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Database: UniProt
Entry: B0WE67_CULQU
LinkDB: B0WE67_CULQU
Original site: B0WE67_CULQU 
ID   B0WE67_CULQU            Unreviewed;      2311 AA.
AC   B0WE67;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   05-JUN-2019, entry version 83.
DE   SubName: Full=Acetyl-coa carboxylase {ECO:0000313|EMBL:EDS45294.1, ECO:0000313|VectorBase:CPIJ005524-PA};
GN   Name=6037039 {ECO:0000313|VectorBase:CPIJ005524-PA};
GN   ORFNames=CpipJ_CPIJ005524 {ECO:0000313|EMBL:EDS45294.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176 {ECO:0000313|Proteomes:UP000002320};
RN   [1] {ECO:0000313|Proteomes:UP000002320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|Proteomes:UP000002320};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA   Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J.,
RA   Mauceli E., Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L.,
RA   Amedeo P., Antoine C.H., Arensburger P., Bidwell S.L., Crawford M.,
RA   Camaro F., Devon K., Engels R., Hammond M., Howarth C., Koehrsen M.,
RA   Lawson D., Montgomery P., Nene V., Nusbaum C., Puiu D.,
RA   Romero-Severson J., Severson D.W., Shumway M., Sisk P., Stolte C.,
RA   Zeng Q., Eisenstadt E., Fraser-Liggett C.M., Strausberg R.,
RA   Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS45294.1, ECO:0000313|VectorBase:CPIJ005524-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS45294.1,
RC   ECO:0000313|VectorBase:CPIJ005524-PA};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|VectorBase:CPIJ005524-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|VectorBase:CPIJ005524-PA};
RG   VectorBase;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|SAAS:SAAS00197451};
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DR   EMBL; DS231905; EDS45294.1; -; Genomic_DNA.
DR   RefSeq; XP_001847001.1; XM_001846949.1.
DR   STRING; 7176.CPIJ005524-PA; -.
DR   EnsemblMetazoa; CPIJ005524-RA; CPIJ005524-PA; CPIJ005524.
DR   GeneID; 6037039; -.
DR   KEGG; cqu:CpipJ_CPIJ005524; -.
DR   VectorBase; CPIJ005524-RA; CPIJ005524-PA; CPIJ005524.
DR   eggNOG; KOG0368; Eukaryota.
DR   eggNOG; COG0439; LUCA.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG4799; LUCA.
DR   HOGENOM; HOG000214115; -.
DR   InParanoid; B0WE67; -.
DR   KO; K11262; -.
DR   OMA; LPYGEWN; -.
DR   OrthoDB; 156081at2759; -.
DR   PhylomeDB; B0WE67; -.
DR   Proteomes; UP000002320; Partially assembled WGS sequence.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234148};
KW   Biotin {ECO:0000256|SAAS:SAAS00296904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002320};
KW   Ligase {ECO:0000256|SAAS:SAAS00232059};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320}.
FT   DOMAIN       92    588       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      241    436       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      715    789       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN     1538   1876       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000259|PROSITE:PS50980}.
FT   DOMAIN     1880   2196       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000259|PROSITE:PS50989}.
FT   REGION       25     67       Disordered. {ECO:0000256|MobiDB-lite:
FT                                B0WE67}.
FT   COMPBIAS     37     65       Polar. {ECO:0000256|MobiDB-lite:B0WE67}.
