ID A0A166ZZ94_9PEZI Unreviewed; 1104 AA.
AC A0A166ZZ94;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Na+ h+ k+ antiporter P-type atpase {ECO:0000313|EMBL:KZL79533.1};
GN ORFNames=CI238_05822 {ECO:0000313|EMBL:KZL79533.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL79533.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL79533.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL79533.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL79533.1}.
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DR EMBL; LFIW01002076; KZL79533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166ZZ94; -.
DR STRING; 1573173.A0A166ZZ94; -.
DR Proteomes; UP000076584; 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000076584};
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 151..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 342..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 892..912
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 993..1013
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1034..1053
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1065..1083
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 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 122274 MW; A13ADFD1F47FFC5F CRC64;
MDESEKQQSQ AAGERIRWDA DEEAGRKAHR SSTGPALHHA RSNTSMSIHS IRSRRNSIDA
AAELPIQYRT VSIEIEEYKT KTEAIKKAKN VATELSELEW HILSVDEILR RQSSSLADGL
SPDQIQRRMA HYGRNAPSPA PTNHTKRILG YFFKGFGTVL LMASILVFIA WKPLGSPPAV
ANLALAIVLL AVFFIQAAFN MWQDWSSSRV MNSIKTMLPE NCMVIRDGHQ VELLADQIVP
GDILIVKSGN KLPADVRFLK VSSDAKFDRS ILTGESVPLP ASVESTDNNY LETRCIGLQG
THCVSGTCTG LVVATGDNTI FGRIAKLTNE PKKGLTTLER EVLHFVLIIC SIMFLMIVIV
LIVWGTWLRK QYPDWINVPN LIISCVSVAV AFIPEGLPVA LTASMTISAN MMRKNKILCK
SLKTVETLGS VSIICSDKTG TLTQNKMIVT ECAIGTMTMT AEGARDALTL NKHNAPNNNS
LEQLRAVAGL CNAGQFDAAT MRLPLHERVI HGDATDQAIL RFSESLGQVS ELRRCWQTKY
ELAFNSKNKY MIRVLGLSHP DGLSFALPSD TASVFQPGDV LLTIKGAPDV LMPRLSNYVN
PSGYTVALDP STRASIEQIK DEWSAQGRRV LLLARKAISR SALKGNPSDS SYEMEINNQA
KAGLTLVGIV GIVDPPRPEI PEVMNTLRGA GIRIFMVTGD FALTAQAIAA ECNIISVPRS
QIDDITALQR MTHVDPSIKP VMDDLESSPR HALVLSGPEL MTLNEEQWDQ LAQYQEIVFA
RTTPEQKLRI VRELQARHQI VGMTGDGVND APSLRAADVG IALGSGSDIA IEAADMVLLD
SFSSVVEALR YGRMMFDNLK KTVAYLLPAG SFSEFWPVMT NVMFGIPQIL SSFLMIIICL
FTDAAAAIAM AYEAPEADVL LRKPRVPGKD RLVDWQLVVQ SYGLVGILET LSSFAMSYWY
LERNGIKFTD IWFSFGHLPS NIDKDYYQQK LNIASSIYFV NLVVMQWFNL MAIRTRRLSL
FQHPPVGNKR TQNLYLFPAI VFALLMAIFW LYVPEFQTTL GTAPVPVEYW FLPMTFGLGI
LLIDEARKFA VRRWPNGIVA KAAW
//
