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Database: UniProt
Entry: A0A261V125_9BORD
LinkDB: A0A261V125_9BORD
Original site: A0A261V125_9BORD 
ID   A0A261V125_9BORD        Unreviewed;      1251 AA.
AC   A0A261V125;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   05-JUN-2019, entry version 5.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:OZI67819.1};
GN   ORFNames=CAL20_01925 {ECO:0000313|EMBL:OZI67819.1};
OS   Bordetella genomosp. 4.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463044 {ECO:0000313|EMBL:OZI67819.1, ECO:0000313|Proteomes:UP000216885};
RN   [1] {ECO:0000313|EMBL:OZI67819.1, ECO:0000313|Proteomes:UP000216885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU9919 {ECO:0000313|EMBL:OZI67819.1,
RC   ECO:0000313|Proteomes:UP000216885};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OZI67819.1}.
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DR   EMBL; NEVQ01000001; OZI67819.1; -; Genomic_DNA.
DR   Proteomes; UP000216885; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 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; IPR014084; Urea_COase.
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   TIGRFAMs; TIGR00724; urea_amlyse_rel; 1.
DR   TIGRFAMs; TIGR02712; urea_carbox; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 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   Complete proteome {ECO:0000313|Proteomes:UP000216885};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216885}.
FT   DOMAIN        1    444       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN     1151   1227       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   REGION      786    817       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A261V125}.
FT   COMPBIAS    786    812       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A261V125}.
SQ   SEQUENCE   1251 AA;  135228 MW;  BAF93BB8A5AB6906 CRC64;
     MFHTVLIANR GEIAVRAIRT LKRLGIKSVA VYSDADRNAA HVRDADVAVA LGGDKASDSY
     LRIDRILEAA QATGAQAIFP GYGFLSESAE FAEACDIAGI AFIGPTAAQL REFGLKHRAR
     ELAAAAHVPM TPGTGLLSDV TEALAKAEDI GYPVMLKSTA GGGGIGLSRC ANADELATAY
     SAVQHQGQTF FRDSGAFLER YVDQARHIEV QIFGDGLGKV VALGERDCSI QRRNQKVIEE
     TPAPGLPTAT REALLRAAVM LGESVSYRSA GTVEFIYDSA RDAFYFLEVN TRLQVEHPVT
     EAVTGLDLIE CMLRVAAGDT LDWAALQRPP SGAAIEVRLY AEDPVRDFQP SPGVLTHVSF
     PAGARVDGWV ETGTEVASFY DPMLAKLIVH GSDRTEALGK LRDALANTQL HGIATNLEFL
     RQITADARFE TGALSTRFLD NFDFQPTAIE ILEAGTYTSV QDYPGRVGYW NIGVPPSGPM
     DDYAFQLANR IIGNAAEAAG LECTLIGPTL KFHTDAVIAL TGAKMDAWLD DQPVAMWQPL
     HVRPGQILVI GRALSGCRSY LAIRNGLDVP SYLGSRSTFA LGQFGGHAGR CLRVGDMLPI
     AQPELPASLT PAPNATPSAL DPALIPDYPT QWQIGVLLGP HGAPDFFTPE SITAFFAADW
     EVHYNSNRLG VRLLGPKPVW TRQDGGEAGL HPSNIHDCEY AIGSVNFTGD SPVILTRDGP
     SLGGFVCPVT IAKAELWKVG QVRPGDRIRF IPLTIEDALA LQAQQEAAIA TLAASTPAVT
     ALVGQSGKSA SPSAAHPMTT ALTSSSSPEL PGDSSPILVR LPAKDSRPLI TYRQAGDSYL
     LLEYGDNVLD LALRMRVHLL MQALTETPVT GILEFSPGVR SLQIQYDSHL ISQHALIERL
     LQIEDTLPDV STLKIPTRVV YLPMAFEDSA TLGAVQRYQE TVRANAPWLP NNVDFIQRIN
     GLESRDDVRR IVFDASYLIL GLGDVYLGAP CAVPIDPRHR LLTSKYNPAR TFTAEGTVGI
     GGVYMCIYGM DSPGGYQLVG RTLPIWNKFL KNPMFQNGEP WLLRFFDQVR FYPVSEDELT
     ALREDFREGR ATLRIEEEDF DFAAHQRFLA EHAADIKAFK ATQQAAFESE VALWQAEESI
     TVEPEITDDT ALALSDTERA VSADLCGNVW KIPVSVGQYV KAGDTLVIVE AMKMELSIKA
     AFNGTITAIR CTQGKPVNSG DMLVVIDTGA IPSLAEEDGN PIDGEIQYAA S
//
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