ID A0A0F7ZVM7_9HYPO Unreviewed; 1093 AA.
AC A0A0F7ZVM7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=HIM_03760 {ECO:0000313|EMBL:KJZ76883.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ76883.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ76883.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ76883.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
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DR EMBL; KQ030509; KJZ76883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZVM7; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000054481; 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; 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 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; 2.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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.
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:UP000054481};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 922..950
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 985..1002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1023..1042
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1048..1072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..170
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 120401 MW; 7D9AA3D152A404D1 CRC64;
MASEKPVETQ VVERIRWGDE EQGRPRRRSS RPPLSRTNSQ DSLAIRSITS RAQVDPALTL
PIQYRTVSFQ IEESKGRDRA ELARAANSAA KDLSDLEWHT ITPADVTERL RTSPTGGLSE
DQAKRRIQEY GRNAPSPPKT NRLLTIFGYF FKGFGGILLI GSILVFISWR PLGQPPALAN
LALAIVLLAV FFIQAGFAMF QDWSTSRVMS SIKDMLPEHC QVTRDGQILN IPAESLVPGD
LVSIKAGNKL PADLRFIEIS SDAKFDRSVL TGESRPVAAT VDHTDSNYLE TLNIGMQGTH
CIIGSGKGIV VATGDRTVFG RIATLTNEPS TKMTTLEREV LYFVTFICGI MFTMIAVVLI
VWGAWLRRDY PNWINVATLI VDCVSVAVAF IPEGLPIAIT AGLTITANMM RKNMILCKSL
KTVETLGSVS GKMSLTDCSI GASNMSVESL KQDLASEKAG DAHDKKTAPF LQLGAMAALC
NAAEIDAAQN DVPIERRNIF GDATDTAVLR FSESLADGNV GYFRACWNRV FELAFNSKNK
FMIRCFTIAR REALPFTLHD TAAESFTDDD LLLTIKGGPD VLISRCSEYL APSGELMPID
AQMADNFERV KNIYSSQGKR CLLLARKILT AGTITAEAGT PKYEEAMMEE ARSGLTLVGL
VAIVDPLRPE IRDVVSTLRG AGIRIAMVTG DFALTALAIS REAGIVSCLQ VDAVENLERT
PDIGSGSDSE DSKTSSSGSR GAIVISGPEL TGLNEHQWKL LTEYEEIVFA RTTPEQKLRI
VREFQNKEVV AMTGDGVNDA PSLKAADVGI SMGSGSDIAM EAADMVLLDT FSSVVVAVQY
GRVVFDNLKK VIAYLLPAGS FSEFWPVMTS VLFGLPQILS SFLMIIICCF TDCAAATILS
FEKPEADVLL RRPRNVKKDR LVNWQLIFHA YGIIGVTETL ASFAMSFWYL QRNGIPFSDL
WFSFGRLPSS IDPDYYNAKL TEASSIYFVN LVVMQWFNLM ATRTRRLSIF QHPPLFNKDT
ENLYLFPSIL FALGMAVIWL YPPAIQRVIG TAAVPVEHWF LPFAFGAWII LLDEARRFWV
RKHPNGLLAK AAW
//