite; BXY_0773900.1; BXY_0773900.1; BXY_0773900.
DR eggNOG; KOG0208; Eukaryota.
DR Proteomes; UP000095284; Unplaced.
DR Proteomes; UP000582659; Unassembled WGS sequence.
DR Proteomes; UP000659654; 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; 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; SFLDS00003; Haloacid_Dehalogenase; 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 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:UP000659654};
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 139..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 287..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 317..335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 490..514
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1019..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1047..1067
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1088..1111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1131..1153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1165..1184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1204..1222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 230..315
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1349 AA; 151780 MW; 1EB90B9995561187 CRC64;
MQGEGESNIF GSIFPTRRWS GDAEREQLIS QASPTFDQPT TSRQDNYGSL ENPRRRTLRA
SDPEMANMVV RKNKESPKIR TALSAGHLEN LETTSDSSSE DSFEFHGASD AANAHYAVIH
LNDEDLHIWA YKLCLWKAIL MYLFSFATLG IVRLVLYWYP KLYVHCTSNK STMAESDYML
VRDDHQNLAF RKIRIAKPPS NDFLSMPVGK GKMVSVSSLR YFTYRKLCYV WHPTESRFST
TDQLENDLPL GYFHDCWDGQ KGLTEAEVQR RLTVYGKNLI EVKLKPIIVL LFKEVISPFY
IFQVFSVLVW YSDDYEYYAS IIVLMSVCSI VMDIFQIRRQ EKKLRAMVHS EDVVEVVRDG
GKVKKVSSSS LVPGDVILIP PRGCILQCDA VLMNGTVILN ESMLTGESVP VTKVALPEPE
DDKHREYEFS LKEHSKHILF CGTSVLQTRF YGGKPVQAIV LRTAYLTLKG QLVRSIMYPK
PVDFRFTKDL FRFVGFLSMI AMVGFGYTIA VMIMRGSALK KIILRSLDII TIVVPPALPA
AMSIGIFAAQ MRLRAKQIFC ISPSTINTCG AINVVCFDKT GTLTEDGLDF HCLRAVYEEP
RQLQAVREEA HEPVFGEELY EFHRDELPHD GELVKAVATC HSLTRIENEL CGDPLDLILF
NKTNWIIDES PTDDQIEETA LFDMLQPTVI RSPAGHFGSN EPETEMAVIR QFTFSSSLQR
MGVIVHNPNE PGRSMHLYVK GAPEIVASLC RPESVPSSYD NVVNHYAQHG YRLIAVASRK
LDLSYAKAQK VKRDVIECDL RMLGVIVMEN RVKTQTCPVI GQLNKARIRT VMVTGDNVLT
AMSVARECGI IRPYKRTFLL EHGGVMGDGR VHLSLRQSAS ASDELNEFEE SSTTVDPECG
HLVDSSYQLA ITGPTFAAIC DDYPELLDKL ICVCDVYARM SPDQKQLLIN TLQEVNYTVA
MCGDGANDCA ALKAAHAGIS LSEAEASIAA PFTSKIPDIR CVPMVIREGR AALVTSFGVF
KYMAGYSLTQ FITIMQLYWL NTNLTDFQFL YIDLGLITLV ALFFGYTPSC EKLDSTPPPT
RLLSLASALS IIGQLFIIAG FQLFVFIYTA MQPWFIPYAM PMGDDVEDRR SMQGTAIFCV
STFQYITLAI IYSKGHPYRK PLFSNRPLCF SLIILSLISA WITVNPPDFL SSWLEFDPIP
YFENRLFLLM IAILSGLCSY LFENYVIEHV ILGVRERRKK RQQIVADSSD APRFERILNS
IGSEPQWIRN LTTAGLRSEP SLFTPTHNKF RRIEALNSTQ EDRQSLNSGL VVLRSPNNDS
FASGHPDLNS PSTDRSSAVL LPSNSQLNV
//
