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Database: UniProt
Entry: H1V5P7_COLHI
LinkDB: H1V5P7_COLHI
Original site: H1V5P7_COLHI 
ID   H1V5P7_COLHI            Unreviewed;      1234 AA.
AC   H1V5P7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:CCF35549.1};
GN   ORFNames=CH063_07304 {ECO:0000313|EMBL:CCF35549.1}, CH63R_02411
GN   {ECO:0000313|EMBL:OBR13685.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF35549.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|EMBL:CCF35549.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:CCF35549.1};
RA   Ma L.-J., O'Connell R., van Themaat E.V.L., Stueber K., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Colletotrichum higginsianum IMI 34906.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
RN   [3] {ECO:0000313|EMBL:OBR13685.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:OBR13685.1};
RA   O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT   "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000092177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX   PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA   Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA   Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA   Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA   Thon M.R., O'Connell R.J.;
RT   "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT   structure and association of transposable elements with secondary
RT   metabolite gene clusters.";
RL   BMC Genomics 18:667-667(2017).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CACQ02001583; CCF35549.1; -; Genomic_DNA.
DR   EMBL; LTAN01000002; OBR13685.1; -; Genomic_DNA.
DR   RefSeq; XP_018162202.1; XM_018297386.1.
DR   STRING; 759273.H1V5P7; -.
DR   EnsemblFungi; CCF35549; CCF35549; CH063_07304.
DR   GeneID; 28861493; -.
DR   KEGG; chig:CH63R_02411; -.
DR   VEuPathDB; FungiDB:CH63R_02411; -.
DR   eggNOG; KOG0238; Eukaryota.
DR   HOGENOM; CLU_002162_0_1_1; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   Proteomes; UP000092177; Chromosome 2.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 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; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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; Cyclophilin-like; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          8..461
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          124..322
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1153..1231
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          797..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..817
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1234 AA;  134284 MW;  6A8BD95FFD8C6923 CRC64;
     MEPKPLLNIK KVLVANRGEI AVRCIKACRE LGVHSIAVYT DADTTSLHAL LADEAIPLRG
     SDTYTDGAAI LSICRSTRAD AVFPGYGFLS ENVEFADAVT NAGIVFVGPS SASIKAMGLK
     HEARSIAEAV NVPVIPGTSL IPSTHEAIEG AKKLGFPVML KATGGGGGMG LQICYDDDDV
     PKAFATVESR AGALFKNSGV FLEKYYPRSR HIEVQVFGNG VEVVALGERE CSLQRRHQKV
     IEECPSPFVE RTPGLREKML QAAVNYASQL KYKSAGTVEF LVDDETADFF FLEMNTRLQV
     EHGITEMCYG VDLVHLMLYQ ADFERGGHLG IPSVELQSIS RPQPLGSAIE ARVYAEVPLL
     DFAPSPGVLQ HVHWPQGDGV RVDTWVKSGQ HITPLYDPLV AKVMVHSPAG RVDAQKRMLA
     ALADTALQGT QTNLQYLSQV LRSDAFTKGN TLTNFLASFQ VDACAVQVLS PGVFTTVQDY
     PGRRAVGHGV PPSGPMDDLS SRAANILVGN DPQAELLEIT MTGPELMFHE SAVVAVCGAQ
     VPVAVNDEDR PMWSRIIVRR GQTLKIGNVI GDGLRTYLAV KGGFPEIPLY LGSKSTAPEL
     VLGGLQGRKL QTNDILALSS ESGLWADTAS PFSLPRGAIP DYSVSEVYCL NGPYGSEDIL
     TPEGMETITS SKWTVSHNSS RSGVRLEGPR LKWARTTGGG GGSHPSNVFD YGYPNGGVNW
     TGEYPIIFSR DRPDLGGFAC PVTICSAEMW KVGQLKPGDA VRLQLVNFED AMEITRENEA
     YLESVAALVD GQDIAVSPPR KTFGPQNNTS SILQTTRPHG DHPRVTYRQG GDTSIIVEYG
     EQVADLRNTV CVQILKEKVA ARGIVGVRCE PNLATLTVHY DPVQIHQSEM FQSLRQLDES
     IEEIVGTRMA VRELSLPLCV DHPTVQEATE RYMESIRPTA AYLPDNVEYL RKNNALKSRR
     EVFDSLVNTP WLTVAVGFFV GTPILFPLDP RYVFTGQKYN PNRAYTPSGS VGLGGSLLAI
     YPVAAPGGYQ LMGRTLGTWD MMGTRPGFSP SRPWLFDHFD IVRFREVSKE EFDQAERDFE
     GGRYEFEISE GVLAMDEYIA KFDAAARDPA HQEWRERQAA AAREMGELEQ RLFGEWSEAK
     AAEMAGQSEV GAEAASADTV TIESPMNANV WKTLVKVGDV LEDKQTVAIL EAMKMEIKVV
     VSEAQAGAVV TKITRPPGSV VSPGTPIVVC KKAR
//
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