ID W7M8Y6_GIBM7 Unreviewed; 1340 AA.
AC W7M8Y6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=FVEG_05248 {ECO:0000313|EMBL:EWG44035.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG44035.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG44035.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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}.
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DR EMBL; DS022247; EWG44035.1; -; Genomic_DNA.
DR RefSeq; XP_018750226.1; XM_018893381.1.
DR GeneID; 30063257; -.
DR VEuPathDB; FungiDB:FVEG_05248; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000009096; Chromosome 3.
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: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:UP000009096};
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 298..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 498..520
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 552..573
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1066..1085
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1105..1127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1148..1170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1182..1201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1213..1236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1256..1275
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 235..301
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1034..1286
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1340 AA; 149572 MW; BE27C6F13B31A226 CRC64;
MAGRPPGGGF DTGQSNNRDD LLLDLDNDQP VYNGGQRSNL NDDDLMRFHE QNQDPPPGRT
SVSYDDFVGA RDANHASTAQ PAGGLGVPPR SGPGSTPYLT RQYSQTSELG NYQRYADDFD
DYPVEGDSYY HQDGGARVDE TTPGLGRNNA RNRNSVLGLG GGFIGKVKNR LGLGQGYSEM
DLPLTEPGHE RGDSVGGNSH QPTQQAQKGR FDMGNFKFGF GRSKPDPSTL GPRLIYLNNP
PANAANKYVD NHISTAKYNV ATFLPKFLYE QFSKFANIFF LFTAALQQIP NLSPTNPYTT
IAPLIVVLII SAVKELVEDY RRKQADNALN TSKARVLRGS TFQETKWINV AVGDIIRVES
EEPFPSDLVL LASSEPEGLC YIETANLDGE TNLKIKQGLP ETSSMVSPNE LSRLGGRIKS
EQPNSSLYTY EATLTMQTGG GEKEFALNPE QLLLRGATLR NTPWVHGVVV FTGHETKLMR
NATAAPIKRT KVERKLNMLV LLLVGILLVL SIVCTVGDLI QRKVEGDALS YLFLDPTNTA
GQITQTFLKD MVTYWVLFSA LVPISLFVTV ELVKYWHGIL INDDLDMYYD KNDTPATCRT
SSLVEELGMV EYVFSDKTGT LTCNQMEFKQ CSIAGIQYSE DVPEDRRPTM VDGVEVGLFD
YKALKSNLAN GHETAPAIDH FLSLLATCHT VIPEMDEKGG IKYQAASPDE GALVAGALDL
GFKFTARKPK SVIIDANGRE LEYELLAVCE FNSTRKRMST IYRCPDGKIR CYCKGADTVI
LERLNDQNPH VEVTLRHLEE YASEGLRTLC LAMREIPENE FQEWYKIYDT AQMTVGGNRA
EEVDKASEII EKDFFLLGAT AIEDRLQDGV PETIHTLQQA NIKVWVLTGD RQETAINIGM
SCKLLSEDMM LLIVNEETAA ATRDNIQKKM DAIRTQGDGT IETETLALII DGKSLTFALE
KDLEKLFLDL AIMCKAVICC RVSPLQKALV VKLVKKYQKE SILLAIGDGA NDVSMIQAAH
IGIGISGEEG LQAARSADVA IAQFRFLRKL LLVHGAWSYQ RVTKTILFSF YKNIALYMTQ
FWYTFQNVFS GQVIYESWTL SFYNVFYTVL PPLALGILDQ FISARLLDRY PQLYMMGQQN
YFFRFKVFTQ WIGNAIYHSI VLYIWAQLFW YGDLIQGDGK IAGHWVWGTA LYGATLLTVL
GKAALVTNNW TKYHVLAIPG SMAIWYVLTA VYGIVAPMAG VSMEYFGTIP RIYESPVFWL
QTVCLAIMCL LRDFVWKYAK RMYRPQTYHH IQEIQKYNIQ DYRPRLVDSS PRHGTPKTNV
FQNGAVSESN SESAASATHA
//
