ID R9AI40_WALI9 Unreviewed; 2497 AA.
AC R9AI40;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=P-type phospholipid transporter {ECO:0000256|ARBA:ARBA00012189};
DE EC=7.6.2.1 {ECO:0000256|ARBA:ARBA00012189};
GN ORFNames=J056_003560 {ECO:0000313|EMBL:EOR01884.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR01884.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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 -!- 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}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109}.
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DR EMBL; KE007228; EOR01884.1; -; Genomic_DNA.
DR RefSeq; XP_009267051.1; XM_009268776.1.
DR STRING; 1299270.R9AI40; -.
DR GeneID; 20376512; -.
DR KEGG; wic:J056_003560; -.
DR eggNOG; KOG0206; Eukaryota.
DR eggNOG; KOG4269; Eukaryota.
DR HOGENOM; CLU_000846_3_0_1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000014064; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 2.
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; PF00169; PH; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064};
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 1080..1098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1445..1466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1493..1513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2142..2162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2174..2195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2225..2247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2259..2280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2287..2312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2332..2352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 163..292
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 300..415
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 603..827
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 348..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1975..2008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2395..2429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2446..2497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..812
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1991..2007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2460..2474
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2479..2497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2497 AA; 280618 MW; 3C10AB8125E0980D CRC64;
MASPLTLQDI LDLKGEDPLL FLLNERNTLA SQNNQLWNLI DRQKSTINKL NVELDTLPHE
QQQHSQPTHH LALSKKSHSH DDAINLPIKP AMLSAMEKAQ LSQQHKSKSS PYMQHASHSF
NTLPQARSHY QHLSPKQPAI TPSVKTAAPP VPVFKLTPTL VPALQLAVLS SSVKPNKDNK
SVYSFTITVK YEPSNAEWKV DKSYDSIHAL DIKVREIIKK PYFKHTKGRL VSLPDKSIFK
DRSPSKVLQQ KTQLENYFHS IISIPHTYTI IPKNSATPHM ELAAFLSSDF VRPNQASQIN
GTKDGYLTKK GKNLGGWKTR YFTIGREGIL DYYEQRGGSQ IGSIRIHDAS IGRQHPSRAS
SDSSSANERD SAFKHAFLIL ERHQATQNEK DRHILCAEND LERDNWINTL LWHQRTHSNV
GGASSPVLHE RTNIAEDSTP NSANNGLKRR ATSLKTRSLE THKLKDVERP RTSDSKPISK
EEIQPSNSVS LTSLPPEVSS KFSIPKVLAD ARNTGKVDAL GISQHGESAN LLPQRQGSIH
SLSGQYKAVG AKLNESCESI DKSEKQHERD HKGKSRGFWG AFSGSSSGSS KDKSAPKLPV
FGVPVDDSLQ QAQIAGLPAV VFRCIRYLQH VKAEEEEGIY RLSGSSTQVK GLKERYNSEG
DIDLIESDDV FDPHAITGLL KLYFRELPVS LLTRELHFQF LQVADIPDPK KRVRELGRLV
SLLPIANYAL LRALVSHLTD VVSSEEINRM SLRNVSIVFS PTLGIPAPLF GLLLTEFKYV
FNVGDGGKPV PLEDQSTEEE DNDNDNDDDN DHVDNVDSIA ESLAESFVST AKPSFETTPT
EIMEDETVDV VMPAPKVNTE RKRPPAPLKI PPLNAPISAP LNRTFSPPIT TPTTPARPSR
HRRKNRNSAL YEDVDIDSIL GLRPKNIHAH EMNNDRNSSS KQDNKMTFED SDVDPAMPSE
RLPTSTPTKP GIFQKWDEFS IEKMFASKKR KPLPRSVYLN SPLPHESTLG KKTWTEKLLH
PRSTHHVGPG WVYTTNQIIS SKYTILTFVP RNILEQFRRV ANLFFLGIAI LQFFPKFSTI
NAGVVILPLI IIVFITACKD GYEDIKRHQS DRKVNHSKVK VLKGKYGESR HSDYHYHNFN
HIEAKSKTFT GGLPKGAMLG KLRLKKKSKN RDHVPPPNLP DAVTSLDDEL KFESDQMGRH
SVGNPPELND TGEFNGRQVG LVDDLENPRT YTPPPPPAQL PAGPIPENDA EEVEEGEEDD
GQDDAGNSWR TMLWEDVKVG DFVKIHNNEP FPAGERRVQE SISTLLIRVL DIVVCSTSEE
EDVCFVETKN LDGETNLKSR HAIPQLSHLT SPAAIARECH GYRIDSEPAD VNMFRLNAAV
VKEDQQPVKC PVDMSTMLLR GTVLRNTKWV IGVVLFTGSD TKIIANSGIT PSKRAKTERL
MDPQVGFNLA LLAIISAICA IVAYTIEVDD QRNGAYWTYN DDRPDDNPST NGVFTFFNGL
ITFQNIVPIS LYISMEFVRT CQAGWIYLDK EMRYKKNGYR TVARSWNLSD ELGQIQYIFS
DKTGTLTQNA MIFRQCSIAG KVYKADENTV VESKLSIGHS PDIPASIVDS VTPLNQTKAG
SEFNSSDGHE PHVNKHTTTR GENPQETEEV PKFFSSVLQE DIRGGVNEEA EKKSQDTDAF
LTCLSLCHTA LAAEKEDGTL EYKAQSPDES ALVQGAADIG YVFKGRDRNI LKLQTPFTGD
GMDHYELLNV LEFSSARKRM SVVIRKLSPK RAQMKIDMAN NVARGERNPK IALDDDDEEE
SEIILLTKGA DNIIFERCEA NVHNQGMKDA TDKDLSLFAS EGLRTLCLGY RVVPTEVYEE
FSKEYNDATV SLEDRENLIE AVASKFETNL TLLGATAIED KLQDGVPETI RDLKRAGIKV
WVATGDKLET AIAIGYSTQL LTDDNNLIIV RGGEYGDRNS AYSQMRRAME QFFPGENIPS
RLRNQPPDNH YDGGSKRSST QSHAMSDMES LVGADNGQRD GGYALVIDGT ALTHALSEPW
SKDLLLNLAL KCQSVVCCRV SPLQKALVVR LIKDNLDTMT LAIGDGANDV SMIQAAHVGI
GIAGEEGLQA VNSSDYAIAQ FRYLKKLLLV HGHWYYYRNS NAILSFWIKN INGAAVLFWY
QFYCAFSTSY VYAYIYLLLW NVLWTICPPI GLGLFDSVLS DRVLMAIPEL YKYGRTAQYF
NHRLFFLYVF EAIVQSTIVF FFTYYAYQSP TARSDGFDVY IYEMSTTMIV SIVTGTNLLI
SLNARSWNWW IAFGMFFGIV LVWAFTGVYS ALSPQLVWTN VWGNDYFVFH SPLFWFCVIF
TVIFSLIPRY LFKAYKFQFH PDDIHIMQYV QKKDDNHDFE NDPLMQSHLQ NAYYEDSEYP
PNRPSSARSG QRIDMRTGER SSGRNATFNF DQEENGYALQ RLQSHLSETS SQFHRRPSTH
DAQARKRKLK RKSKNWTSRT VDSFKTAMPT MRKTKNS
//
