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CPCF_SYNP2
ID   CPCF_SYNP2              Reviewed;         205 AA.
AC   P31968; B1XIU3;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Phycocyanobilin lyase subunit beta;
DE            EC=4.-.-.-;
DE   AltName: Full=Phycocyanin operon protein CpcF;
GN   Name=cpcF; OrderedLocusNames=SYNPCC7002_A2214;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=1644801; DOI=10.1016/s0021-9258(18)41978-3;
RA   Zhou J., Gasparich G.E., Stirewalt V.L., de Lorimier R., Bryant D.A.;
RT   "The cpcE and cpcF genes of Synechococcus sp. PCC 7002. Construction and
RT   phenotypic characterization of interposon mutants.";
RL   J. Biol. Chem. 267:16138-16145(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=1495995; DOI=10.1073/pnas.89.15.7017;
RA   Fairchild C.D., Zhao J., Zhou J., Colson S.E., Bryant D.A., Glazer A.N.;
RT   "Phycocyanin alpha-subunit phycocyanobilin lyase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7017-7021(1992).
CC   -!- FUNCTION: Required for the chromophorylation of the cpcA gene product.
CC   -!- SUBUNIT: CpcE and CpcF associate to form a lyase.
CC   -!- SIMILARITY: Belongs to the CpcE/RpcE/PecE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACB00195.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M93569; AAA27309.1; -; Genomic_DNA.
DR   EMBL; CP000951; ACB00195.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041443591.1; NC_010475.1.
DR   AlphaFoldDB; P31968; -.
DR   SMR; P31968; -.
DR   STRING; 32049.SYNPCC7002_A2214; -.
DR   EnsemblBacteria; ACB00195; ACB00195; SYNPCC7002_A2214.
DR   KEGG; syp:SYNPCC7002_A2214; -.
DR   eggNOG; COG1413; Bacteria.
DR   HOGENOM; CLU_094955_0_0_3; -.
DR   OMA; DYNYGAR; -.
DR   BRENDA; 4.4.1.32; 6187.
DR   Proteomes; UP000001688; Chromosome.
DR   GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   Pfam; PF03130; HEAT_PBS; 2.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Antenna complex; Lyase; Phycobilisome; Reference proteome.
FT   CHAIN           1..205
FT                   /note="Phycocyanobilin lyase subunit beta"
FT                   /id="PRO_0000199280"
SQ   SEQUENCE   205 AA;  22305 MW;  A002E8FACB6B60AB CRC64;
     MTVDVLIRAV NNPTSAQDLV KNVAQLAATK DEQAIPTLVE VLKFNNPGAA VAAVNGLINI
     GEAVVPYLLE NVDGYNYGAR AWMLRIFAGI GDPRALDLLI EAANKDFAFS VRRSAAKGLG
     NIQWHKVPDS EREVQQQKVC DCLFLALEDG EWVVRYGAIA GLEGLSQAIP EARKIVIKNK
     LTEFLTTEPE AAIRARIQKA ILSLP
 
 
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