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RPOC2_CARPA
ID   RPOC2_CARPA             Reviewed;        1387 AA.
AC   B1A925;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
OS   Carica papaya (Papaya).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Caricaceae; Carica.
OX   NCBI_TaxID=3649;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SunUp;
RX   PubMed=18432245; DOI=10.1038/nature06856;
RA   Ming R., Hou S., Feng Y., Yu Q., Dionne-Laporte A., Saw J.H., Senin P.,
RA   Wang W., Ly B.V., Lewis K.L., Salzberg S.L., Feng L., Jones M.R.,
RA   Skelton R.L., Murray J.E., Chen C., Qian W., Shen J., Du P., Eustice M.,
RA   Tong E., Tang H., Lyons E., Paull R.E., Michael T.P., Wall K., Rice D.W.,
RA   Albert H., Wang M.L., Zhu Y.J., Schatz M., Nagarajan N., Acob R.A.,
RA   Guan P., Blas A., Wai C.M., Ackerman C.M., Ren Y., Liu C., Wang J.,
RA   Wang J., Na J.K., Shakirov E.V., Haas B., Thimmapuram J., Nelson D.,
RA   Wang X., Bowers J.E., Gschwend A.R., Delcher A.L., Singh R., Suzuki J.Y.,
RA   Tripathi S., Neupane K., Wei H., Irikura B., Paidi M., Jiang N., Zhang W.,
RA   Presting G., Windsor A., Navajas-Perez R., Torres M.J., Feltus F.A.,
RA   Porter B., Li Y., Burroughs A.M., Luo M.C., Liu L., Christopher D.A.,
RA   Mount S.M., Moore P.H., Sugimura T., Jiang J., Schuler M.A., Friedman V.,
RA   Mitchell-Olds T., Shippen D.E., dePamphilis C.W., Palmer J.D., Freeling M.,
RA   Paterson A.H., Gonsalves D., Wang L., Alam M.;
RT   "The draft genome of the transgenic tropical fruit tree papaya (Carica
RT   papaya Linnaeus).";
RL   Nature 452:991-996(2008).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_01324}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01324};
CC   -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC       composed of four subunits: alpha, beta, beta', and beta''. When a
CC       (nuclear-encoded) sigma factor is associated with the core the
CC       holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01324}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_01324}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR   EMBL; EU431223; ABY86772.1; -; Genomic_DNA.
DR   RefSeq; YP_001671673.1; NC_010323.1.
DR   AlphaFoldDB; B1A925; -.
DR   GeneID; 5878449; -.
DR   KEGG; cpap:5878449; -.
DR   OrthoDB; 731145at2759; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
DR   HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR   InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR   TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..1387
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000353550"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1387 AA;  157580 MW;  80CC84B3B23693EE CRC64;
     MAERANLVFH NKVIDGTAIK RLISRLIDRF GMAYTSHILD QVKTLGFQQA TATSISLGID
     DLLTIPSKGW LVQDAEQQSL ILEKHHHYGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
     VTDPFNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
     SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTIRGISVSP KNRTMPERIF
     IQTLIGRVLA DDIYMGPRCI AIRNQDIGIG LVNRFITFRT QSISIRTPFT CRSTSWICRL
     CYGRSPTHGD LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE HVRSPSNGKI
     KFNEDLVHPT RTRHGHPAFL CYIDLSVVIE SEDIIHNVTI PPKSFLLVQN DQYVESEQVI
     AEIRAGTYTL NYKERVRKHI YSNSEGEMHW STDVYHAPEF TYSNVHLLPK TSHLWILSGG
     SSRSSLVPFS LHKDQDQMNI HSLSVEQESI SSLAVNNDQG RHKFFSSNFS DKKKCGIPDY
     SEFHRILDTG HCNLIYFASL HENSDLLAKR RRNRFIIPFQ SIQEQEKELM PRSGISIEIP
     INGIFRRNSI LAFFDDPRYR RKSSGILKYG TIGAHSIVKK EDVIEYRGVK KFKTKYQMKV
     DRFFFIPEEV HILPESSSIM VRNNSIIGVD TRITLNIRSQ VGGLVRVERK KKSIELQIFS
     GDIHFPGKTD KISRHSGILI PPGRGKTNSK ESKKLKNWIY VQRITPTKKK YFVLVRPVAT
     YEIADGINLA TLFPQDLFRE KDNMQLRVVN YILYGNGKPV RGIFDTSIQL VRTCLVLNWD
     QDNKSSSVEE VRTFFVEVST NSLIRDFLRI DLVKSQSHIS YIRKRNDPSG SGLISDNGSD
     RINPFYYKER IQQSLSKNHG TIRTLLNRNK ECQSLIILSS SNCFQMGPFN HVKYHNVIKQ
     SIKKDPLIPI RNSLGPVGTA IQIANFYSIY HLITHNQISV TKYFQLDNLN QIFEVIKYYL
     MDETGRVYNP DPCSNIILNP FNLNWYFLYQ NYHHNYCEET STIISLGQFI CENVCLAKNG
     PHLKSGQVLI VQVDSVVIRS AKPYLATPGA TVHGHYGEIL YEGDTLVTFI YEKSRSGDIT
     QGLPKVEQVL EVRSIDSISL NLEKRVEGWN KRITRILGIP WGFLIGAELT IVQSRISLVN
     KIQKVYRSQG VQIHNRHIEI IVRQITSKVL VSEEGMSNVF LPGELIGLLR AERTGRALEE
     AICYRAILLG ITRASLNTQS FISEASFQET ARVLAKAALR GRIDWLKGLK ENVVLGGMIP
     AGTGFKGLVH CSRQHTSILL ETKKKNLYLF EGEMRDIFFH HRELFDSCIS KNLHNTSERS
     FIGLNDS
 
 
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