ID A0A1V8TQM4_9PEZI Unreviewed; 1351 AA.
AC A0A1V8TQM4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=B0A48_01899 {ECO:0000313|EMBL:OQO13670.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO13670.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQO13670.1}.
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DR EMBL; NAJO01000003; OQO13670.1; -; Genomic_DNA.
DR STRING; 1507870.A0A1V8TQM4; -.
DR InParanoid; A0A1V8TQM4; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000192596; 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 CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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; 2.
DR PANTHER; PTHR24092:SF214; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 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:UP000192596};
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 493..514
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1094..1116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1137..1154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1174..1195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1202..1222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1234..1261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 228..294
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1023..1276
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1351 AA; 150948 MW; E7018B8F09877BFC CRC64;
MAQGGSRGHG GNDLLGLDDN AGPYYNSGQR APANDDDLLN EYDIDDTETR VSTSRDAFVG
GNSTAGLPGG PSRPGPQASV ESLQPPTMLG QAGRNYSQTS DLNNYQRYSD VDDNRSDAGG
YYAMGGNIDE DNVPGLPLNN KSKHRSRNSI LSLGGGMIGR VKNTLGMGPE YSEMDLPLTE
TPAGRGHAQS VGTESLPPRK RTTPGSKFKF GIPGRGKVDP STLGPRIIHL NNPPANATSK
YADNHVSTTK YNIATFLPKF LFEQFSKYAN LFFLFTAILQ QIPNLSPTNR WTTVVPLGIV
LLVSAAKEII EDNRRRSQDA QLNRSPTRVL RGSRFEDVKW IDVHVGDILR VESEESFPAD
IVLLASSEPE GLCYIETANL DGETNLKIKQ GIPETCNLVS SAELGRLGGR LRSEQPNSSL
YTYEATLTMQ TGGGEKELPL QPDQLLLRGA TLRNTPWIHG VVVFTGHETK LMRNATATPI
KRTAVERTVN MQILMLGGVL VALSVISSVG DLVIRNTSGD KLWYLLYPSI NGAQLFFSDI
FTYWILYSNL VPISLFVTVE IIKYYQAFLI SSDLDIYWDK TDTPANCRTS SLVEELGQVE
YIFSDKTGTL TCNQMDFRQC SIGGIQYAEE VPEDRKIIGE DDTGTGIYDF KGMEKHRRGG
ENAAQIHHFN TLLSTCHTVI PEIKADKPGV IKYQAASPDE GALVEGAVLL GYKFVARKPR
SVTIELEGQR YEYELLAVCE FNSTRKRMST IFRCPDGKIR CYCKGADTVI LERLGVRDDI
VEKTLLHLEE YAAEGLRTLC LAMREVPESE FREWWDVYNT AQTTVSGNRA EELDKAAELI
EHDFTLLGAT AIEDKLQDGV PDTIHTLQTA GIKVWVLTGD RQETAINIGM SCKLISEDMT
LLIINEENAS ATRANIEKKL EAIRSQHAGG IEMETLALVI DGKSLTYALE KDLEKQFLDL
AVMCKAVICC RVSPLQKALV VKLVKRHLKA ILLAIGDGAN DVSMIQAAHI GIGISGVEGL
QAARSADVSI AQFRFLRKLL LVHGSWSYQR ISKVILYFYY KNTALFITQF WYSFQNAFSG
QVIYESWTLS FFNVIFTALP SFVIGIFDQF VNARLLDRYP QLYQLSQKGV FFQTHNFWSW
VGNGFYHSVL LYFFSELIWR NDGILSDGTV AGHWVWGTAL YTAGLVTVLG KAALITNVWT
KYHVIAIPGS LGIWFIFLPL YATVAPRLGF STEYAGLLSI LLTSPTFWLM GCMVLPALCL
TRDFAWKYAK RMYYPQSYHH VQEIQKYNIQ DYRPRMEQFQ KAIRKVRQVQ RMRKQRGYAF
SQTDESQARV LQAYDTTKER GRYGEMTSSR R
//
