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RPOC1_TETOB
ID   RPOC1_TETOB             Reviewed;        1529 AA.
AC   Q1KVT3;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE            Short=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
GN   Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323};
OS   Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX   NCBI_TaxID=3088;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 393;
RX   PubMed=16638149; DOI=10.1186/1471-2148-6-37;
RA   de Cambiaire J.-C., Otis C., Lemieux C., Turmel M.;
RT   "The complete chloroplast genome sequence of the chlorophycean green alga
RT   Scenedesmus obliquus reveals a compact gene organization and a biased
RT   distribution of genes on the two DNA strands.";
RL   BMC Evol. Biol. 6:37-37(2006).
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_01323}.
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_01323};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
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_01323}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_01323}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01323, ECO:0000305}.
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DR   EMBL; DQ396875; ABD48274.1; -; Genomic_DNA.
DR   RefSeq; YP_635991.1; NC_008101.1.
DR   AlphaFoldDB; Q1KVT3; -.
DR   SMR; Q1KVT3; -.
DR   PRIDE; Q1KVT3; -.
DR   GeneID; 4099810; -.
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:0000287; F:magnesium ion binding; 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; 1.10.274.100; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR034678; RNApol_RpoC1.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 2.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR   SMART; SM00663; RPOLA_N; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..1529
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353515"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         1328
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         1330
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         1332
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ   SEQUENCE   1529 AA;  182051 MW;  7ABC52F2407063F5 CRC64;
     MKNFKNQNFQ KENLNLSFSQ KRKKFSGKIG ICFFEYNFFQ KNFHVQNFPI KKCRLLAQVS
     EQTPQISSFR QTSNFTPNLI KKKLLNGYSK IHELKLVTIE LASPEKIKAW AEKELPNGKI
     FGEVTNANTF HYRTFKPSKG GLFCEHIFGP LKDFECACGK RQRPSALESR KILEHQKTSR
     YFCPNCDVEY TWSIIRRYQL GYIKLNAPVT HLWYFKTNPS YLSILFDMKR RHLESIIYCT
     ETITIENTWK YSQQTSILNR SPKDLYLTWQ KFFTLEEQLQ QYNRIYQNKH QHQKQRKLEF
     RNLSILQNKI SPQINWKNFD QQIVEKNQNN SVFAKNFQTF ENIETFGLKR KHSIFENISM
     QKQKKFGTYF FEEIWKIILQ KSYKNSFLFL NSQECFSEHF FQNIYRISNI FLFSSKKIQK
     FLKFHEIFIF GNTESLNKTI LELKNKKRTV NFFSKDFTPF FIDQNVFESH NSLKIKKQYW
     KSFFFLFEFT RFFLSKKNTK IQNLNVLSKK DFLFLVNLIP FLKKLALFQN LQVFKKNTKK
     SHAFYIQNLS KKNKSLKKKI FLKKNLFTEQ NLISFQNQVQ KNKIFSVEPN FSEKIFSTFF
     SNDFLNSNQT FEFNLFNLFF DVSLNFGKIL AFLKLYYEID FCSFVQKHSF DFEKNYSFKN
     SFSTKQFELF SNQSTLVSMY ETVFFDYFSF FFHFLKIFKF SNFNMSNSVS LEFLNDSEKE
     NIFYSQNFRT QKNFFFSLKA LSFLLVGFNY ENKQNLLSDP FDSGFEIFPN QNSVFMTQNF
     FSSKLFFKEK KQKKNNSKKL KKQLEIFISN KPLLSRQNFT ERKKQIQNKK VQKFFDFDSM
     TENFECSFSS EKKFKLFQKK VSNSSLQLTQ IQKKFKEPFL YKFIKQKNQK KKKFNNFHVF
     LSTKANSNLF FFEKKQKQQI QEKFQKMEKN HFLQNSILTI AYNYLWNNDA DWKYFIYYNS
     LFFYEFEDHP IFLYRSLSPI KDTKNNQAFM FSDTNSSAIK FGQSFSSFLS WSIDDLPKNF
     FVGAGILEKL LTEYTSSELR KMTKQHQILL PKINQMLRFL KQNAKTKKDS LKIQKYFQKR
     EQIIRRLKFL RKFSRRNSNP TFMILKNLPV LPPDLRPILK LQNQIAASDL NRFYQRIIYR
     NDRLKKFAKD SATNQSFEIK YAQRLLQEAV DNLIQNGKGS VKAETNSRGQ PLKSLSEILK
     GKQGRFRQYL LGKRVDYSGR SVIVVGPELK LYECGLPKEM ALELFLPFLI QYILQNKLAQ
     TVVGAKNLLK SDSNLTLHLL HKVIKNIPIL LNRAPTLHRL GFQAFLPKLI EGRAILLHPM
     VCPSFNADFD GDQMAVHIPL TVEARTEAWK FMLATNNLMN SATGEAIILP SQDMVLGCYY
     LTLDFQSKFV GVQLSNLLKK QNSFFPFSKP TYLGKEKTFQ IQGKNFEKFG IQNKAFLLFS
     NFLSVLNAYQ RKEISLHTPV WVKWNSNVDF GNEFSKPVEI RLQINGSWEE IQPKYTTFYN
     YKNKQLQKII RTTPGRILMN FMIQQCSMS
 
 
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