ID A0A1Q8RC53_9PEZI Unreviewed; 961 AA.
AC A0A1Q8RC53;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE SubName: Full=Putative urea carboxylase 1 {ECO:0000313|EMBL:OLN81829.1};
DE Flags: Fragment;
GN ORFNames=CCHL11_08902 {ECO:0000313|EMBL:OLN81829.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN81829.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN81829.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN81829.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:OLN81829.1}.
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DR EMBL; MPGH01000241; OLN81829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8RC53; -.
DR STRING; 708187.A0A1Q8RC53; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000186583; 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 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; 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; 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 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; 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; 1.
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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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}; Reference proteome {ECO:0000313|Proteomes:UP000186583}.
FT DOMAIN 4..453
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 109..314
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OLN81829.1"
SQ SEQUENCE 961 AA; 104450 MW; E900B49457B6A622 CRC64;
PLRNIKKVLI ANRGEIAVRC IKACHELSIH TVSIYTDGDA TSLHVLHADE AVLLRGGDST
AYTDGDAILD ICRNTGVDAV FPGYGFLSEN ADFADAVTAA GFTFVGPSSA SIKAMGLKHE
ARSIAEAVNV PVIPSMHEAI EGAKRFGFPV MLKATGGGGV MGLQICHDDD DVPKAFATVE
SRAGALFKNS GVFLEKYYPQ SRHIEVQVFG NGVDVIAIGE RECSLQRRHQ KVIEECPSPF
VERTPGLRER MLEAAVNYAC QLGYKSAGTV EFLVDEETAD FFFLEMNTRL QVEHGITELC
YGVDLVHLML QQADYECGGQ PGLPLEDLRS IGRPKPFGSA IESRVYAEIP LPGYAPSPGL
LQHVQWPQGG GVRVDTWVKS GQKITPLYDP LVAKVMVHSL DGRETARKKM LKAPDETSLH
GTQTNLSYLS SVLKSRAFKE GNTLTNFLST FKVDACVVQV LNPGVFTTIQ DYPGRTAVGH
GIPPGGPMDD ISSRAANILV GNDARVELLE ITLVGPELLF HEPAVVAICG AQASVTVNGE
DRPMWSRIVV RQGQTLKIGN VVGHGLRTYL AVKGGFPEVP LFLGSKSTAP ELVFGGLQGR
KLQTNDILAL APESGDWAAM SSSHSLPHGA ILDYNFTEVY CLNGPYGSED ILAPEGMNTI
TSSLWTVGHN SSRSGIRLEG PRLQWARTTG GGGGSHPSNV FDYGYPNGGV NWTGEYPIIF
SRDRPDLGGF ACPVTICSAE MWKVGQLKPG DTIRLKLTTF DNALKITKQN EAYLHAIAAL
SEVREVQVPS IKAIFGLEST SSILRTAPRS QDHPRVTYRQ GGDTSIVVEC GEQIADLRNT
VCVQLLKEKL LSRNMYGVRC EPNIATLTVH YEPSKIGQSE LLKVLERLDE SIGGTSSVKV
PIRQIKLPLC VDHPTIKEAT KRYMESIRPR AAYLPDNVDY IRKSNALESR RDVFDSLLNT
P
//
