ID A0A2G5I2Z1_CERBT Unreviewed; 1236 AA.
AC A0A2G5I2Z1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE SubName: Full=Putative urea carboxylase {ECO:0000313|EMBL:PIA98872.1};
GN ORFNames=CB0940_02447 {ECO:0000313|EMBL:PIA98872.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA98872.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA98872.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA98872.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) 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:PIA98872.1}.
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DR EMBL; LKMD01000101; PIA98872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5I2Z1; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000230605; Chromosome 3.
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; 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_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; 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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 3..457
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1153..1234
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT COILED 1096..1138
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1236 AA; 135343 MW; 37F8378294CB4CF3 CRC64;
MEKLKTLLIA NRGEIAVRII RTAKQLGIKT VSVYTSADAA SLHVSDADEA VLLPTLQSYT
DGDELLRIAK EKGVDAIIPG YGFLSENAAF AKAVSDAGLA WVGPREDAIK AFGIKHTARD
LAKQSGVPIV PGTEGLVESE EDAVKQSDSL GYPVMLKITA GGGGSGLITC QNAEQVKDGF
KKAQSRGQAL FKDSGVFIER YYPEAHHIEV QVFGNGLGHA IHFGERECSI QRRHQKVIEE
CPSPFVQNHS GLREKICSAA VSLAQSVKYG SAGTVEFLVD DKTADFFFLE MNTRLQVEHP
ITEACYDVDL VELMLKQADA QLTGQGGLSA EYLDSLQKPG PFGAAIEARL YAENVLRDYA
PSPGLLTEVY WAERQNARID TWVRTGLRIS PNYDPLIAKV INHAKTRDAA LKGMGMLLEQ
SVVSGPPNNL DFLGAIIKDE TFQSGRTITS FLQSFEYKPN VIDVATAGAY TLVQDLEGRP
SVGKGIPRSG AMDPIALAVA NALVGNERGQ EGLEITLSGP ELKFHGPAVI AVTGAPIEVA
LDGDSIPMWT RKHIKPGQIL KIGKTTAGGC RSYLAVYGGF TSVADYFGSK STSPIVAIGG
YQGRQLAPGD QLSLVKEIPS NLHSHPSVPE SLRPDYSSPW TINALPGPHE EGYLTEQDIE
MLYSTEWKVS HNASRSAIRL IGPVPKWARA DGGEGGSHPS NLVEYGYSCG SLNWTGDEGC
IFALDCPNFG GFASSATAIR ADYWKLGQLK AGDSLKYQRV SLEEALSLRR NVEDYIEGIS
KAVQTNDFNN VKPLASDFKA SGNYSKAVLW ERPASGAQPQ VRYRQAGDAY LLVEYGNEQF
DLNYRCRVTA LEKAINDSTA PTWLKKDLIT TVGCCTSLNI HYDGSQMDRA QLIAHLQTLE
DQIGDLSKTK VPNRRFKLPL SFESKEQTEA TERYMSNQRP HAPYLPDNLD FVAKNNAFTA
DQLKHNMLTG ELMAVVVGFY CGNTVSLPVD PRMRMSAPKA NPSRVFTPEG TFGWGGSCAS
IYPVDSPGGY QMLGRTIPCF DYYGFKSGFT PTRPWLFQDF DILTFHRVSE SELNAQLELF
RSGQYEFTYE DSEFDMAEHN KLLEATKSEV EEIRAKQRKV QEEMIRAENE SLKRWREEKE
KRKPDLSTIE SLLGQEGVGV VEAPVDANVW KVEVKEGDEV EGNQVVVILE AMKLEINVYV
PEGFASGGKK AVVEKLLVEP GETIKAGGRI ALIRSS
//
