ID A0A550C389_9AGAR Unreviewed; 1338 AA.
AC A0A550C389;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=BD626DRAFT_508757 {ECO:0000313|EMBL:TRM59263.1};
OS Auriculariopsis ampla.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Auriculariopsis.
OX NCBI_TaxID=97359 {ECO:0000313|EMBL:TRM59263.1, ECO:0000313|Proteomes:UP000320762};
RN [1] {ECO:0000313|EMBL:TRM59263.1, ECO:0000313|Proteomes:UP000320762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL-1724 {ECO:0000313|EMBL:TRM59263.1,
RC ECO:0000313|Proteomes:UP000320762};
RX PubMed=31257601;
RA Almasi E., Sahu N., Krizsan K., Balint B., Kovacs G.M., Kiss B.,
RA Cseklye J., Drula E., Henrissat B., Nagy I., Chovatia M., Adam C.,
RA LaButti K., Lipzen A., Riley R., Grigoriev I.V., Nagy L.G.;
RT "Comparative genomics reveals unique wood-decay strategies and fruiting
RT body development in the Schizophyllaceae.";
RL New Phytol. 0:0-0(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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:TRM59263.1}.
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DR EMBL; VDMD01000029; TRM59263.1; -; Genomic_DNA.
DR STRING; 97359.A0A550C389; -.
DR Proteomes; UP000320762; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF153; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000320762};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 80..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 103..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 348..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1010..1027
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1057..1079
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1091..1112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1119..1137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1157..1179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 53..109
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 943..1189
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1210..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 150572 MW; 84433D3CADA9082A CRC64;
MSKQSNTLSV WRERLSIERL FGPKQRRVEP RTVFVHEALP KDFHDHRGRV LKQHVYTPNQ
IISSKYTLIT FLPRNLLEQF RRIANLFFLG IAIIQFFPEF STITPIVAIL PLIIIVVVTA
LKDGYEDYKR HVSDRSVNQS KVTVLSGGDW TNPNAMKRKQ KTFVRRLIPN QLPGRKRRDL
EGAVDDPHVP HWKTELWEDV RVGDFVKITD GEAIPADVLI CSTSEDGNVA YVETKNLDGE
TNLKSRNAVA SLTHIRTAED CANPENKFSV ECDRPDMNMY RINAAVSQWG MKSAVDLANV
LLRGTVLKNT EWAVGVVLFT GVDTKIVLNA GLTPSKRSKI ERQMNSQVLI NLALLGVMSV
VCGIVDSVLE QKYYPLGAPW LYGDDQNDDN PSINGLITWA FALLTFQIII PISLYISLEV
VRTLQAAWIY LDDDIRHGPT GQRTVARSWN LADDLGQIEY IFSDKTGTLT QNVMVFRECT
IGGRCYTGDE DTEVNEPIAA AKLSSSSEAL PKLKTNIPHF KDAVLQSDLD AAFSDKPDPA
DAAHARMLNG FLSCLSLCHT VIAAHDKETD QIEYKAQSPD EAALVQAAAD IGYIFLGQEK
GVLTLQTPSS IERYELLNVL EFTSARKRMS VVLRKLDDDD GRLFLFTKGA DNVIFERLRP
GADDMKTTTE DHLSEFARHG LRTLTLAYKV IREEDYVAWS DRYHNASVAM EEREEKIEAV
CEELETDLRL LGATAVEDRL QDEVPETIAD LKRGGIKIWV ATGDKLETAI AIGRSTNLIG
EESNIIVVRG GNPNGRPVRQ QMHAAIETFF PGQVNDEERS ELEKTGEAGM PPLRRINTGV
SSIVGPENGD RPGGFILVID GSALHDAFAD QENSATLLRL AMLCEGVICC RVSPRQKAQI
VRLVKDGLGV MCLAIGDGAN DVSMIQAADI GVGISGEEGR QAVNSSDYAI AQFRFLKRLL
LVHGHWSYAR ISKMILTFFY KNIMPVGVLW WFQIYSAWSG YYVFDYEYVL FYNSIWTVLS
CPAIGLFDRI ADDRDLMELP ELYKYGRLGT WFSYKNFFIY MLDGIYQSVI VFFFVLYSYV
STSAREDGYT IGLYEMSTTM IMAIVLIVNF YIGFSATAWT WWLLFGIFVG TVIVWAFTAI
YSSLAPQNTV TNLYGNYYFL FHSAIFWFCL PLTFCLSFAP RYLSRAWKVG FGKLDDLEMV
NVIRKTDPHH SLKLGPSSED RDSSEIEMER LKRRQSRPRS MMSTASSMSR LSRPATAMAS
RTDMSTGIVS VDRGFDFAAE EPGPAIRRIQ TNLSERRSSR LGLQSGLGEH DRQRQHKTSL
RDGLHNLTRG LTRKRGTH
//
