ID A0A067D8V0_SAPPC Unreviewed; 1335 AA.
AC A0A067D8V0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=SPRG_00285 {ECO:0000313|EMBL:KDO35437.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO35437.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO35437.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO35437.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000256|ARBA:ARBA00006934}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK583189; KDO35437.1; -; Genomic_DNA.
DR RefSeq; XP_012193777.1; XM_012338387.1.
DR STRING; 695850.A0A067D8V0; -.
DR EnsemblProtists; KDO35437; KDO35437; SPRG_00285.
DR GeneID; 24122932; -.
DR KEGG; spar:SPRG_00285; -.
DR VEuPathDB; FungiDB:SPRG_00285; -.
DR OMA; PGMREMV; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000030745; 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; 2.
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; 2.
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 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:UP000030745};
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 125..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 861..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1212..1230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1251..1271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1283..1299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..145
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1335 AA; 146161 MW; 7B7CB9FBC95435E8 CRC64;
MERQNSLRER AGSARLRAGS HRASMRQRSS ADIVAVSTEM RQRMEARKQA KKGGKKGGDD
HHDARRELVM TEHTVSIPEL CADLMTDDEV GMSTDHVEMR KQKEGLNMLT PPKEVSEWVK
LFRELTGFFS ILLFVGAAAC FGCYFLAYDI TQIYTATALF TTILVTGFFS YFQNRKSSNL
MESFKNMMPT MITVVRDGKS QKINASQLVR GDIVLLKGGD KVPADIRVVE CSDDFLVDNS
CLTGESEPLK RVPHCTDENP LETKNLCFFG TLIPQGNGKG IVVNIGDSTV MGRIAKLATA
TGTELTPIAR EINHFVHIIT GVAVTTGVIF FIVGFIKKLE FSTNLAFMIG IIVANVPEGL
LATVTVCLSL AASRMAKKNM LVKNLEGVET LGSTTCICSD KTGTLTQNIM TVANVVYDNK
IFDAECSLTP TPSYNVADDS FVRLQRCATL CNNAVFDEES KFETIVSADG DAISRGAPLV
FKVGDKINWE TIGDASESAM IKFVQDKRDI MEYRKACPKV KEIPFNSKNK YQVSIHKLDD
DESKNLLLVM KGAPERITAR CGSVMINGQE LPMTPERLAE IDDLQLQLSK RGMRVLGFAE
KSLDVARYPH SYDFSTDNPN FPLGEKDVDY DMIPTPFKNV EEPLCFVGLM ALIDPPRPEV
PGAVEKCKTA GIRVIMVTGD HPVTAKAIAH KVGILWGPTK EDIEESNAAG NLYEDPSSAR
AIVVPGWTIS VDTPEEEWDR ILDHPQLVFA RTSPQQKLII VENCQRRKEI VAVTGDGVND
SPALKKADIG VAMGIMGSEV SKEAADMILL DDNFASIVCG VEEGRIIFDN LKKSIAYALA
ANIPELVPVL LNVIINVPLP LTALLMIAIC LGTDMVPAIS MAYEGAENDI MLRPPRNAAV
DRLVTKKLIT FSYLMMGIIE ATAGMFCYFT VMNSFGYSPK VLPGLGGAYY GRHVLWCKTD
GGVYCSAGGK SLDTPLGAFG PDAKCGLMYN ATIPTGGNIF DAQIFWDPKE DGTLVDCQYA
VGNFAGSDSK PDNFDKFNPT TYGSFTNKNA VPTYQSMAAA TAAGYHPYTP MKARRSSFFK
KTYLEYDVTS SDVVGLGGAT PELMASYQPF GVWAATSTDT DGGLTSSDYV DNFKDQLVAI
VSANGTASAT TAPMGDQKYS KATYVRQVKN ADGSVTCSGV ACLLDFAAGF SYTDASGKTY
SNVLSRVMQS EALAIAQTAY FVAVIMSQWG NLLICKTRYL SLFTQGMHND VMFMGLMFET
LLGAVMSYSG FFNTIFSTGS MRLTHWFCGM PFTLLIFSVD EMRKYMLRET SVTTVDPDTG
RMVRTPGWIE RNTYY
//
