ID Q75A67_ASHGO Unreviewed; 1819 AA.
AC Q75A67;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 2.
DT 01-MAY-2013, entry version 91.
DE SubName: Full=ADR051Cp;
GN ORFNames=AGOS_ADR051C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS Y-1056) (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient
RT Saccharomyces cerevisiae genome.";
RL Science 304:304-307(2004).
CC -!- SIMILARITY: Contains 1 biotin carboxylation domain.
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DR EMBL; AE016817; AAS51971.2; -; Genomic_DNA.
DR RefSeq; NP_984147.2; NM_209500.2.
DR ProteinModelPortal; Q75A67; -.
DR STRING; 33169.AGOS_ADR051C; -.
DR EnsemblFungi; AAS51971; AAS51971; AGOS_ADR051C.
DR GeneID; 4620296; -.
DR KEGG; ago:AGOS_ADR051C; -.
DR HOGENOM; HOG000251581; -.
DR KO; K14541; -.
DR OrthoDB; EOG4CVKG0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0043419; P:urea catabolic process; IEA:EnsemblFungi.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR003833; Allophan_hydro_1.
DR InterPro; IPR003778; Allophan_hydro_2.
DR InterPro; IPR014085; Allophanate_hydrolase.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR024946; Arg_repress_C-like.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR014084; Urea_COase.
DR Pfam; PF02682; AHS1; 1.
DR Pfam; PF02626; AHS2; 1.
DR Pfam; PF01425; Amidase; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00289; CPSase_L_chain; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF75304; Amidase_sig_enz; 1.
DR SUPFAM; SSF51230; Hybrid_motif; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 1.
DR TIGRFAMs; TIGR02713; allophanate_hyd; 1.
DR TIGRFAMs; TIGR00724; urea_amlyse_rel; 1.
DR TIGRFAMs; TIGR02712; urea_carbox; 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; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW Biotin; Complete proteome.
SQ SEQUENCE 1819 AA; 197589 MW; A96D78109A7CA6F4 CRC64;
MTDHSSTVGW TSQQWREFHR RASADASLAR LLALAHAERD AGAAWISVAS DEHIEHQWRV
LQSRGDRQRL PLYGVPVAVK DNIDVRGLAT TAACPSFAYT AAQDATAVRL LRDAGAVILG
KTNMDQFATG LVGTRSPYGS VASAFSSAHA AGGSSSGSAV VVARGAVPLT LGTDTAGSGR
VPAALNNLVG VKPTRGTVSC TGVVPACRSL DCVSVFARDV ADAHRCLRIL ARPDGSDPYS
RPSPADAPRR FGTCPVVGVP REAEWFGESQ NAELFAAACQ RMRAAGARVV EVDPQPLLDL
GRSLYEGPWV AERYAAMRAF YSGQPPRDTL DPTVTGIITS AGGYSAADVF DHGLRRQKLV
AAIEAELAGV DALLVPTCPL NPTLAAIAAE PLLVNARQGM WTNFVNLADL AAVAIPAGFR
RDGLPQGVTL VGRKFSDLAL LELGSRLLRV EDAEPRRCGA LPAGQALCED EVVSGSEERD
STVLLAVVGA HLRGLALHWQ LDEVQAEFVR EARTAPSYRL YALPKTGPVL KPALRRVCAG
KGAAIELEVY SVPEATFGRF VAMVPAPLAI GSVELESGEY IKSFVCEEDG YIQDGTVDIT
HFGGFRRYVE HLRRQRDVDK PFDTVLVANR GEIAVRIIRT LKRLGIRSVA VYSDPDRHSQ
HVRDADVAVA LGGSSAAETY LDIDKILAAA KKTDTQAIIP GYGFLSENAT FAERCGAEGI
VFVGPSGDSI RKLGLKHWAR ELAASAGVPL TKGTGLLQSA SAALEAGEEI GYPLMVKSTA
GGGGIGLQRV DSAAELAAAF EQVQRQGELY FTDSGVFLES FIARARHVEV QIMGDGHGRT
VALGERDCSL QRRNQKIIEE TPAPNLPAHT RQKMRQAAQR LCSAVKYKCA GTVEFMYDEQ
KDEFYFLEVN TRLQVEHPIT EMVTGLDLVE WMLRIAANTP PDFDAGVEIE GVSMEARVYA
ENPVKGFTPS PGLLTEVVFP SWARVDTWIL KGTRVAAEYD PTLAKIIVHG KDREDAVSKL
LLALSETRIA GCMTNLDYLK SIASSEEFRK ASVFTRLLND FEYTPTAFEV KIPGAYTTIQ
DYPGRVGYWR IGVPPSGPMD SYSFRLANRV VGNDSKAAAL EITLNGPELK FHSDAVIAVT
GGAVPVTLNG KPVLQYVPLT LEKGDVLKIG KLESGSRAYL AVRGGIDVPE FLGSRSTFAM
GGIGGHNGRV LAPGDVLFIN KDSSVAVGDT VTIPSGLQPV IPRESWKIGL VCGPHGSPDF
FKREALEEFF SSPWKVHYNS NRFGIRLIGP KPKWARSDGG EAGLHPSNTH DYVYSVGAIN
FTGDEPVIIA AEGPSLGGFV CAAVVPEAEL WKVGQLKPGD TIKFVPISVD TARALKRSQD
AAVDALDILS SIKLDDSMVL PSYQDPVLLR LAKRSGLCPK VTFRQSGDRY ILIEYGENEM
DINISYRIKQ LQEMVTKNKV TGIVEMSQGI RSLLVEYNGY TISQEDLLSV LSAYELEINF
DVDWKVKAKL FRLPMAFEDS KTLEAVRRYQ ETIRSDAPWL PSNADFVANV NGITRADVRD
LLYSATFMVL GLGDVFLGAP CAVPLDPRQR LLGTKYNPSR TYTPNGVVGI GGMYMCIYCT
DSPGGYQLMG RTIPIWNRLQ LGEAWKDHPW LLTPFDQVEF YPVSEERINE LTEEVENGTF
ELEVKETVFD NGAYNRWLED NRESIQAFKE GQSGERAAEF ARLIKVANSD LETAVRKEAE
PVEYPEDAHM VYSEYAGRFW KQVVSVGDKV KEGDKLVIIE AMKTEMVVSA TADGEVINIL
HANGDMVDAG NLVVVLKNC
//
