ID A0A1B8ATM5_FUSPO Unreviewed; 1525 AA.
AC A0A1B8ATM5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=FPOA_04262 {ECO:0000313|EMBL:OBS23714.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS23714.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS23714.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS23714.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) 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:OBS23714.1}.
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DR EMBL; LYXU01000002; OBS23714.1; -; Genomic_DNA.
DR STRING; 36050.A0A1B8ATM5; -.
DR OMA; QALRCGR; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000091967; 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; 1.
DR PANTHER; PTHR24092:SF150; 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; SFLDS00003; Haloacid_Dehalogenase; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000091967};
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 143..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 513..538
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 558..581
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1143..1159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1171..1192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1222..1243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1263..1281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1288..1308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1328..1348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 113..165
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1108..1357
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 880..907
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1525 AA; 172241 MW; A7775A4BCFE7CA0C CRC64;
MTTTTADGHL APDDSQHLSA TQRSRWATQR KSVNSSNNKR NSLLERMGHK KTGSNEKNPP
SDGSDPAGDD GQPPEANPNN EDHAEEEEEH ENRILYFNQP LPAELLDETG TPSQTFTRNK
IRTAKYTPLS FVPKNLWFQF HNVANIFFLF LVILVIFPIF GGVNPGLNAV PLIFIIAVTA
IKDAIEDYRR TVLDIELNNA PVHRLRNWNN VNVLEGDVST WRQFKKANSK FFGAIWRACQ
SVWSKKAKEE RAKRKAAPTD NDAPRPSVET QRTRQSMRQS IASPFSGRES FMSAREDIQM
TPVPSPSPQA TPHAHFEMPD EQDAKRAAAL MQMKSDVINY HHPASGARFQ KDTWKSLNVG
DFVRIYNDEE LPADVIILST SDPDGACYVE TKNLDGETNL KVRQAVRCGR SLKHARDCER
AEFIVESEGP QPNLYKYNGA IKWKQPVPGY LDDEPEDMTE PITIDNLLLR GCNLRNTEWI
VGVVIYTGHD TKIMMNAGIT PSKRARIARE MNFNVVCNFG ILLIMCLLAA IINGVAWAKT
DASLHFFEFG SIGGKPAMSG FITFWAAIIL FQNLVPISLY ITLEIVRTLQ AVFIYNDVEM
YYEPIDQPCI PKSWNISDDV GQIEYIFSDK TGTLTQNVME FKKATINGQP YGEAYTEAQA
GMQKRLGIDV EKEGERVRAE IADAKVRALA GLRNIHDNPF LHDDALTFIA PDFVSDLAGE
SGPAQKDANE FFMLALALCH TVMAEKVDGD SPKMIFKAQS PDEEALVATA RDMGFTVLGS
SGEGINLNVM GEDRHYQILN TIEFNSSRKR MSSIVRMPDG RIILFCKGAD SIIYSRLKRG
EQKELRQTTA EHLEMFAREG LRTLCIAWKE VTEQDYRVWK KEHDAAASAL EEREEKLETV
AELIEQDLYL VGGTAIEDRL QDGVPDTIAL LGNAGIKLWV LTGDKVETAI NIGFSCNLLN
NDMELIHLKV DEDESGEITD EAFFEMAEKL LDDNLQIFGI TGNDHDLALA KKNHEPPAPT
HGLVIDGFTL RWVLNDRLKQ KFLLLCKQCK SVLCCRVSPA QKAAVVAMVK NGLDVMTLSI
GDGANDVAMI QEADVGVGIA GVEGRQAAMS SDYAIAQFRF LSRLVLVHGR WSYRRLAESI
SNFFYKNMVW TFGIFWYEIY CDMDMTYLFD YTYILMFNLF FTSIPVAIMG VLDQDVSDKV
SLAVPQLYRR GIERLEWTQL KFWLYMIDGV YQSIMVFFIP YLLFMPGTFL TMNGLGLEDR
LRFGAYVAHP AVITINMYIL INTYRWDWLM VLIVVISDVF IFFWTGVYTS FTSSVYFYGT
AAQVYGEATF WACFFLVPVI CLFPRFAIKA LQKVYWPYDV DIIREQERMG QFAHLYQTDE
TSDPPTADTK SDKSKSSKSS RRSKKMPKHV AYGSVDEDLR PIYPPSTATR TTTYNQHSQN
GSDSTNYTAH RISLDVPMQA RPSIERARPS YDRMRASMDR VRPSFEASND FTSAARLSRI
ESSQSQAGRF HPRLRGLSLT KSANI
//
