ID A0A179F352_METCM Unreviewed; 1084 AA.
AC A0A179F352;
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:OAQ59549.1};
GN ORFNames=VFPPC_03781 {ECO:0000313|EMBL:OAQ59549.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ59549.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ59549.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ59549.1};
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:OAQ59549.1}.
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DR EMBL; LSBJ02000002; OAQ59549.1; -; Genomic_DNA.
DR RefSeq; XP_018137542.1; XM_018283240.1.
DR AlphaFoldDB; A0A179F352; -.
DR STRING; 1380566.A0A179F352; -.
DR GeneID; 28847234; -.
DR KEGG; pchm:VFPPC_03781; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000078397; Chromosome 2.
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 140..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 913..941
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1014..1033
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1049..1066
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..168
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1084 AA; 119297 MW; F58AA7C8D95058BB CRC64;
MAPPGSLKWR VGDEETARST ARTTFVETEK GEGSDSRRRS RSRSRRRSRS IDPANALPIQ
HRTLSIDIEE ARRADYRKSG DRTRDAIVSK FESTEWHKLA TEEIQKRLSV DTQSGLSTSD
AQKRLQEHGK NKITPIPNPI LWTIFGYFFK GFGGILFVGG ILVMVSWKPL GNPPAVANLA
LGIVLFATFL LQAAFSAWQD WSSSRVMKTI NAMLPESCVI LRDGVRSEVQ AMDIAPGDII
FLKAGNKIPA DLRFLEVSHD TTIDRAVLTG ESKPIKATLE STDDNYLETH CIGLQGTHCV
SGSATGIVVA TGDSTVFGQI AKLSGEPKTG LTTIEKEVLR FVLLIVAIMG TWIVILVSIW
GGWLRKEHPN WINVPALIVS CVSVTIAYIP EGLPIATSAS LTITANLMKK HKILCKSLKT
VETLGAVSVI CSDKTGTLTR NKMFATDYSL GTTKLVVGES EKEMQSPATQ QVRAIAGLCN
SAEFDQSSAS LPLADRHIFG DATDQAALRF SESLGPVSAL RDACKFIFEL AFNSKNKFMA
KAFKFQNGQG RSICLSPAEN GSVEADSLFL SVKGAPDILI ERCTSILMPD GTVSPLTSDV
KSRVLLMKDE WSMNGKRVIL LARKLIREPN ILPEPGSPDL EAKMMEELQG GLTLVSLLGI
VDPPRQEIPE VVKTLHGAGI RVFMVTGDFG LTALAIARQC NIVTRDSVHG ISNLVRFPSA
NDDTHKPTPT AAILLNGSDL ITLNDHQWSQ LCAYPEIVFA RTTPDQKLRI VRELQSRDEV
VGMTGDGVND APALKAADIG ISLSSGSDIA IEAADMVLLD SFGAIVEAVR YGRLVFDNLK
KVIAYLLPAG SWSEFWPVFA NIAFGIPQIL SSFLMIIICC FTDCIGSIAL AYEVPEADVL
LRPPRNTKKT RLVNWQLMFH AYAFTGMIET TLSFTMAFWY LQRNGIPFSD LWFKFGELPS
YIDPDYYNSQ LNVASSIYFI NLVIMQWFNL MAVRTRTRSI FQHPPLFNKE TQNLLLFPAI
LIALGLAVIW LYIPELQVVL STAGPPVEFY FYPAALGIGL LGLDEIRKAM VRRYPDGLLA
KMAW
//
