ID H1UVE3_COLHI Unreviewed; 695 AA.
AC H1UVE3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Carbamoyl-phosphate synthase subunit L {ECO:0000313|EMBL:CCF31944.1};
GN ORFNames=CH063_04422 {ECO:0000313|EMBL:CCF31944.1};
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:CCF31944.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {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).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CACQ02000275; CCF31944.1; -; Genomic_DNA.
DR AlphaFoldDB; H1UVE3; -.
DR STRING; 759273.H1UVE3; -.
DR EnsemblFungi; CCF31944; CCF31944; CH063_04422.
DR VEuPathDB; FungiDB:CH63R_05895; -.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_000395_3_1_1; -.
DR Proteomes; UP000007174; 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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
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 SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..388
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 52..252
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 695 AA; 76818 MW; F8D1A2355EE2A470 CRC64;
MAQRRCFATL HPGYGYLSEN PDFASSVRHA GLIFVGPPSE AMSTLGDKRS SKDYLRQKAP
EVPLIPGFTG TSLEIEDLKK AAVNIGFPVM LKASAGGGGK GMRVVHEVSQ LQSELRRAQS
EAQRSFGSRD CILEKFIENS KHIEIQVVGD QYGHVVSFLE RDCSIQRRNQ KVIEETPCLF
LDQETRRHMS DTAVRIVKLI GYEGAGTVEF VFDTATKKFY FLEVNTRLQV EHPITEEVVG
VDLVALQLFV AAGGRLSELP ELSHIVQTGH AIECRLCAED PRRDFLPSHD KILLWKPASP
ERVPGSVVRY ETAICSGTSV SIYFDSMICK IVVWAPTRSQ AISRLAKELA GTACIGVRTN
QLFLQSCLLH PAFQDFGYKT SFIPDNITRL LQSPYSPDLP GYITLVPALF LRSVQQLQTG
KLSVRRPFQA VRRRFHNQKF DAFHNSCEII SLRDSNSPAG EIVRNDACLI KPASTDAEHE
WSVYLYPLVR GSKKPSMNQT GSSAQDLAAT YSHTSRALRT GEAWLGPSFK ATHVDVRPVY
QHETVPSTTG ASSAAMSMTL SLDGQRMCAY LAVSDDGDGR QSLSLNETIK VLCHLPQLGE
WKEFRRDSLL SFYTSLRKEA LSNSDQESGV KAPMPCKVLS IAKALGEDVS AGECVMVIES
MKMEINIIVG VSGKFQTKWK IGEAVDEGAV LCLVE
//