ID W6ZDL1_COCMI Unreviewed; 1077 AA.
AC W6ZDL1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=COCMIDRAFT_88396 {ECO:0000313|EMBL:EUC48090.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC48090.1};
RN [1] {ECO:0000313|EMBL:EUC48090.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC48090.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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DR EMBL; KI963945; EUC48090.1; -; Genomic_DNA.
DR RefSeq; XP_007685454.1; XM_007687264.1.
DR AlphaFoldDB; W6ZDL1; -.
DR GeneID; 19127255; -.
DR KEGG; bor:COCMIDRAFT_88396; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_4_1_1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 148..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 865..885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 906..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 969..986
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1007..1026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1038..1056
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..172
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 28..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 117790 MW; 4A49BE281FF881EF CRC64;
MDNEEKGIPR VRFGELNLPA EADGYVTHDR RHERPLSRRS SVGSMSIRSA GGARTVQPET
ALPIAYRTLS IEVDERQLEK QAETKKAKEK AAIDVAGLEW HTLAVPDLCQ RLSVNTECGL
SDDDVKRLRN QYGLNKITPP PSGLVGKLIG YFFGGFGSIL IVAGILVFVS WKPLGDPPAT
ANLALACVLI AVWLIQAGFN AWQDWSTSKV MASIGTMLPD QCIVVRGGSQ TSISAQDLVP
GDVIVIKQGN KLPADVRFIE VSGDAMFDRA ILTGESEPVN ATVNRTEDNY LETNNIGLQG
THCVSGSCMG VCVATGDDTI FGRIAKLTSN PTTGMTPLQK EIWHFVLIIS AFIFCVVVFI
IILWAAWLRT AHPKWINVPQ LIVSCVSAAV AFIPEGLPIA LTTSLTIVAN MMRKNKILCK
SLKTVETLGS VSVICSDKTG TLTKNKMVVT DVCSVDKTYT VDAALREMAA AEFVTNGTVP
KPAAIDQIRI VGGLCNSGEF DAATMHLPIA DRKINGDATD QAILRLSESF GSISELRNQW
KKTFEIAFNS KNKFMVRIMV AADQPSTSSV GTLLVKGAPD ILLPRCELAL NEQGEEVVMS
DLKRQWIEGV KDDWSRQGKR VILLARKPTI VATSGAQEKD VLASIRDGLT FVGIVGIVDP
PRDEISDVVR ILRGASIRIF MVTGDFKLTA QAIAEECGII SNSAIVDDIS ALDRYGNSTG
KSKQAIVLSG SELITLNEAQ WDQLCAYQEI VFARTTPEQK LRIVKEFQAR ENVVGMTGDG
VNDAPSLKAA DIGIAMGGGS DIAIEASDMV LLDSFAAVVE AVKYGRLVFD NLKKTIVYLL
PAGSFSELWP VVTNVVFGIP QILSSFLMII ICCLTDCAAA VTLAYEKPEA DVLVRPPRNI
KKDKLVNARL IFHAYFFVGL LQCFLAFTMS FWWIERNGIP FTAMWLKFGN YDPQYSPELI
TKLTNEASSI YFVTLVVMQL FNLLATRTRR LSIFQQPPIF NKATQNLSLF PAMIFAIAVA
FIFLYIPSLQ NVISTTTVPV EHWFLPAAFG AGLLLLDEAR KYCVRSWPNG FLAKIAW
//
