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Database: UniProt
Entry: G3JBY5_CORMM
LinkDB: G3JBY5_CORMM
Original site: G3JBY5_CORMM 
ID   G3JBY5_CORMM            Unreviewed;      1215 AA.
AC   G3JBY5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=Urea amidolyase, putative {ECO:0000313|EMBL:EGX93703.1};
GN   ORFNames=CCM_01972 {ECO:0000313|EMBL:EGX93703.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX93703.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX93703.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX93703.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; JH126400; EGX93703.1; -; Genomic_DNA.
DR   RefSeq; XP_006667189.1; XM_006667126.1.
DR   AlphaFoldDB; G3JBY5; -.
DR   STRING; 983644.G3JBY5; -.
DR   GeneID; 18164001; -.
DR   KEGG; cmt:CCM_01972; -.
DR   VEuPathDB; FungiDB:CCM_01972; -.
DR   eggNOG; KOG0238; Eukaryota.
DR   HOGENOM; CLU_002162_0_1_1; -.
DR   InParanoid; G3JBY5; -.
DR   OMA; TLQMWNR; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000001610; 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:0016829; F:lyase 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; 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   NCBIfam; TIGR00724; urea_amlyse_rel; 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; 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; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lyase {ECO:0000313|EMBL:EGX93703.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT   DOMAIN          6..447
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          119..318
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          660..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1215 AA;  131819 MW;  F20599206F433CCB CRC64;
     MSAPTPSKRL LIANRGEIAN RILKTARLLN YCIISIYMPS DASSPHVTDS DVAVPVSSYS
     DINEIVAIVR QQAVEFVIPG YGFLSENAQF AAAVEDAGAV FVGPAPEHIV MFGVKHTARD
     VAAQVGVPIC PGSGIVQSAD EAVLEASRIG YPIMLKATAG GGGMGLKICK DESEVRSSFA
     SVVSRGTALF SNPGVFLERY FPVSRHIEIQ VFGDGRGDCV AFGERECSIQ RRHQKVIEES
     PSPFVAARPA LRQRLVQASR LLASSIRYRS AGTVEYLVDD ATGDFFFLEM NTRLQVEHGI
     TELRFGIDLV ALMLQQAEQP LDLCDLKMLE PSGAAMEARI YAENPGKNYF PSPGQLQLVE
     FSSDPGVRVD TWVQTGTNIS LAFDPLLAKV MVHAETRSCA VSKMRQALDK TKLRGVVTNT
     DYVRRIFETE WFLQGQTTTT VLDSFQYTPR ALEIVAPGSY TTVQDFPGRV GVGFGIPEGG
     PADALHARLA NCVAGNEPGC ELFEITFTGP TILFHGKAII ALAGGVVEAR LDGRPVSMYA
     RIEVPAGSVV TIGRLLQGCR TYLAIQGGLP GIPTYLGSKS TSPIIEVGGH QGRPLVAGDL
     LDIGAPAEFV PFTLPSALVP VLDLKTVYCL SGPHDSPDIM TSSGAEAIYA SEWTVSHQAS
     RTGVRLDGPR PQWARQTGGQ GGSHPSNYLD YPYSLGALNW TGDSAVVFPA DAPSLGGFVT
     SHVIPRAELC KIGQLKPGDQ FRFAQITLQS AMDLYQAQET YIQHVKRLAA GIKTSEALSS
     LKLQAKSLAL STPSTAIIGT HGDVTIRQAG DSYVLVEFLQ SLQLEVRCKV QAVTEAIDNC
     IIDGIHLVTP IGCSLLVQYD GFKICQAQLV DRIQSILGAH GASPLLSNKL SSRHIRLPMV
     FDDKVNRASV ERYMKTQRPT ASYLPDPVEF IARSNGLESK HQVLEKVLST RILVVGVGFW
     SGTPIGFPVD PRCRLMVPKF NPSRTFSPAG GLGIGGCFFC CDPTDAPGGY VNFGRTLPGW
     DKFCVNKSFG KRPWLFENFD QLSFYVVDED EFERIYSRFQ AGKYQFDITP TEFDVVEYTK
     FCESVADETT AFQARQKQAT EIETEKCGRL ARYQWLKEQT VERDAVPALE EIDDALKIDA
     EMHASIYKIK IQKGDTLNNG DIMLILEAMK MEINIAVSAA QAGLVVDSVV VAPGDVVKPG
     DVLVVLARPG EAKTG
//
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