(data stored in SCRATCH zone)

SWISSPROT: C7QHH2_CATAD

ID   C7QHH2_CATAD            Unreviewed;       528 AA.
AC   C7QHH2;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   16-JAN-2019, entry version 53.
DE   SubName: Full=Bilirubin oxidase {ECO:0000313|EMBL:ACU69111.1};
DE            EC=1.3.3.5 {ECO:0000313|EMBL:ACU69111.1};
GN   OrderedLocusNames=Caci_0156 {ECO:0000313|EMBL:ACU69111.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69111.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69111.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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DR   EMBL; CP001700; ACU69111.1; -; Genomic_DNA.
DR   RefSeq; WP_012784406.1; NC_013131.1.
DR   STRING; 479433.Caci_0156; -.
DR   EnsemblBacteria; ACU69111; ACU69111; Caci_0156.
DR   KEGG; cai:Caci_0156; -.
DR   eggNOG; ENOG4105E3B; Bacteria.
DR   eggNOG; COG2132; LUCA.
DR   HOGENOM; HOG000096435; -.
DR   OMA; EDMAMMA; -.
DR   OrthoDB; 971126at2; -.
DR   BioCyc; CACI479433:G1GFP-156-MONOMER; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0047705; F:bilirubin oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   Gene3D; 2.60.40.420; -; 4.
DR   InterPro; IPR011706; Cu-oxidase_2.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 2.
DR   SUPFAM; SSF49503; SSF49503; 3.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
DR   PRODOM; C7QHH2.
DR   SWISS-2DPAGE; C7QHH2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Oxidoreductase {ECO:0000313|EMBL:ACU69111.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     31       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        32    528       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002981644.
FT   DOMAIN       81    144       Plastocyanin-like. {ECO:0000259|Pfam:
FT                                PF07732}.
FT   DOMAIN      167    227       Plastocyanin-like. {ECO:0000259|Pfam:
FT                                PF07732}.
FT   DOMAIN      417    527       Plastocyanin-like. {ECO:0000259|Pfam:
FT                                PF07731}.
SQ   SEQUENCE   528 AA;  56794 MW;  027AE151882B3FE0 CRC64;
     MSGPRLSRRG ALRLFGGAGA VAVLSPTLAG CAKPGNDGIN PGTLSSKAKL PKPFSIPLPI
     LKPLAPDSTD AQGVHYSMTL KQAEVEILPG YRTKIFGYNG TFPGPYLDVH AGTPMVVHQT
     NQLPVPIVTH LHGGLTPPSD DGFPTDLVFP QALADMADPG MAASMAGMDG MPSMKDPLAH
     LTAVQRDYVF PLNQRASTLW YHDHRMDFSG VQVWRGLFGL CVLRDAEDDK LPLPKGEREI
     PLMIADRAFD ADGQLIYPEK DPTLLGKPSM DKSIAAGAQG DVILVNGAPW PYLEVAAVKY
     RLRLLNASNA RRYELKLDGP GGGEFVQVGS DGGLLAAPLT HSTLHMSPAE RFDVVVDFSK
     YPVGSTVTLK NSAASGGPGQ VMQFKVTSHA ADDSSVPATL STIEKLTVNG AKRRLVFALD
     GDQWHVNGKA FDPAHPLVKP EFGKTEQWTV TSVERHPVHL HGAHFQVTGR GSGGLGEYDH
     GWKDTVELSP GSEITLAVRF DSYRGRYVAH CHNLEHEDMG MMATIQVV
//

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