(data stored in ACNUC8465 zone)

SWISSPROT: Q6FJK7_CANGA

ID   Q6FJK7_CANGA            Unreviewed;      1834 AA.
AC   Q6FJK7;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 108.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62563.1};
GN   Name=DUR1,2 {ECO:0000313|CGD:CAL0136535};
GN   OrderedLocusNames=CAGL0M05533g {ECO:0000313|CGD:CAL0136535,
GN   ECO:0000313|EMBL:CAG62563.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62563.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|SAAS:SAAS00198459};
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DR   EMBL; CR380959; CAG62563.1; -; Genomic_DNA.
DR   RefSeq; XP_449587.1; XM_449587.1.
DR   ProteinModelPortal; Q6FJK7; -.
DR   STRING; 284593.XP_449587.1; -.
DR   EnsemblFungi; CAG62563; CAG62563; CAGL0M05533g.
DR   KEGG; cgr:CAGL0M05533g; -.
DR   CGD; CAL0136535; DUR1,2.
DR   EuPathDB; FungiDB:CAGL0M05533g; -.
DR   eggNOG; KOG0238; Eukaryota.
DR   eggNOG; KOG1211; Eukaryota.
DR   eggNOG; COG0154; LUCA.
DR   eggNOG; COG0439; LUCA.
DR   eggNOG; COG1984; LUCA.
DR   eggNOG; COG2049; LUCA.
DR   HOGENOM; HOG000251581; -.
DR   InParanoid; Q6FJK7; -.
DR   KO; K14541; -.
DR   OMA; HYNSNRL; -.
DR   OrthoDB; EOG092C0324; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0004039; F:allophanate hydrolase activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004847; F:urea carboxylase activity; IEA:EnsemblFungi.
DR   GO; GO:0043419; P:urea catabolic process; IEA:EnsemblFungi.
DR   Gene3D; 2.40.100.10; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR014085; Allophanate_hydrolase.
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; 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; IPR003778; CT_A_B.
DR   InterPro; IPR003833; CT_C_D.
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; PF01425; Amidase; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF02626; CT_A_B; 1.
DR   Pfam; PF02682; CT_C_D; 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;
DR   PRODOM; Q6FJK7.
DR   SWISS-2DPAGE; Q6FJK7.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00449439};
KW   Biotin {ECO:0000256|SAAS:SAAS00064008};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Ligase {ECO:0000256|SAAS:SAAS00234187};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00449848};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN      629   1072       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      748    945       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN     1753   1832       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   1834 AA;  204072 MW;  E9C0E20122CB5E8F CRC64;
     MTATNICPSI GWSIQDWIDF HFKSTPKDSY ESLLELVKNQ RIAPEDPAWI SVATESLLEQ
     QWQLLQSRHE KEKLPLYGVP IAVKDNIDAK GFPTTAACPS FSYMPTRDST VVELLKQAGA
     IIIGKTNLDQ FATGLVGTRS PYGRTPCVFS DKHVSGGSSA GSASVVARGI VPIALGTDTA
     GSGRVPAALN NIIGLKPTRG IFSCSGVVPA CKSLDCVSVF SMNLSDAEKC LKIMTKLDIE
     NDEYSRSFPA NPLQSFNKNL TVAIPKNVMW YGEKENPLLY DRAIDNFKQL GAQIKIIDFE
     PLLELARCLY EGTWVAERYA ATRKFLETSP QQSTLDPVVY GIIKSATKFD AADAFEYEYK
     RQGILRKVEV LLQDIDVLCV PTCPLNPSFE EVDKEPILVN SRQGTWTNFV NLADLSALAI
     PVGFRSDGLP NGVTLIAKKF EDYALLQLAK RFLAQLYPSG TRPYGMFLDR YVGLKDDSLE
     GPIVSSDDSI VLAVVGAHLR GLPLHWQLEK VNATFICSTK TAKKYELYAL PKNGPVLKPG
     LRRITSGTGS QIELELYSVP KEKFGEFISF VPEPLGIGSV ELENGKWVKS FICEESGYNS
     TGSIDISHYG GFRAYIESII PSNESKKGHF KTVLVANRGE IAVRIIKTLK SMQIKSLAIY
     SATDKYSQHV LDVDMAQALD GHTVEETYLH VEKIISIAKK YDVDAIIPGY GFLSENASFA
     DRCEQEGIQF IGPRGETIRK LGLKHSAREV AKSAGVPLVP GSPLVKNADE AFTIAKNIGY
     PVMVKSTAGG GGIGLQKVDN EQDMRKAFET VKHQGSSYFG DSGVFMEKFI DNARHVEVQI
     MGDGKGKTLA LGERDCSLQR RNQKVIEETP APNLPRETRQ KMLTAAERLG AYLNYRGAGT
     VEFIYDEQRD QFYFLEVNTR LQVEHPITEM VTGLDLVEWM IKISAGVMPS LDEFNISQNG
     ASIEVRVYAE NPLKDFRPSP GELVDVQFPN DCRVDTWVKK GTKISPEFDP TLAKIIVHGK
     DRNEAILKMK KALNETKIYG CVTNVDYLKS LISSEMFRNA QLSTNYLNTY EYSPSAVEII
     EPGALTTIQD YPGRVNYWRI GVPPCGPMDN YSFRLANRIV GNDERTPGIE ITLTGPTIKF
     YSDSLVSIAG GEVCCKLDEK KIPMFEPISV KTGSVLSIGK IVKGSRAYLA IRGGIDVPKY
     MGSFSTFTMG NLGGFNGRAL KRGDVLSLPQ QFDSEHGIPS PCFSPEKAPI YVRPDIPNDG
     VWTIGVLAGP HGAPDIFESE GMMEFFKSEW KVHYNSNRFG VRLIGPKPKW SRTDGGEGGL
     HPSNTHDYVY SLGAINFTGD EPVIITCDGP SLGGFVCQAV VSEAEMWKVG QLKPGDTINF
     TPIDWQSARN LKENQDVIIN DMSSCALQKL SDQPLLKSPE DPILFQKDGQ ELQSPKVVYR
     QAGDRYILIE YGDDIFELNL CYRIKSLIDI ISQRNTKGIK EMSQGVRSVL VEYDGYEISQ
     KELLKTLIAY EEQLPQEKNW SVKSRIFRLP MAFEDKETLA CVKRYQETIR SKAPWLPNNV
     DFVAEVNNLT HDDIRQLIYT TRYMVLGVGD VFLGSPCAIP LDPRNRLLGS KYNPSRTFTK
     RGVVGIGGSY MCIYAADSPG GYQLVGRTIP IWDRLMLQSK KDEPWLLSPF DQIEFYPVSE
     EQIDEYTDEW DNGNYKIDVD DVVFDHGSYL KWVQDNIEAI EEHQRAQRGD NYSKFAQKIQ
     EANADLKQTT TEVIEQNILE DDCEYIFSEY AGRFWKPIVE IGASIEKDQG VAVIEAMKTE
     MIVSSSVVGK LKKFLFKNGD MVDAGDPVAI IQCL
//

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