SQ   SEQUENCE   2311 AA;  259788 MW;  F9442C808FFD66FE CRC64;
     MKEKIEKGRK TGSKVLDAIL CRSGSRQSPL VDGGGGSAAP STSSAVESAE TQTSPRPSMS
     HGTGLGQERY QERDFVLSTT EEFVKKFNGT RAITKILIAN NGIAAVKCMR SVRRWSYEMF
     KNERAVRFVV MVTPEDLKAN AEYIKMADHY VPVPGGSNNN NYANVELIVD IALRTQVQAV
     WAGWGHASEN PKLPELLHKK GLVFLGPPER AMWALGDKVA SSIVAQTAEI PTLPWSGSEL
     KAQYSGKKIK ISSDLFARGC VTTSEHGLVA AAKIGYPVMI KASEGGGGKG IRRVDCADEF
     PALFRQVQAE VPGSPIFVMK LARGARHLEV QLLADQYGNA ISLFGRDCSI QRRHQKIIEE
     APAIIAEPEV FEDMEKAAVR LAKMVGYVSA GTVEYLYDAE GRYFFLELNP RLQVEHPCTE
     MVAEVNLPAC QLQIGMGIPL YRIKDIRLLY GENPWGSSVI DFDNPNNKPR PRGHVIAARI
     TSENPDEGFK PSSGTVQELN FRSSQNVWGY FSVAASGGLH EFADSQFGHC FSWGENRQMA
     RENLVIALKE LSIRGDFRTT VEYLITLLET NSFLENTIDT AWLDALIAER VQSDKPDIIL
     GVICGALHIA DRKITDAFTS FQTSMEKGQI QAANTLTNVV DVELINESIR YKVQAAKSGL
     NTYFLVMNGS FKEVEVHRLS DGGMLISLDG SSYTTYMKEE VDRYRIVIGN QTCVFDKEND
     PSVLRSPSAG KLINLLIEDG AHVNKGQPFA EIEVMKMVMT LTAGETGSIS FVRRPGAVLD
     AGSLLGHLEL DDPSLVTKAQ PYKNPWPLTG DSVQMPEKLN RVHSSYKMIL ENTLAGYCLP
     DPYNAPRLRE IIEKFMQSLR DPSLPLLELQ EVIASISGRI PLSVEKKIRK LMQLYERNIT
     SVLAQFPSQQ IASVIDMHAA TLQKRTDRDV FFLTTQGIVQ LVQRYRNGIR GRMKAAVHEL
     LRQYYAVESQ FQHGHYDKCV AAIRDKHKDN MDVVVGTIFS HSQVAKKNLL VTLLIDHLWA
     NEPGLTDELA ATLSELTSLN RAEHSRVALR ARQVLIAAHQ PAYELRHNQM ESIFLSAVDM
     YGHDFHPENL QRLILSETSI FDILHDFFYH SNRAVCNAAL EVYVRRAYTS YDLTCLQHLE
     LSGEVPLVHF QFLLPTAHPN RYKLLPDGTE SDNLTDSFMR TGCMAAFDSY EHFTQYSDEI
     LDLLEDMAST AFVNPKMLEA VEAGDSDRRM STSINVSISE QVSGASVVST EGAVAPHPAE
     AIHILSIAVR DMGDMDDLQM EAVFGAFCAQ HREELLSRRV RRITFAALKK RQFPKFFTYR
     ARDNFEEDRI YRHLEPACAF QLELNRMRTY DLEALPTANQ KMHLYLGRAK VPKGQEVTDF
     RFFIRSIIRH SDLITKEASF EYLQNEGERV LLEAMDELEV AFSHPQAKRT DCNHIFLNFV
     PTVIMDPAKI EESVTKMVLR YGPRLWKLRV LQAELKMVIR QNTQSPTTSV RLCIANDSGY
     FLDIAMYTEV TDPETHVIKF QAYGSRQGPL HMLPISSPYM TKDYLQQKRF QAQSNGTTYV
     YDIPDMFRQM TERLWKEFSK ARPTEDIRIP EKILLVCNEL VLKGDTLEEI QRLPGENNVG
     MVAWRIVLAT PEFPEGREIV VIANDLTYFI GSFGPQEDLL FYKASELSRQ RKCPRIYISV
     NSGARIGLAE EVKSLFKIAW EDPDEPEKGF KYLYLTTEDY SKIANTNSVR AILIEDEGEQ
     RYKITDIIGK TDGLGVENLR NAGMIAGETS RAYEDVVTIS MVTCRTIGIG SYLVRLGQRV
     IQIENSHIIL TGFSALNKLL GRKVYASNNQ LGGIQIMHNN GVTHKTEALD LDGVYTILYW
     LSYIPDVRGG TLPIVTASDP IERPIDFMPT KAPYDPRWML AGRVNPANPS EWETGFFDRG
     TWSEIMEPWA QTVVVGRAKL GGIPVGVIAV ETRTVELTIP ADPANLDSEA KTFQQAGQVW
     FPDSSYKTAQ AIKDFGREEL PLIILANWRG FSGGQKDMYE QIVKFGAYIV DGLREYNQPV
     VVYLPPNAEL RGGAWAVLDP TINPRFMETY ADPESRAGVL EPEGIVEVKF KEKDILKAIY
     RLDPVVLDLK QKIANAGANK EAVTELENQL KTRVTALLHV YHTVAVHFAD LHDTPERMLE
     KGCISEIVPW RSSRSYFYWR LRRMLLEEHF IKQILSAQDS LAVGQAKEML RRWFVEDKGA
     TEAYLWENHN EPVVEWLEGQ KKSDSTVCRN IYAVKKDAIV SQIQKALEDC PEAALDAVIG
     LCQALSPAHR GEVVKTLSQL EFTEKEHASM G
//
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