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Database: UniProt
Entry: D0LNA1_HALO1
LinkDB: D0LNA1_HALO1
Original site: D0LNA1_HALO1 
ID   D0LNA1_HALO1            Unreviewed;       536 AA.
AC   D0LNA1;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding protein {ECO:0000313|EMBL:ACY15278.1};
GN   OrderedLocusNames=Hoch_2750 {ECO:0000313|EMBL:ACY15278.1};
OS   Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Nannocystineae; Kofleriaceae; Haliangium.
OX   NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY15278.1, ECO:0000313|Proteomes:UP000001880};
RN   [1] {ECO:0000313|EMBL:ACY15278.1, ECO:0000313|Proteomes:UP000001880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14365 / JCM 11303 / SMP-2
RC   {ECO:0000313|Proteomes:UP000001880};
RX   PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E.,
RA   Lapidus A., Lucas S., Glavina Del Rio T., Nolan M., Tice H.,
RA   Copeland A., Cheng J.F., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Mavromatis K., Pati A., Mikhailova N., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Brettin T., Rohde M., Goker M., Bristow J., Markowitz V., Eisen J.A.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Haliangium ochraceum type strain (SMP-
RT   2).";
RL   Stand. Genomic Sci. 2:96-106(2010).
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DR   EMBL; CP001804; ACY15278.1; -; Genomic_DNA.
DR   RefSeq; WP_012827886.1; NC_013440.1.
DR   STRING; 502025.Hoch_2750; -.
DR   EnsemblBacteria; ACY15278; ACY15278; Hoch_2750.
DR   KEGG; hoh:Hoch_2750; -.
DR   eggNOG; ENOG4105CER; Bacteria.
DR   eggNOG; COG0439; LUCA.
DR   HOGENOM; HOG000008988; -.
DR   KO; K01961; -.
DR   OMA; LVKWQLM; -.
DR   OrthoDB; 361205at2; -.
DR   BioCyc; HOCH502025:G1GGI-2940-MONOMER; -.
DR   Proteomes; UP000001880; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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|PROSITE-ProRule:PRU00409,
KW   ECO:0000313|EMBL:ACY15278.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001880};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001880}.
FT   DOMAIN       11    461       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      130    331       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   536 AA;  57358 MW;  CF0B324126673315 CRC64;
     MSSSAPPLSR PIRRVLVANR GEIAVRVMRT CRDRGIETVA VFSDADRLAP HVLMADRAHH
     IGPPPARESY LVSERILQAC RDSGADAVHP GYGFLSENDA FAEACEQAGI AFIGPRPEAM
     RTMGSKTRAR AAMIAAGVPV VPGDNGPGEG GFPNAAAALE AARTIGFPVL IKASAGGGGK
     GMRLVEEEGA FEAAFDGARR EAASSFGDDT VYVEKAIIRP RHVEIQVFAD AHGNVVHLGE
     RDCSLQRRHQ KVVEESPSPV VDAGLRSRMG ESAVAAARAC AYVGAGTVEF LLADDGSFYF
     LEMNTRLQVE HPVTEAVYAL DLVSWQLDVA MGERLPLTQE EINARHRGAA IECRVYAEDP
     VRFLPSTGTI THLRVPGGPH VRDDSGVYEG SEISMFYDPM VSKLVVWGED REQALGRMRR
     ALDEYAVRGI QTNLSFHRRV MRHEGFCSGI YDTGFIAREH DTIWADDSAV APATPEGAAE
     GEGEAAAPLP EDLALALGAA AIDRAERAPT VLPKAPAGAG ISAWRLGRAG RGWGAL
//
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