(data stored in SCRATCH zone)

SWISSPROT: Q4WD68_ASPFU

ID   Q4WD68_ASPFU            Unreviewed;      1060 AA.
AC   Q4WD68;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 123.
DE   SubName: Full=Sodium P-type ATPase, putative {ECO:0000313|EMBL:EAL85670.1};
DE            EC=3.6.3.7 {ECO:0000313|EMBL:EAL85670.1};
GN   ORFNames=AFUA_6G03690 {ECO:0000313|EMBL:EAL85670.1};
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:EAL85670.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85670.1, 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   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. {ECO:0000256|SAAS:SAAS00832166}.
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:EAL85670.1}.
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DR   EMBL; AAHF01000012; EAL85670.1; -; Genomic_DNA.
DR   RefSeq; XP_747708.1; XM_742615.1.
DR   STRING; 746128.CADAFUBP00009196; -.
DR   EnsemblFungi; EAL85670; EAL85670; AFUA_6G03690.
DR   GeneID; 3505061; -.
DR   KEGG; afm:AFUA_6G03690; -.
DR   EuPathDB; FungiDB:Afu6g03690; -.
DR   HOGENOM; HOG000265621; -.
DR   InParanoid; Q4WD68; -.
DR   KO; K01536; -.
DR   OMA; EMIFTKG; -.
DR   OrthoDB; 100699at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008553; F:proton-exporting ATPase activity, phosphorylative mechanism; IBA:GO_Central.
DR   CDD; cd02086; P-type_ATPase_Na_ENA; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006414; P-type_ATPase_IID.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   SMART; SM00831; Cation_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; TIGR01523; ATPase-IID_K-Na; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WD68.
DR   SWISS-2DPAGE; Q4WD68.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00832164};
KW   Hydrolase {ECO:0000313|EMBL:EAL85670.1};
KW   Membrane {ECO:0000256|SAAS:SAAS00832173, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00832168};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Translocase {ECO:0000256|SAAS:SAAS01237809};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00832175, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00832181,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        72..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        784..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        821..841
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        861..888
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        908..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        959..980
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        992..1011
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..92
FT                   /note="Cation_ATPase_N"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          404..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  116447 MW;  3FEFDBEBBAB6CDAD CRC64;
     MGAQKKQSSD NSQALSQPAH ALRYEDVLRE LAVDPDQGLT VGEAKRRLQQ YGPNELEGGE
     GVSIVKIVIR QIANAMMLVL IIAMAVSFGI QSWIEGGVIG AVIGLNIVVG VYQDYAAEKT
     MDSLRSLSSP TGTVTRDGKT STIPANEIVP GDMIELKVGD TVPADLRLVD AMNFETDEAL
     LTGESLPVQK EVDTTFDPDT GPGDRLNIAY SSSTVTRGRA RGVVISTGMQ TEIGAIAAAL
     RASDSKRRPV KRGPEGETKK RWYVQAWTLT CTDAVGRFLG INVGTPLQRK LSKLALALFA
     IAIIFAIIVM GVNGFRNDKE VIIYAVATGL AMIPACLVVV LTITMAVGTK QMVERHVIVR
     KLDSLEALGA VTNICSDKTG TLTQGRMVAK RAWIPSVGTF SVGSSNNPLN PEEGDLSLLP
     DPPVKVGPDA HGEPSRPEDL LKDNPLLEQY LNVAAMANLA HVHRSEHNEW QARGEPTDIA
     IQVFASRFNW GRDRWTKGEK PVWRQKAEYP FDSTVKKMSV IFKNTNDDRE MIFTKGAVER
     VIEACTTVTW TAGSDPIALD ENIKEEILQN MEALAKEGLR VLCLACRENH NPVKGEVVPA
     REEVEKDLTF CGLIGLYDPP RPETAGAIDE CYRAGISVHM VTGDHPGTAR AIAAQVGIIP
     ANMDSLAKDV ADAMVMTASQ FDKLTDEEID ALPTLPAVIA RCAPNTKVRM IDALHRRGRF
     AAMTGDGVND SPSLKRADVG IAMGQSGSDV AKDASELVLT DDNFASIING IEEGRRIFDN
     IQKFVLHLLA ENVGLALTLL IGLCFKDDNG QSVFPIAPVE ILWIIMITSG LPDMGLGMEI
     AAPDIMDRPP QSKQGIFTWE VIVDTMVYGV WMAALCLASF SLVLFGWGDG NLASGCNSDY
     SPECDGVFRA RATTFVCMTW FALFLAWEMI DMRRSFFRMQ PNSKRYFTQW MFDVWRNKFL
     FSGIMIGFVT TFPILYIPVI NDVVFKHVGI SWEWGVVFVE AILFFAGCEA WKWCKRIYFR
     HTSQKETGRE RVLRDFSRYT TMSRSETQAT GDLNVEKSMV
//

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