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Database: UniProt
Entry: J4KN04_BEAB2
LinkDB: J4KN04_BEAB2
Original site: J4KN04_BEAB2 
ID   J4KN04_BEAB2            Unreviewed;      2049 AA.
AC   J4KN04;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:EJP64859.1};
GN   ORFNames=BBA_06034 {ECO:0000313|EMBL:EJP64859.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP64859.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP64859.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP64859.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; JH725166; EJP64859.1; -; Genomic_DNA.
DR   RefSeq; XP_008599353.1; XM_008601131.1.
DR   STRING; 655819.J4KN04; -.
DR   GeneID; 19889046; -.
DR   HOGENOM; CLU_001643_0_0_1; -.
DR   InParanoid; J4KN04; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd12148; fungal_TF_MHR; 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   InterPro; IPR007219; Transcription_factor_dom_fun.
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   Pfam; PF04082; Fungal_trans; 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; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000002762}.
FT   DOMAIN          13..468
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          131..329
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          1430..1451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2049 AA;  222402 MW;  596447CF11FB13C1 CRC64;
     MAPDSSSTEP LRHIRRVLIA NRGEIAVRCI KACKELGVHC ITIFTNADTT SLHAKLADES
     VLLPGDNGTG YTDSASILEI CKRVGADAVI PGYGFLSENA EFADAVTAAG IVFVGPSSAS
     IRAMGLKHEA RAIAVAANVP VIPGTSLLES ADDACVAARA LGFPVMLKAT GGGGGMGLQV
     CHTEQEVTDA FSVVKSRGST LFKNSGVFLE KYYPSSRHVE VQVAGNGEIV VAFGERECSL
     QRRHQKVIEE CPSPFVERHP GMREKMCQAA TNYASRLKYK SVGTVEFLVD DETADFFFLE
     MNTRLQVEHG ITELCYGVDL VHLMLRQADH ERAGRLGLHS DELQRLVKLE PHGWAIEGRV
     YAEVPLRNFA PAPGVLQHVG WAEGDGIRVD TWVSSGQNVT PYYDPLIAKI MVHSPDGRSA
     AQATMLKALN NSALQGTQTN MEYLAKIIAS PMFVNGQTLT NSLSNFHFES CSLQVLDPGV
     LTTLQDYPGR VNVGHGIPPG GPMDDLSARV ANILVGNEPG AELFEITLVG PELLFHEAAV
     VAICGAELLV TLEEQTQPMW SRLIVGKGQI LKLGRVGKDG TRTYLAVKGG FPQVADYLGS
     KSTAPELGIG GVQGRKLQAH DILALDPRSG TWAKQASPLS LPKEGLPIFD SDSATVIRCI
     DGPYGSEDIL SPKGHTTLYE AEWSVSHNSS RSGVRLSGPR LKWARTSGGG GGSHPSNVFD
     YGYPNGGVNF TGESPIIFAH DRPGLGGFAC PTTVCSAEMW KVGQLKTGNK VRFQSISFDD
     ALQLSKSKEG YLQAIKAYSN GGTRTIPSPH VEVAKAPASS ILHQTPASGS HPRVTYRQGG
     DTGIIVEYGE QLPDLRNTAC VYLLLQGLSR AQLPGVRGEP NFATLTVHFN QQSTPRESLL
     ARLIQLDREA GEISGIQIPA RQLRLPVCLD HSSFAESNQR YMENIRPTAA YMPDNVEYLR
     KNNALDSRQD VFDSILKAPW LTVAVGFFVG TPILYPLDPW RVITGQKYNP TRIYTPRGSI
     GLGGSLAAIY PVAAPGGYQL MGRTLGGWDA AGNRPGFSPD KPWLFNQFDL VKFHQVSEEE
     YTKIEQDFDA GRYVFDIVET TINMDQYIAQ FDEAARDPKY QEWKRRKEVA SKEMAELEEK
     LYEEWVEAKR LATADAIEHE GDEESENVAL IKSPVDANVW RVLVKEGDEI QKGQTVAILE
     AMKMEINIIA GDKEAGFVVA GIPQPPGSVL RALRPLKKIW AVGRESPLRR ASFARGHLNA
     RNIWIDIYGR TQGSGPFNVL AVACSPGTSA SSLSPPSLPE NTNDRASAPR FGVAADVALA
     EDSQQNCASP ATDERLPQAL SYLPVDMSPS VEVDWGLHAM QTEAFSLDVL PNEAEVIDNY
     FMGIFHPTNA DMDPLLNTTS LTTVSGALPS TASPDTTSYV QTRTPAITNR NYASSTTPST
     TTPQTAMRQS PSRIPGPLDA MEDVAAANPW TISSSAYARL QTEVNKFSHV LPAPFTLPSR
     PKLSRFIASW MRGYHPHLPF LHIPTANIDT MKPMLVLTLA ATGSFYGFEH TEGYPMYVLA
     KAMITSELEK RRVGATLCLL HGLPQYAELP TDHSASPIRE PAATHHSSPQ PPAFDVELLQ
     ALLVLIMTMS WLDAPFAQEA LAMSSQLSTL TREALSQARL DDDDDANGGS WIDWGKAEER
     RRSIFAAYFT LNIQTICFNV PPQLTNSEMK LLLPCCEAEF RAPNADAWKN SVLNTKPNNT
     RNRDYQDCLA QLLAGKPLEP AAVISEFGNY LLVQSLLMQI YLERQAVSPL LGPSQNLPAA
     TVAVYDRALA AWQQSCWDPA IETTSLDPST SAQGPVAFNA AAVLRLAHVH LGAGLQAHCE
     LLTRDPRALA EAFSPVRNPL LLESAAARAA AAARTTTTKT AVRHAVCALR IPVRVGIAFV
     ARGRTGHWSA QHAISNYACA LLLTHWLDSM ARVVAEHHGG DDDDGGGGLE AEERMLLGAV
     ERLVEETHLE CSLGPKEDGG RPCPGRMRRL SIAALRLWAQ TCKGIQVYEI VHVVGEALSI
     AADSIERGL
//
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