ID A0A167DJJ2_9PEZI Unreviewed; 1823 AA.
AC A0A167DJJ2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:KZL83961.1};
GN ORFNames=CI238_06964 {ECO:0000313|EMBL:KZL83961.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL83961.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL83961.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL83961.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-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:KZL83961.1}.
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DR EMBL; LFIW01001005; KZL83961.1; -; Genomic_DNA.
DR STRING; 1573173.A0A167DJJ2; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000076584; 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; 1.20.58.1700; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 1.
DR InterPro; IPR014085; Allophanate_hydrolase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
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 InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR02713; allophanate_hyd; 1.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 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; PF01425; Amidase; 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; SSF75304; Amidase signature (AS) enzymes; 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};
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584}.
SQ SEQUENCE 1823 AA; 196377 MW; A64CF0F51395F5B3 CRC64;
MGSTTQDTFP LTVPEWREVQ EAGDGLGRLL SLRQSEARLN SNAWIALATQ SQIEQQWTHA
ESLRISGASL PLFGVPFAVK DNIDVASFLT TAACPSFAAG PVDKDATIIA RLKAAGAIVL
GKTNLDQFAT GLVGTRSPYG PVSNSFDPSR VSGGSSSGSS VVVARGVVPF SLGTDTAGSG
RVPAGLNNLV GLKPTRGALS TTRVLPACRS LDCVSIFALT VDDAETVLAA AEGFDPEDSF
SRARPDKPST VNGHHLAVCD NPPWFGKTEQ AAAYAQALRK AENLGWTLES KDFSPLFKLA
SLLYEGPWVA ERYAAIKDFI EAHQDEMDPT VREIILRAKE FNATDLFASE YLRQDLTREI
EDKFGEFDGI LVPTTPTFPT IEDLVREPIK ENAYLGTYTN FVNFMDWTAL AIPAGFRSDG
LPFGITLISS TWDEPKLLSM AREWLSTEPR PLGATKIERL EVRKPDAIAA GEPKTTRLVV
VGAHLMGFPL NKDLTSRGGT IETATTTSPN YKLYSLNTGS KVKKPGLQRV LSGGSPIQVE
VWSLPTIELG SFLKTVPSPL GIGSVELADR SWAPGFICEP YGLESATDIT SFGGWRTFIE
SLASEAPPIK TTLTISDIKS VLIANRGEIA VRIIRTLHSL GLKAITIHSA ADARSPHVRN
ADVSLLLEGT SVLETYLNGV QIIALAKSAG ADAIIPGYGF LAENADFASA VEAEGMIWVG
PTADQMRQLG LKHLARDVAI GAGVPVVPGS KYLLKSVEEA LTEAERIQYP VMLKSTAGGG
GIGLKRCDDA VSLVEAFESV QRLAQANFGD AGVFLEHFIE NARHIEVQII GDGCGNVTSA
GERDCSLQRR NQKVIEESPA TFVPPDVRKR MRQAAVDLAS AVKYRNVGTI EFIYDIDTSE
FYFLEVNTRL QVEHPVTESV TGLDLVECMI RVASGNGKDI FVDKLRGIEV RGSSIEVRVY
AESPLQNFRP SPGRLLDVSF PEGVRVDTWV AAGMEMSSSY DPLVAKIIAT GENRAEAMVK
LANALEKTVI TGVETNLEYA RHIVASEMFK SGAFTTTSLN SFTFDASIFE VVDSGTLTAV
QDYPGRKGLW HVGVPPSGPF DDYSFRLANR LVGNDSRAAG LECTIHGPSL LFHCDAVVAV
TGASTEVKLD SAVAQLNTPI TVRKGQTVSV GTATSGYRSY IAIRGGIAVP EIFNSCSTFA
LGKVGGHNGR NLRSGDLIPV GSMTSTAPSV ASGPATPLPA DPTNAYWSIG VVPGQHSAPE
HFTEQGFNTL FAGEWIVHYN SNRIGIRLDG PKPQWARQTG GEAGLHPSNI HDSPYSVGSV
SFTGDEAVIL TCDGPSLGGF VVFCVVASAE MWKLGQLRPG DKVKLQPITV DDALFLESAI
EKSITELTPL AVDVAPLANS PTTPDSNPLL GDIGSAGRRI AVRQAGDNAM LLEFGTEDVF
SLRQSFQIFS FIARHKTHPI PDVLELSPGV RTLHVQYTPK TLPATILSAL RAHEASLGDE
IPSSIPSRTF HLPLAFDDSV SRAAVARYVA TIRATAPWLP SNVDFLQHLN ALDSPADVER
IFLSATFLVL GLGDVFLGSP CAVPLDPRHR LFGTKYNPSR SFTPRGAVGI GGQYMCIYGM
DSPGGYQLVG RTVPIWDDVT ASAVASWGDA KPWLFRLFDR ISFYPVSETD LDAAITQDRM
ADLINIEEGS LDLEEYESWL DANKADIEAT RNLRAEAIRS VPFMEELLQP YNPPEAERRG
VFGEEGEDSV PGERVKAQMP GRCWKCEVKV GDEVEVGDAL VWIESNKMEI KIGSPVRGRV
AKMLVSEGDI VGPYDDLLIV ESQ
//
