ID A0A2N5W8H0_9BASI Unreviewed; 1516 AA.
AC A0A2N5W8H0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
DE Flags: Fragment;
GN ORFNames=PCANC_00022 {ECO:0000313|EMBL:PLW58527.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW58527.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW58527.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW58527.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) 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}.
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:PLW58527.1}.
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DR EMBL; PGCJ01000002; PLW58527.1; -; Genomic_DNA.
DR STRING; 200324.A0A2N5W8H0; -.
DR Proteomes; UP000235388; 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; 1.
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.
DR PROSITE; PS01229; COF_2; 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:UP000235388};
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 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 502..518
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 524..542
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 711..735
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1270..1288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1294..1313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1334..1354
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1381..1399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1411..1430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 293..441
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT REGION 1..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PLW58527.1"
SQ SEQUENCE 1516 AA; 169161 MW; 0D23F284ADC0F13F CRC64;
QQDNTGNMDD SPSAGPSLDQ DTLPVSQQEE TDEVDDFRFD DREQQPNLPD LLIYDDPTGS
MFSGPVAEVT PSSVTNMHLD TRFDSRSCRS TRSPGEGTSI RESRPPNHRR KPSVSSRSIR
SHAPSKSSRS RRAQDDRKSE AGVSVTSSRR HTTLSKTKTQ DSTRLSPTEE PESGFFNNLS
AFLKGKGRSR SRDSRASSSR DNYHYHSVND KRRRQSLSRS IRSAKSSTWR SLKSARSKSR
KTPNEGLNDH RIEVIPLTHP ISNSQGHSWH PTDHEMTKAQ RLSTQSVYII EDDLQIQFFG
WKSVGWKVTL WWIGCVMSTG ILWLVGRWKV AWRLKMGILK PFNLASHIVA YTEYGQPDII
DLQILTFSQP IKLSTLCPPS LRVPPTSKDD PLIPINSDTT TKSPSPIPTE PASEPPVNRP
LSELLLTEIH YIDFRYHRFL LHPITQAFMR ARDWQDPAWS KSVANLAVGL DHQESLHRTQ
LFGNNIIEVA GKSTSQLLMD EVLHPFYIFQ IASIILWSVD DYYYYAFCIA LISVISVLSA
LMDMKRNLAR MRELSRFTCE VKLLRGASWL AAVSTELVPG DVIDVSETSL HTFPADLLLL
SGDAIVNESM LTGESVPVSK FALPSSNLNL MASLSGDPSP ALAKHILFCG TNIIRVRKAN
QLARSKGSVP ENAALAMVVR TGFSTTKGAL VRSMLFPKPM DFAFYRDSFR FIGALTLIAG
FGFVGSSINF LRMGIDWRTI MVRALDLITI VVPPALPATM SIGTSFAMSR LRKKKIFCIS
PNRVNMGGKI NLVCFDKTGT LTEEGLDILG VRTVDRSDGN FSELYDEIDN VPVVGAEDLK
TPLVHALATC HGLKAVNGQI IGDPLDLRMF QFTGWSMEEA GDSLGPSNTP DESQTLLPSQ
PHKTPKMIER QAALVQTIVR PPGGSTFEVE DALKSTRFLE LGIIRTFDFA SELRRMSVLV
KKLKSSTIEA YVKGAPEAMV GICMKETLPA DYEEFLNYYT RHGYRVIAVA AKSFPKLSWI
KAQRLTRSQV ESELRFIGFV IFENKLKLAT EPAIQLLKSA HIGVRMCTGD NIRTAISVGR
DCGMIEDSMR VYLPTFTSEG SSTLADSTIA WFDIDNESAL LDPYSLMPLP IQNDESDTRS
MDSHVTSIRS EDYVLAVSGD VFRWIMDYGS LETIERMLYK GVIFARMSPD EKHELVEQLQ
GLDYTVGFCG DGANDCGALK AANVGLSLSE AEASVAAPFT SRQPEITCFI DLIREGRCAL
VTSFSCFKYM ALYSLIQFTT ITLLYSLPSS LGDFQFLYID LFIIIPVAVT MGRTHPYGRI
VAKRPTANLV SKRVLTSLVG QILINSTVQL LVFLRVASQH EPVQVPANGE KLPTTNQENS
ALFLVSIFQY ILVAATFSVG PPYRKPIFSN YLLVLCLLIL GGFSLNLLFL DSGFLFNLLE
LVPLDYALRL ELLLWISFNI FSSWLFENYA TQPIALWVGG QSKSLRKQWN VVFGCDGSSK
RDRKRYKIIA DSMETF
//
