ID A0A179F1R4_METCM Unreviewed; 1093 AA.
AC A0A179F1R4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Na/K ATPase alpha 1 subunit {ECO:0000313|EMBL:OAQ59387.1};
GN ORFNames=VFPPC_10448 {ECO:0000313|EMBL:OAQ59387.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ59387.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ59387.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ59387.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ59387.1}.
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DR EMBL; LSBJ02000011; OAQ59387.1; -; Genomic_DNA.
DR RefSeq; XP_018137411.1; XM_018288819.1.
DR AlphaFoldDB; A0A179F1R4; -.
DR STRING; 1380566.A0A179F1R4; -.
DR GeneID; 28852813; -.
DR KEGG; pchm:VFPPC_10448; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000078397; 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:UP000078397};
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 155..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..898
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 919..948
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 986..1003
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1024..1042
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1054..1072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..179
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 120803 MW; 89CB29BFC3F66533 CRC64;
MPEDTASPAG ETVEKEGDRD LRIVFDDAAH PRGRTADQGR RRDSRSQSRR RSMSRDGITT
APYSGLPITY RTLSIQVAES RKVETDNIAD AKANKKEDED YFSNLTFHQL QPDQLCQQLN
VSDVSGLSES SAANRLQRDG GNTLPKPKTN YLKKILMYVF GGFCSVLWVG VVVFFVCWKP
LSNPPSPTNL ALAILVIMVI MLQAGFSAFQ DWSTSRTMKS ITDLLPSEAL VMRDGQLKKM
PATQLVSGDV VHLKIGNKVP ADMRLISHSG DIRFDRAVLT GEPDEIEGAV DMTDENFLES
RNIALMGTLV VNGSGVGVVV LTGPRSVMGR IAKATAATEE RATLIQKEIW RFVYIIVALT
ICLALLILFT WVGWLRRDHF EYMNVVAMLN NVMSCVVAFI PEGMPVAVAL TLMMVARKMK
AVNILPKGLA TVETLGCVNV ICSDKTGTLT QNQMHVNSAS FIDEPIELDE FYKTLNSEKP
KASSTRLLAA ASSCNDATFD PTTMNLPVSS REVQGNATDA AVLRFAATAK SAEFGTAVVP
RLFQIAFNSK NKWMLTLHRK EADTNSSANE FQVFVKGAPD VLLPTCTKYW SKKSDSVQPM
DEAARAAFKT YQDKLSRNAE RVIVLCEKTI VATNAPGTNA FSDEIALTAT EDLTIVGILG
IIDPARPETA HTVAECRRAG ARFFMVTGDY GLTAAAIARN TGIFTSEQDP DTIVTIKGGK
HLSAPELALA RTTGERHSLL LEGRDLGNLI QEDWDVICEY GEIVFARTTP EQKLRIVEEF
RKRDNVVAVT GDGVNDAPAL RAADVGVAIV TGSDVAIEAA DLVLLDKFDS IIEAIRWGRL
VFQNLQKVIA YLLPAGSWSE IWPVLVNVFF GVPLPLSSFL MIIICVFTDL FLSLSLIMEK
EEFDLLSLPP RNHKKDHLIS LKIYIQAYLF TGFMETCTAH AMFFLYYWKE AGIPISSLFF
AFEKYTDGFY GYTQDELTHF NAVGQGVYFV TLVILQWGNI LAVRNRRLSI LQADPITEKR
RNPWLILSMV ISLAIAIFVT EVPGIQNLFG TASVPIQFWF IPIPLALGIL CMDEIRKLIV
RLFPNGPVAK IAW
//
