ID K3WIH2_GLOUD Unreviewed; 1133 AA.
AC K3WIH2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
OS Globisporangium ultimum (strain ATCC 200006 / CBS 805.95 / DAOM BR144)
OS (Pythium ultimum).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Pythiales; Pythiaceae;
OC Globisporangium.
OX NCBI_TaxID=431595 {ECO:0000313|EnsemblProtists:PYU1_T004764, ECO:0000313|Proteomes:UP000019132};
RN [1] {ECO:0000313|Proteomes:UP000019132}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RX PubMed=20626842; DOI=10.1186/gb-2010-11-7-r73;
RA Levesque C.A., Brouwer H., Cano L., Hamilton J.P., Holt C., Huitema E.,
RA Raffaele S., Robideau G.P., Thines M., Win J., Zerillo M.M., Beakes G.W.,
RA Boore J.L., Busam D., Dumas B., Ferriera S., Fuerstenberg S.I.,
RA Gachon C.M., Gaulin E., Govers F., Grenville-Briggs L., Horner N.,
RA Hostetler J., Jiang R.H., Johnson J., Krajaejun T., Lin H., Meijer H.J.,
RA Moore B., Morris P., Phuntmart V., Puiu D., Shetty J., Stajich J.E.,
RA Tripathy S., Wawra S., van West P., Whitty B.R., Coutinho P.M.,
RA Henrissat B., Martin F., Thomas P.D., Tyler B.M., De Vries R.P., Kamoun S.,
RA Yandell M., Tisserat N., Buell C.R.;
RT "Genome sequence of the necrotrophic plant pathogen Pythium ultimum reveals
RT original pathogenicity mechanisms and effector repertoire.";
RL Genome Biol. 11:R73-R73(2010).
RN [2] {ECO:0000313|Proteomes:UP000019132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RA Buell R., Hamilton J., Hostetler J.;
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:PYU1_T004764}
RP IDENTIFICATION.
RC STRAIN=DAOM BR144 {ECO:0000313|EnsemblProtists:PYU1_T004764};
RG EnsemblProtists;
RL Submitted (FEB-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000256|ARBA:ARBA00006934}.
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DR EMBL; GL376631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K3WIH2; -.
DR STRING; 431595.K3WIH2; -.
DR EnsemblFungi; PYU1_T004764; PYU1_T004764-p1; PYU1_G004753.
DR EnsemblProtists; PYU1_T004764; PYU1_T004764; PYU1_G004753.
DR VEuPathDB; FungiDB:PYU1_G004753; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_4_0_1; -.
DR InParanoid; K3WIH2; -.
DR OMA; NGQEYSM; -.
DR Proteomes; UP000019132; 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 GO; GO:0008556; F:P-type potassium transmembrane transporter 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; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
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 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000019132};
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 143..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 862..882
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 888..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..958
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..163
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 22..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 124507 MW; E14BFB2A62631356 CRC64;
MDGPGTPKHA FVRMDDEAVA NLPPSAALRP REASRRSSVR SSAEIIAATE EMRQRIESRK
QRRSKPKPAA ETAGAAEASE DAKRELVMTE HKMGITELAA ELLTDVVHGM NADNIDMRRE
TEGLNQLTPP KKVPEWLKYW RELTGFFCLL LWAGSLMCFV SYAIQYSVDN LYLGIILALV
VLITGSFSYV QNYNSSNLME SFKNMMPTMI TVIREGKSQK IDASLLVRGD LVVLKGGDKV
PADIRIIECS DDLTVDNSSL TGEPEPLKRI PECTDENPLE TKNLCFFGTF VPQGSGKGIV
VNIGDKTVMG RIARLATSTV VDQTPIAKEI DHFVHVIALV ATIIGLFFFI VGFLIGTDFV
SNLVFMIGVI VANVPEGLLA TVTVCLSLAA KRMAGKNMLV KNLQGVETLG STTCICSDKT
GTLTQNVMTV ANVVYDNKIW DAECSITPVG NYSMQDVSFQ HLQRCATLCN NAVFDEESKY
EKIVRGSGDT LTITRGAPLP VKTEDGKMNW ETIGDASESA MIKFCQDKKD VVEYRNENAK
IKEIPFNSKN KFQVSIHKQN NDDSVPMLLV MKGAPERIIS RCHTILLNGE EVELTADKLA
EIEKLQLELS KRGMRVLGFA EKVLDPTKYP SDYKFNTDIP NFPLGEKDVD FSAVPKPHPN
VQEGLCFIGL MALIDPPRAE VPGAVEKCKT AGIRVIMVTG DHPVTAKAIA HKVGILWGPT
KEDIEEGNAS RGLVRGSAGW EDPETAPAIV VPGWDISVDT PVEEWDRILD HSQIVFARTS
PQQKLIIVEN CQRRNEIVAV TGDGVNDSPA LKKANIGVAM GIMGSEVSKE AADMILLDDN
FASIVSGVEE GRIIFDNLKK SIAYALAANI PELIPFLLNI VIRIPLPLTT VLMLAICLGT
DMVPAISMAY ESAESDIMAR APRNAAVDRL VTKKLISFSY LQIGIIEAAA GMFTYFVVMN
DFGYPPRVLP GLGMGTSFGR QVMWCKTTGG EFCTPGGRHK NDAGVWTSLG ASETPVCEKD
YNATIPAGGS IYDARIFWAP NHDGKVKDCQ YALANFKGSN HKPEGYERLN IATYKGYTAD
QEVPTLQSMQ AAWLAGYRPY FPMRARRSHF FNKNWMHWDV SDSDAEGWSR TCS
//
