ID A0A165H1N5_9APHY Unreviewed; 1140 AA.
AC A0A165H1N5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Aminophospholipid-transporting P-type ATPase {ECO:0000313|EMBL:KZT11119.1};
GN ORFNames=LAESUDRAFT_691638 {ECO:0000313|EMBL:KZT11119.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT11119.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT11119.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT11119.1,
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; KV427607; KZT11119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165H1N5; -.
DR STRING; 1314785.A0A165H1N5; -.
DR InParanoid; A0A165H1N5; -.
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; 2.
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; 2.
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 146..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 838..860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 950..970
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1020..1040
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1052..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1090..1110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..170
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1140 AA; 125812 MW; C5CB3209C2482623 CRC64;
MDSGEPVVES LARLPDEDAV LGTRAVAFPD DHGEIIEEKL QHWHGRPRGV EMKREMTKED
KELAAAGYEH LDEQKMKKGS DQLDDVDIFE HQLSFHELGS ALDTTFDSKD PGQSYGLSTE
EAKARLARDG PNVLTPPKKK SALRMYIDLL LTMFNILLIF AGVLEYILLG IDFKDNFANT
YLGGILIAVA FLNAFIEFFQ LQKSEAILAS FLAMIPPSCH VVRDGAITQV PAADLVKGDI
VLLRTGDKTP ADLILFAATD LKVDNSNLTG ESEAQERLEK PEGSKARPVE AENLVFNSTL
IVNGEGWGVV VRTGDHTLIG QIAALTGGEM GNKSPLAVEI ARFVMMVSGI AIIFAVVFFV
VGITTVYKGK GAETVTFAVS ILVAFVPEGL PSVVTLLLSI AAKRMAAQNL TLLATDKTGT
LTRNQMTVTN LWSGEKMYTA FQSNNDSETT EAFSINAPGM HEMVDIAALN SRVKFDKTDV
PFDQRTILGD ATETGLTRFA GRYIPDYDAL HKQHPKVFEI PFNSSNKWAL VILHKPHAAG
PLTLYIKGAP ERVLAKCSTY LKDGSIEPIT DDFKNAYDEA YNYMASRGHR VIACAQKLLP
ADQYDYSYQF SKNDGQYPSS EYCFCGLISL EDPPKHGVRE AIGTLRLAGI KVMMVTGDHP
KTAEAIARKI NLILGDTKET LSAKTGRPIE EIYEDEVDAV VVHGDEIDGL QGWQWDQIFA
KKEIVFARTS PQHKLEIVKH AQALGHIVGV TGDGVNDSPA LKRADLGIAM NVSGSDVSKE
AANMILLDDN FASTVKGVAE GRQIFVNLKR SIQYTISHST PEVIPQLLYV VGPIPLPLSA
ILILVIDLGF ELFVALSFAW DKPETKDGLM RMAPRKPVNE RSIMSLKKRA LKRTKTLRRD
TETQEVIQPS KISAWASSVK APFQRQWWED AMERTDDEGL VDSKLLSYSY LEAGVIEMIG
ALVAYFVVFY KNGFSPSDLR DAQSSSTAYF TKSSPDFMNG RGQLIDAAQQ VEALAKAQSI
VYLSIFIIQC FNVYAVKARF SFPFGRSIIG NYYNFLGILG GACLGIFIIY TPPLHVVFGG
TYHLSPLYWL IPMAFGCVLL LWASIRVLLL RKGIEQSRVK DIKGLMMFPT MRTLSMRSKH
//
