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Database: UniProt/TrEMBL
Entry: Q75A67_ASHGO
LinkDB: Q75A67_ASHGO
Original site: Q75A67_ASHGO 
ID   Q75A67_ASHGO            Unreviewed;      1819 AA.
AC   Q75A67;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   26-NOV-2014, entry version 105.
DE   SubName: Full=ADR051Cp {ECO:0000313|EMBL:AAS51971.2};
GN   ORFNames=AGOS_ADR051C {ECO:0000313|EMBL:AAS51971.2};
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 {ECO:0000313|EMBL:AAS51971.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51971.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
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., Pohlmann 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).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- COFACTOR:
CC       Note=Biotin. {ECO:0000256|SAAS:SAAS00064093};
CC   -!- SIMILARITY: Contains ATP-grasp domain.
CC       {ECO:0000256|SAAS:SAAS00146608}.
CC   -!- SIMILARITY: Contains biotin carboxylation domain.
CC       {ECO:0000256|SAAS:SAAS00064021}.
CC   -!- SIMILARITY: Contains biotinyl-binding domain.
CC       {ECO:0000256|SAAS:SAAS00064091}.
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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   InParanoid; Q75A67; -.
DR   KO; K14541; -.
DR   OrthoDB; EOG7PGDZZ; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 2.40.100.10; -; 2.
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; IPR029000; Cyclophilin-like_dom.
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; SSF50891; SSF50891; 2.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   SUPFAM; SSF75304; SSF75304; 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   ATP-binding {ECO:0000256|SAAS:SAAS00146616};
KW   Biotin {ECO:0000256|RuleBase:RU000428, ECO:0000256|SAAS:SAAS00064008};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000591};
KW   Ligase {ECO:0000256|SAAS:SAAS00057833};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00146599};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
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
//
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