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Database: UniProt
Entry: T0KTW7_COLGC
LinkDB: T0KTW7_COLGC
Original site: T0KTW7_COLGC 
ID   T0KTW7_COLGC            Unreviewed;      1544 AA.
AC   T0KTW7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   31-JUL-2019, entry version 37.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:EQB56113.1};
GN   ORFNames=CGLO_03899 {ECO:0000313|EMBL:EQB56113.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB56113.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in
RT   Colletotrichum gloeosporioides as revealed by transcriptome
RT   analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|SAAS:SAAS00197451};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EQB56113.1}.
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DR   EMBL; AMYD01000795; EQB56113.1; -; Genomic_DNA.
DR   STRING; 474922.ELA26223; -.
DR   EnsemblFungi; EQB56113; EQB56113; CGLO_03899.
DR   OrthoDB; 254436at2759; -.
DR   Proteomes; UP000015530; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
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_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR011053; Single_hybrid_motif.
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; SSF53335; SSF53335; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 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:UP000015530};
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:UP000015530}.
FT   DOMAIN        7    463       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      125    321       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      808    834       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1544 AA;  169885 MW;  222C7BC687D3D3A3 CRC64;
     MTSSLKAIKK VLVANRGEIA VRCIKACREL GVKTVAIYTD ADASSLHIVS ADEAVLLPGS
     DRTAYTDGDA IINIAKTHNA DAIIPGYGFL SENADFAAAA EAAGIIFVGP SVTSIRAMGL
     KHEARDIAHQ AGVPTVPGTT LLSSAAEARE NATRLGFPVM LKATGGGGGM GLQICQDEAE
     VEKAFETVVS RAGTLFKNSG VFLEKYYPRS RHIEVQVAGN SEAVVSFGER ECSLQRRHQK
     VIEECPSPFV DATLRRKLCQ SAIDYASQLN YKSVGTVEFL VDDETAEYFF LEMNTRLQVE
     HGITELCYGV DLVHLMLRQA DCEKAGLGGI PTAELRSLWR EQPLGSAIEV RVYAEDALND
     FAPRPGLLQS VRWPESEGDE GVRVDTWVKG GQRITPYYDP LVGKIMVHDD QGREQARQKM
     IRVLKGTTLQ GTQTNLQYLT KVLQSEAFIQ GNTLTTFLND FVFEACAIQV LEPGMMTTIQ
     DYPGRVSVRH GVPRSGPMDT LSSQIANVLV KNEPGTELLE VTLTGPTLRF YVDAVVAVCG
     GSVPVTVDDM DQPMWSRFVV RRGQVLKLGQ LGGSGFRAYI AIKGGFPGIP LFLGSKSTAP
     ELGYGGLEGR KLQMHDVLDL AEQSAQWAAE ATLFQLPSEA VPNLDIRQVW CMEGPYGDND
     ILTPAGRAAL YEAVWKVNHN SGRSGVRLAG PQLEWARSSG GGGGSHPSNV FDYGYPVGGV
     NWTGDFPVIF SVDSPDAGGF ACPLTICSAD FWKLGQLKPG DEIRFTPTTF ESAMAMLKYQ
     DEYVASVATC SYASQVTAPI PPRYVEGYSQ ASSGSPTLRE TPATDSDPKT TYRQGGDSSI
     IVEFGTQVAD LRNTICVRLL AKQLEERQLD GVSWTPSIAT LTVHSNPKKI PQTELLNILS
     ELPCGLSQSS NQMPVREIQL PICLDHSAIA EAVQRYMYNI RKEASYLPDN VEYIRENNAL
     SSRQAVFDAF LNTPWLTVAV GFYVGTPFLF PLDPKYVYVG QKYNPSRVFT PSGSVGLGGS
     LVAIYPVAAP GGYQLIGRTI GCWDETGNRP CFEPSKPWLF RHFDLVRFVE VGEEEYDKLK
     HDYDIGQYEF TISETTINMD HFIAKFDAAN QDPAHLEWTK RQSEASQELA RRETELFDEW
     HAATTASTNG AAAAGGELEE HSGSNVLRIK SPVSASVWKV EVGVGDVLKS GQTVAVLEAM
     KMEIKVICGK DEDGMVVKSI VTDDNASEIG TSVASSTASV TSSVLSYREE NGRKYHGYKD
     GKYTAPNDEQ EQDRLDLQHN LFLLTFDNAL GLAPPNQPNS NVQRVLDVGT GTGIWAIDFG
     EDHEQAEVLG IDLSHSMPEF VPPNVRFEID DLDEEWTYSQ PFDYIHTRGM NSCIADWKVF
     LTKVFDNLTP GGYFELQELE VFPRSDDGTL TPECQLSQCM KYVHEAFEIF GRSFQEIPDL
     VKVMEDVGFV DVKMSLFKWP SNTWPKDPKY KELGDWNNEN INNGFVAITM APFTRALGWT
     KEEVHVFLPG VRKDLNDKSI HAYWPVYVVY GMKPMEKKTE TAEA
//
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