(data stored in ACNUC16935 zone)

SWISSPROT: Q5AS02_EMENI

ID   Q5AS02_EMENI            Unreviewed;      1466 AA.
AC   Q5AS02; C8VLI2;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 113.
DE   SubName: Full=ATP-binding cassette multidrug transporter [Source:UniProtKB/TrEMBLAcc:P78576] {ECO:0000313|EMBL:CBF84638.1};
GN   ORFNames=ANIA_08928 {ECO:0000313|EMBL:CBF84638.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF84638.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
CC       family. PDR (TC 3.A.1.205) subfamily.
CC       {ECO:0000256|SAAS:SAAS00709344}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00434}.
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DR   EMBL; BN001307; CBF84638.1; -; Genomic_DNA.
DR   RefSeq; XP_682197.1; XM_677105.1.
DR   STRING; 162425.CADANIAP00007936; -.
DR   EnsemblFungi; CADANIAT00007936; CADANIAP00007936; CADANIAG00007936.
DR   EnsemblFungi; EAA64062; EAA64062; AN8928.2.
DR   GeneID; 2868201; -.
DR   KEGG; ani:AN8928.2; -.
DR   HOGENOM; HOG000162078; -.
DR   OMA; IFYAFEI; -.
DR   OrthoDB; EOG092C1HKF; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
DR   GO; GO:0035690; P:cellular response to drug; IEP:AspGD.
DR   CDD; cd03233; ABCG_PDR_domain1; 1.
DR   CDD; cd03232; ABCG_PDR_domain2; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR029481; ABC_trans_N.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR034001; ABCG_PDR_1.
DR   InterPro; IPR034003; ABCG_PDR_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010929; PDR_CDR_ABC.
DR   Pfam; PF01061; ABC2_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF14510; ABC_trans_N; 1.
DR   Pfam; PF06422; PDR_CDR; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q5AS02.
DR   SWISS-2DPAGE; Q5AS02.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
KW   ECO:0000256|SAAS:SAAS00555301, ECO:0000313|EMBL:CBF84638.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
KW   Membrane {ECO:0000256|SAAS:SAAS00709359};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
KW   ECO:0000256|SAAS:SAAS00555311};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Repeat {ECO:0000256|SAAS:SAAS00709352};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00709342};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00709353};
KW   Transport {ECO:0000256|SAAS:SAAS00709346}.
FT   NP_BIND     865    872       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   1466 AA;  162817 MW;  8A11334F185D1FA3 CRC64;
     MGVPDELPPG SSETDTIVSS SQPTNRSPMD LISEAESLNL RRIATNQSKA QCRPGSAAVP
     SHDNPPNDDL EDATLDPNSA SFSLEKWLRA AVSDASQHGL STPSGGILFR NLTVSGSGSA
     LQLQPTVGSV LTAPLRFASL LRHRRIEPRR ILHGFDGVMK TGELLLVLGR PGAGCSTFLK
     TVCGETNGLH IDADSVLHYN GVSQQRMMKE FKGEVVYNQE VDKHFPHLTV RQTLEFAAAA
     RTPAHRFQNM SRDEFASYAA SVVMAIFGLS HTHNTKVGND FVRGVSGGER KRVSIAEMAL
     AMTPFAAWDN SSRGLDSATA LKFVQALRLS ADLAGAAHAV AIYQASQSIY EVFDKVTVLY
     EGRMIFFGPT GTAKEYFERM GWVCPARQTT GDFLTSITNP LERKARAGME DVVPKTPKDF
     EIYWRQSPEY KTLLGEMTEF ETQHPTGNDE QASAELRARK ENSQSRNSRA ASPYILSIPM
     QIKLNTKRAY QRIWNDMSST MSTVVGQIVI ALITGSVFYD SPNTTAGFQS KGGTLFYAVL
     LNALTAMSEI TSLYSQRPIV EKQASYAFYH PATEAIAGVV SDVPVKFLLA VAFNVIMYFL
     ANLRREPAQF FIYFLMSFTV MFVMSAVFRT MAAVTKNAAQ AMGLAGVLML ALVVYTGYVL
     PVPSMHPWFE WIHYLNPIYY AFEAMIANEF HGRDFDCIAF VPSYADLDGD SFSCSSLGSV
     AGERMVSGDS YINFNYTYTY SHVWRNFGVL LAFLIGFMAI YFLASELNSS TTSTAEALVF
     RRGHVPEYMR PGYTRPTDEE KAVTQSDIKP SSPSPTNTDL PLPPQRDIFT WKDISYDIEI
     KGEPRRLLDD VSGWVKPGTL TALMGVSGAG KTTLLDVLAH RTTMGVITGD MFVNGKGLDA
     SFQRKTGYVQ QQDLHLETAT VRESLRFSAL LRQPASVSIR EKHDYVESVI EMLGMGDFAE
     AVVGTPGEGL NVEQRKLLTI GVELAAKPKL LLFLDEPTSG LDSQSSWAIC TFLRKLADSG
     QAVLCTIHQP SAILFQEFDQ LLFLAKGGKT VYFGPIGPNS RTLLDYFESN GARKCDEAEN
     PAEYMIEVVN AEVNDRGTDW FDVWKGSKEC QAVKEEIERI HEKKRGTAGA IEETDDGSTK
     SEFAMPFWFQ LYVVTVRVFQ QYWRMPEYII SKGALAIVAG LFIGFSFYDA KTSLAGLQTL
     VFSLFMVCAL FAPLVNQIMP LFITQRSLYE VRERPSKAYS WKAFLIANIL VEIPYQVLMG
     ILTFVCYYYP VVGSSQGPDR EGLVLLFCIQ FYVYASTFAH MCIAAMPNAE TASPIVILLF
     SMCLTFCGVM QPPDALPGFW IFMYRVSPFT YWVAGMATTQ VHGREVVCGE NELSIFDPPT
     NQTCGQYMER YISVAGGQVL NPSATAGCEY CSLTVADEYL AASQIYWSDR WRNFGLIWVY
     IGFNIFVATA VYYLFRVKKW NGRRKK
//

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