(data stored in ACNUC7421 zone)

SWISSPROT: Q4WD94_ASPFU

ID   Q4WD94_ASPFU            Unreviewed;      1277 AA.
AC   Q4WD94;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 122.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=AFUA_6G03950 {ECO:0000313|EMBL:EAL85644.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85644.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85644.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(2)O + phospholipid(Side 1) = ADP + phosphate +
CC         phospholipid(Side 2).; EC=7.6.2.1;
CC         Evidence={ECO:0000256|RuleBase:RU362033,
CC         ECO:0000256|SAAS:SAAS01189249};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362033}; Multi-
CC       pass membrane protein {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|RuleBase:RU362033,
CC       ECO:0000256|SAAS:SAAS00533978}.
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:EAL85644.1}.
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DR   EMBL; AAHF01000012; EAL85644.1; -; Genomic_DNA.
DR   RefSeq; XP_747682.1; XM_742589.1.
DR   STRING; 746128.CADAFUBP00009170; -.
DR   EnsemblFungi; EAL85644; EAL85644; AFUA_6G03950.
DR   GeneID; 3505047; -.
DR   KEGG; afm:AFUA_6G03950; -.
DR   EuPathDB; FungiDB:Afu6g03950; -.
DR   HOGENOM; HOG000201571; -.
DR   InParanoid; Q4WD94; -.
DR   KO; K01530; -.
DR   OMA; FSIEQFC; -.
DR   OrthoDB; 587717at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 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   PANTHER; PTHR24092; PTHR24092; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WD94.
DR   SWISS-2DPAGE; Q4WD94.
KW   ATP-binding {ECO:0000256|RuleBase:RU362033, ECO:0000256|SAAS:SAAS00311808};
KW   Hydrolase {ECO:0000313|EMBL:EAL85644.1};
KW   Magnesium {ECO:0000256|RuleBase:RU362033, ECO:0000256|SAAS:SAAS00311822};
KW   Membrane {ECO:0000256|RuleBase:RU362033, ECO:0000256|SAAS:SAAS00076974};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00311833};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Translocase {ECO:0000256|RuleBase:RU362033, ECO:0000256|SAAS:SAAS01101229};
KW   Transmembrane {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00311809};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00311798}.
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        518..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        550..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1100..1123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1153..1175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1196..1222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1242..1263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          181..232
FT                   /note="PhoLip_ATPase_N"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          1041..1269
FT                   /note="PhoLip_ATPase_C"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          1..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..50
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..95
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..383
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1277 AA;  141045 MW;  502DBF7EA4FADDF0 CRC64;
     MPSSSEYLHP HGRTSVAGDS GSDDDLDLEE LDPTTATIHK SPRLSKDEAT RQRGYGSGIA
     LRNLRVGGGS RGWKRSASGI RNRDSEEDTH GLLEDQEGGA LRSSHASSRN FTDDDAPLLD
     NPRRSSTRSF AGDGPVRRRG SQSRFFGFKA ANIFSGPSSW SHRNDENNAT KPPREVFVGQ
     SQRSKYPANI VSNAKYTPWS FLPRTLYNEF SFFFNIYFLL VALSQIIPVL RIGYMSSYIA
     PLAFVVSISL GKEALDDIGR RRRDAEANSE EFTVLSFDKP VGRRAFATPA NNYSDSDEVF
     EITKKSRDLK VGDVLKVRKN QRLPADVVIL KTISNDSVTA RRSSSAEVTA DLMRPDPESV
     QPSEVEPSSS AAADEIGTSS ASDTFIRTDQ LDGETDWKLR LPSVLSQSLR LRDFTRLKVT
     ASAPDKRVNE FLGTIELGSQ SGFYDPLVDK AQTGGEASSE DRQANSAPLT IDNTAWANTV
     LASNTITYAV IIYTGSQTRA ALSTSPSRSK VGLLEYEINN LTKILCALTL TLSIILVALE
     GFQPNNDKEW YIAIMIYLIL FSTIIPMSLR VNLDMAKSVY SRFIQRDKDI PGTVVRTSTI
     PEDLGRIEYL LSDKTGTLTQ NEMELKKIHV GTVSYANDAM EEVASFVRQA FAGNTLTTPS
     AAFGAQAGLG AAPRTRREIG SRVRDIVLAL ALCHNVTPTT DEEDGVKVTN YQASSPDEIA
     IVKYTEEVGL KLSYRDRQSI VLETTETGSV VVRVRILEIF PFTSDSKRMG IIVQFETANS
     ILESSNEDAE IWFYQKGADT VMSSIVAAND WLDEETANMA REGLRTLVIG RKRLSLQHFQ
     EFSAKYKQAS LALQGRDVGM AKVVSEHLER DLELLGVTGV EDRLQRDVKP SLELLRNAGV
     KIWMLTGDKV ETARCVAISA KLVARGQYIH TVAKVKDPSA AQEALDFLRN KTDCCLLIDG
     ESLSLMLGQF RSAFISVAVL LPAVVACRCS PTQKAEVAEL IRQYTKKRVC CIGDGGNDVS
     MIQAADVGIG IVGKEGRQAS LAADFSITHF HHLTKLLVWH GRNSYKRSAK LAQFIMHRGL
     IISACQTMYS IASHFDPKGL FINWLMVGYA TVYTNAPVFS LVFDRDVDEH LANLYPELYK
     ELKSGRSLSY RSFFGWVLVS VYQGAVIQGL SQILLNTISG PRLISVSFTA LVINELLMVA
     IAITTWHPVM IFCLIGTALV YAASVPFLGD YFDLEYVITV DWVWRVAAVC SVSVIPVWAA
     KLIQRSWKPP SYRKVRG
//

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