ID A0A4R8QXY2_COLTR Unreviewed; 1073 AA.
AC A0A4R8QXY2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE SubName: Full=Putative urea carboxylase {ECO:0000313|EMBL:TDZ48384.1};
GN Name=lamA {ECO:0000313|EMBL:TDZ48384.1};
GN ORFNames=CTRI78_v008219 {ECO:0000313|EMBL:TDZ48384.1};
OS Colletotrichum trifolii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=5466 {ECO:0000313|EMBL:TDZ48384.1, ECO:0000313|Proteomes:UP000295703};
RN [1] {ECO:0000313|EMBL:TDZ48384.1, ECO:0000313|Proteomes:UP000295703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=543-2 {ECO:0000313|EMBL:TDZ48384.1,
RC ECO:0000313|Proteomes:UP000295703};
RA Gan P., Shirasu K.;
RT "Genome sequence and assembly of Colletotrichum trifolii.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDZ48384.1}.
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DR EMBL; RYZW01000097; TDZ48384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R8QXY2; -.
DR STRING; 5466.A0A4R8QXY2; -.
DR Proteomes; UP000295703; Unassembled WGS sequence.
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; 2.
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 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; 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; 2.
DR PROSITE; PS50979; BC; 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}; Reference proteome {ECO:0000313|Proteomes:UP000295703}.
FT DOMAIN 3..379
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..167
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 191..260
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1073 AA; 116478 MW; 4EFC13DEDA9BDAC8 CRC64;
MRAIRTVLVA NRGEIAVRCI RACRKLGIDT VAIYTAADSG SLHVSQATRS LLLDDDGPGA
FANVEKILDI CKAESIDAVF AGYGFLSENA GFARQVQEHD MAFVGPDYRS IEAMGLKHTA
RELAVAASVP VVKGSGLLRN PDEAVEAARV AGLPVMLKAS GGGGGMGTQV CWTEDEVVEE
CPSPHLADKP ELRQRLLDCA TSLTRSINYR SAGTVEFLVD DESDDFFFLE MNTQLMLVQA
DYELAKAGGI PSDVLLKLQK DTPNGAAIEV RICCENPASQ FLPSSGLVQQ LRWPAEDNAR
VDTWIQAGTR VSSDFDSLLA KVMVRKDTRD SAIRHLVDVL QYTQIGGIVN NLAFLRHLIT
SQPFRSGRTL TMFLSEQYKF EPCGIQVIAP GGHTTIQQAR IRSINGFGIP KGGPMDDLSA
TLANLIVGNE KDTECLEVVM MGPELMFLSE TIISICGADL PVELDGKTVD MWSRVHVRPG
QKLKLGIVRG HGASCYIAFE GGLPSAADWL GSKSTTSSLG LGGLQGRILR HGDYLELAKI
NFDADRGTAT LPLELRPPLN VTEICVMHGP HDSDDFITHK GRDQLSSATW KVNHNCSRTG
IRLDGPSIEW ARETGGTAGA HPSNVVDYPY PSPGGVNWTG DSPAIFPRDA PDLGGFLCSS
TVPSAELWKL GQLKPGHAFR FVPVSFSAAR KLSKLKSAFI DAVRRFLSNE NFESVTWSLD
KEEDTKSSII KVVTGDTHTS TLTIRQAGDT GVLVDLGFQN ATLETSVKAN SLASAIQATS
TSGLSVRINI SSVLVEFDPE LFSQECIVDL VAASSLSVAR IEKPMKCRLL KLPIVFDHPA
IKESEERYTK LIRSKAAYLP DGVAYVQENN ALPKREDVFR ILRNSRFMVV AVGFMIGLPL
MLPLDPRARL SAQKYNPPRT STPPGTVGLG GRSFCIYPTD QPGGYVPIAR SIPVWDTFSL
RKGFAEGRPW LCEPFDLVEF YDVDLDKFSR IEKAFQSGTW EPSIENAIFD GALELVKAGD
KVSAGQTVAI LESMKMEIPI VADSKHDGFF VKVVAAKEGV LVYPGDAIVV LAN
//
