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Database: UniProt
Entry: W9XZW5_9EURO
LinkDB: W9XZW5_9EURO
Original site: W9XZW5_9EURO 
ID   W9XZW5_9EURO            Unreviewed;      1240 AA.
AC   W9XZW5;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   08-MAY-2019, entry version 30.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:EXJ82890.1};
GN   ORFNames=A1O3_06706 {ECO:0000313|EMBL:EXJ82890.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ82890.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ82890.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ82890.1,
RC   ECO:0000313|Proteomes:UP000019478};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|SAAS:SAAS00197451};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EXJ82890.1}.
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DR   EMBL; AMGY01000005; EXJ82890.1; -; Genomic_DNA.
DR   RefSeq; XP_007735013.1; XM_007736823.1.
DR   STRING; 43228.XP_007735013.1; -.
DR   EnsemblFungi; EXJ82890; EXJ82890; A1O3_06706.
DR   GeneID; 19170813; -.
DR   OrthoDB; 254436at2759; -.
DR   Proteomes; UP000019478; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 2.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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   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; SSF50891; 2.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234148};
KW   Biotin {ECO:0000256|SAAS:SAAS00296904};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019478};
KW   Ligase {ECO:0000256|SAAS:SAAS00232059};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019478}.
FT   DOMAIN        3    459       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      121    321       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN     1157   1237       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   COILED     1103   1137       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1240 AA;  136255 MW;  B364709DECB8B2D0 CRC64;
     MEKLKTLLVA NRGEIAVRIC RTARELGIKT ISIYTAADAA SAHVGAADEA VLLSGPDAKG
     YIDAEQIVEI AKYKGADAVI PGYGFLSENT DFARHVTESG MVFVGPSPKC IEDFGIKHTA
     RELAAKADVP IVPGTKGLVG SEEEAVAKAK QLGYPVMLKA TAGGGGMGLM ACSDETAVRE
     SFKTVKSRGE TLFKNSGLFI EKYFPAAHHI EVQVFGNALG QAIHFGEREC SIQRRHQKVI
     EECPSPFLAE HPELREKLGS AAVRLAESIN YGSAGTIEYL VDDASADFFF LEMNTRLQVE
     HGITELCYGV DLVELMLKQA DAELCGKGGL DGDYLQSLQP KGPTGAAIEV RVYAENPAKN
     YAPSPGTLQQ VSWKEVPGSR IDGWVHTGTK VTSFYDPLLA KVMVHASDRA EAIKGMTEML
     EGSKIFGPPT NIEFLATILQ DSTFRGGRTI TKFLDTFDYQ PHAIDVLQGG AYTLVEDWPG
     RPTIGKGFSH TGPMDPVAFR VANALVGNPP GKEGLEITLS GPDLRFLGPA IVALCGAPME
     AKLDGEAVSM WTRIKVEAGQ RLTIGKTTGG GCRSYLAIHG GLPSIATWFR SKSTAPMTNV
     GGYQGRALAA GDLLMITKDL PEIQGELKIP DHLIPSYPAE WDLFSMPGPY DAGFITDDSI
     EEFYNSTYTI SHNAARGGIR LLGPKPKWAR PDGGEGGAHP SNVIEYGYPV GTLNWTGDDP
     CLFPVDAPDF GGFVSATTII KADYWRMGQM KAGNKLRFHR ISYQDAMAKR NEVETFLALI
     HDCCHSKAEF GDVSPLKYEG FPPSTESKGW EAALIHQIPE KGNQPLVSYR QGGDDFLLID
     YGHGSFNLNY RCRAVALYRK LKESTGDISF ANGVLQTGMA SGNSLMIYFD SLKVPRQTIL
     EYLLRLEAEL GDLSEAKFPS RKYKLPITFE SQRQRDSLQR YMQTQRPYAA YLPDPMEFLA
     KNNALTKQQL KDIFTKSSLM VVAVGFFVAL PIALPIDPRQ RLQSPKMNPS RVHTPEGQVG
     WGGSCMAIYN VESPGGYMNT GLSIPGADIL GYKKGYNSER PWLFEDFDQI TFYEVSEDEY
     EDLMATFRSG RYEYQYEDTV FDMKEHNTLL RDTKDEVAQI RARQREAQAE MDKLEKELLA
     KWSKEKEANK ISTNTIDQLL HDPEIIVVEA PLNANVWKVE VKEGDTVELE QTVSILEAMK
     LEIPVKTEPS MTGATVEKVL VKPNDVVDAG KPLMLLRKAK
//
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