ID A0A165EVY8_9APHY Unreviewed; 1066 AA.
AC A0A165EVY8;
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=Calcium ATPase transmembrane domain M-containing protein {ECO:0000313|EMBL:KZT07880.1};
GN ORFNames=LAESUDRAFT_736149 {ECO:0000313|EMBL:KZT07880.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT07880.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT07880.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT07880.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV427617; KZT07880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EVY8; -.
DR STRING; 1314785.A0A165EVY8; -.
DR InParanoid; A0A165EVY8; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000076871; 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 Pfam; PF08282; Hydrolase_3; 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 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:UP000076871};
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 107..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..846
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 893..920
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 953..976
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 996..1015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1021..1044
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..131
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 680..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 117510 MW; E66AAA57C4560D9E CRC64;
MPTKMSPAAT TGNPGDYGIQ IRYRTLSIHV NATRDEKQHP PAKSKGAADP ETTIRQINVH
MLPVDEIYSR YSTSPTVGLD SAAVQRRAVQ GGKNVISPPK SQYWKKILNY IFGGFNFLMW
IAFIVTIISY QPLGGAHPSA FNLGVAILLL LVIIISATFY ALVDWHASRI MSSITTLIAE
NASVIRDGQH QTISAKDLVV GDIVTLSMGD RVPADIRLVQ ASSDLHFDRS LLTGESELIP
GALEMTSDNA LETRNLALTS TFVVQGNCLG VVFAIGDKSI MGRIVAMSSE TKFKLTTIQR
EVWHFTKIIS CIAITMFSIA LIVWGAWLRS SYPGYETASV AIIDSIGCLT AFVPQGLPVG
VALSLTIVAK RMAKRNVLVK NLATIETLGC MSVLCSDKTG TLTMGKMSVQ NVAFVQDQFR
VEDIKEKYSG RDSTNAPAGL KALHMVGRLC NGAKFETSSD DLPIDERPVK GDATDTAVLR
FTEALTIPSL AVDTPSLLAS YEKIFEIPFN SRNKWMLTVV RENRPIGAGE DWQPETWMLV
KGGPDVLFPT CTSVMRADGS VDHLDSAIRS QLFGLQEEWS SQGQRVLALC RRSLADVKLD
MQKMSANDVE ELMYSELQQL TLVGLVGIRD PPRADVPGAV ETIRRAGVRI FMVTGDFKLT
ALAIAKQVGI VTQEKADEVE HLRSPKSEKG YAGLPPSEIK PGEDDPIRAL VLTGEDVETM
DSNDWDEAVG NYTEIVFART TPEQKLRIVE EVKARGDNTV AVTGDGVNDA PALRASDIGV
AMGSGSDVAK EAASMILLNN DLSSIVVAIE MGRLVFDNLK KVMLYLMPAG SYAEFVPVFA
NVFLGMQLAL SSYLQVCYCV FNDITMSISL MYEKPEADLM LRKPRNARTD RLADWRFFVQ
IYLFIGAMLW PCCMSMWFLY MDKQGLGFYD VMLVYNKWTE GHKGYTQDQL NHFVSVGQCI
YYVTMVFGQY GSLLAIRNRR VSILQSNPFW GPRRNFIIPL GMIGTALVAV VNLYGHGLRK
VFGTAAIPGM YWGIPFGFAC GILIMDELRK LIVRTYPKSF VAKMAW
//
