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Database: UniProt
Entry: E9FAL7_METRA
LinkDB: E9FAL7_METRA
Original site: E9FAL7_METRA 
ID   E9FAL7_METRA            Unreviewed;      1238 AA.
AC   E9FAL7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   22-FEB-2023, entry version 64.
DE   SubName: Full=Urea amidolyase {ECO:0000313|EMBL:EFY95203.1};
GN   ORFNames=MAA_09279 {ECO:0000313|EMBL:EFY95203.1};
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY95203.1, ECO:0000313|Proteomes:UP000002498};
RN   [1] {ECO:0000313|EMBL:EFY95203.1, ECO:0000313|Proteomes:UP000002498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2] {ECO:0000313|EMBL:EFY95203.1, ECO:0000313|Proteomes:UP000002498}
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:EFY95203.1}.
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DR   EMBL; ADNJ02000003; EFY95203.1; -; Genomic_DNA.
DR   RefSeq; XP_007825468.1; XM_007827277.1.
DR   AlphaFoldDB; E9FAL7; -.
DR   GeneID; 19263565; -.
DR   KEGG; maj:MAA_09279; -.
DR   HOGENOM; CLU_002162_0_3_1; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000002498; 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   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; 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, 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:EFY95203.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          11..466
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          129..327
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1153..1235
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1238 AA;  133978 MW;  D181674010D57C59 CRC64;
     MGSIKVTSLR NIRKVLIANR GEIAVRCIKA CREVQVHSVA IFTHADATSL HVTLADEAVL
     LPGDDGTAYT DGEAILDICK KTDADAVFPG YGFLSENAEF ARAVSSAGII FVGPSSASIK
     AMGLKHEARA IAEAANVPVV PGTQLLSSAA EVVKAARDLG FPVMLKATGG GGGMGLQACD
     TEIEVEKAFA TVQSRASTLF KNSGVFLEKY YPRSRHIEVQ VAGNGEIVIA FGERECSLQR
     RHQKVIEECP SPFVERHSGL RERMLQAAIN YAARLKYKSV GTVEFLVDDE TADFFFLEMN
     TRLQVEHGIT ELCYGVDLVH LMLLQADYER GGHVGIPSDI LRGLQRHSPR GSAIEARVYA
     EVPLREFAPS PGILQLVHWP QGDGVRVDTW VRSGQRITPL YDPLIGKIMV HNPDGRGAAQ
     SKMLAALRDT TLQGTQSNLE YLISIVASNI FINGRTLTNS LSMFKFKSCS LQVLDPGVMT
     TIQDYPGRTA VGHGVPPGGP MDDLSARVAN SLVGNDWGVE LLEITLAGPE LLFHEAAVVA
     ICGAELPVTV DGTPQPMWSR VIVSKDQILK LGKVSGSGTR TYLAVKGGFP QIPKFLGSKS
     TAPELGFGGL QGRKLQAHDI LALAEESGIW AAAAAPLSLP AKAVPDFSIT SVGCLDGPFG
     SDDILTPEGR KTLYEAQWAV SHNSGRSGVR LEGPRLKWAR TSGGGGGSHP SNVLDYGYPN
     GGVNFTGESP IIFAHDRPDL GGFACPTTLC SAEMWKVGQL KAGNTIQLRS VSYDTALEIT
     RKKEEYLGAI ILYAQGSACQ IPPLDVELSD EPPCSILHQT PPLGSHPRVT YRQGGDTSII
     VEYGHQLPDL RNTACVQLLA NGLLAANLDG VRGDPNFATL TVRFDPLLTE RSKLLAHLIH
     LDGQIGETTG IKIAARQVRL PVCLDHTSLR ESAQRYMENI RPSAAYMPDN VEYLRKNNAL
     NDRRDVFDAI LKAPWLTVAV GFYVGTPVMF PLDPWRVLTG QKYNPSRVYT PGGSVGLGGS
     LVAIYPVAAP GGYQLMGRTL GGWDSGGNRP GFSPEKPWLF NHFDLVTFYE VSEEEYNKME
     QAFETGRYIF DITETTIDMD IYIARFDQAA KDPEYQAWRR RQVAASQEMG ELEQKLFEEW
     TQAKSSGEGG SSFEDDGVDS GKVVLIESPV DANVWKVLVK QGDVLEKGQT VAVLEAMKME
     INVVVSDDQA GAVVYTISQP PGSVVRPGAV VVRAVRPE
//
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