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RPOC2_RHDSA
ID   RPOC2_RHDSA             Reviewed;        1303 AA.
AC   A6MVX2;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 47.
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   Rhodomonas salina (Cryptomonas salina).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Pyrenomonadaceae; Rhodomonas.
OX   NCBI_TaxID=52970;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1319 / NEPCC76 / CS-174;
RX   PubMed=17522086; DOI=10.1093/molbev/msm101;
RA   Khan H., Parks N., Kozera C., Curtis B.A., Parsons B.J., Bowman S.,
RA   Archibald J.M.;
RT   "Plastid genome sequence of the cryptophyte alga Rhodomonas salina
RT   CCMP1319: lateral transfer of putative DNA replication machinery and a test
RT   of chromist plastid phylogeny.";
RL   Mol. Biol. Evol. 24:1832-1842(2007).
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; EF508371; ABO70813.1; -; Genomic_DNA.
DR   RefSeq; YP_001293551.1; NC_009573.1.
DR   AlphaFoldDB; A6MVX2; -.
DR   PRIDE; A6MVX2; -.
DR   GeneID; 5228635; -.
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; 4.
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..1303
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000353588"
FT   BINDING         225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1303 AA;  146349 MW;  24BBB73A193A2794 CRC64;
     MKEKYLFIPP KPKFTNKTID KKELKKLMAW AFSNYGTGRA SYLADKIKDL GFQYATKAGL
     SLSVEDLRVP PTKRELLKRT NEEINLTQQK YERGEITTVE RFQKVIDTWN NASEELKDEV
     VKYFKETDPL NTIYIMAFSG ARGNISQVRQ LVGMRGLMAD PQGQIIDLPI KSNFREGLTV
     TDYIISSYGA RKGLVDTALR TADSGYLTRR LVDVAQDIII REIDCDTDRG ILLKDMVSNN
     QILIPLQNRL LGRVLFETLH SPDSANVIAH INQDLDHNTA EFIVKSGIKS VIVRSPLTCE
     SSRSVCQFCY GWNLAHGSLV DLGEAVGIIA AQSIGEPGTQ LTMRTFHTGG VFTGELAEQI
     RAPFDGVLRI PKSFRTRLIR TRHGEEAFVL EDSYKLDLYD SSYKKHKIEF KQGTILFLND
     NEQFKKSQVI GELSTKSSMI TERVTKDLNT ENSGEVCFSN LYIEEKIDRQ GNSITNTPKG
     GCLWILSGEV YNLPSYADIK IKEKQFVEED EVLATSKVIS DYGGLVRLNQ SNQTSNITEL
     QIVTSSVSLD NATIVTDDQK STNSDPSYTL EMECGIKFHM LCSPGNKIVN SQIIAELIDT
     KYQTSTGGIV KYDGFEVNKK NKNKKGYEIL GEGALLWIPE ETHEINKDIS LLLVEEGQCI
     TAGTQIVKEL YSLTEGYIQI IQENEIVKEV IVKPGKEHVR STTSNNLNEY PKIVKPNDPD
     YAEYNAQGTI YIEELHYKKG NALLIRPVIE FRIDNEKIDL KTNYLTNENH HITIKPTKRV
     LFKDGQRVKS KYGVDLLKTY LIMSVDFDKP HLSADVEFVP AHEDDIYKLH LTVLETLQIK
     QDDFGESKKK STITSLCVKQ NELIKAGSTV AETHLLAHSA GFVQSINQTS QSTCKVLILT
     NSDEKSIDIY NQTPQVSQGD FIRSGDQIAN GIIAETSGQI VEIETNKIKI RSGTPYLVSS
     NAILQVKNGN LVETGDTLAI LVFERSKTGD IVQGLPRIEE ILEARKPKEP SKLSQRPGKI
     TLNYDSEDNK CIRILSSNGE YNEYIMSGIQ KIIVSNGENI LLAEPITDGA PNPHEMLGLF
     FNFYKERMPL YEAAKLALQK VQIYLVNEVQ NVYQSQNVDI SDKHIEVIVR QMTSKVKVED
     GGDTTLLPGE LVELQQIENI NEAMTLTKGL PARYSPVLLG ITKSSLNTDS FISAASFQET
     TRVLTEAAIE GKADWLRGLK ENVIIGRLIP AGTGFNSYND ISKSFVLEKK NQMPDSYEQN
     QNEEQNIEDI ILDDNIARNY ALIENPINNF DTIEQNINQS KDI
 
 
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