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RPOC2_WHEAT
ID   RPOC2_WHEAT             Reviewed;        1479 AA.
AC   Q9XPS9;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 102.
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   Triticum aestivum (Wheat).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring;
RA   Matsuoka Y., Tsunewaki K., Ohnishi Y.;
RT   "Molecular analysis of a 21.1-kb fragment of wheat chloroplast DNA bearing
RT   RNA polymerase subunit (rpo) genes.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring;
RA   Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T.,
RA   Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., Gojobori T.,
RA   Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., Tsunewaki K.;
RT   "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: complete
RT   sequence and contig clones.";
RL   Plant Mol. Biol. Rep. 18:243-253(2000).
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; AB027572; BAA78042.1; -; Genomic_DNA.
DR   EMBL; AB042240; BAB47026.1; -; Genomic_DNA.
DR   RefSeq; NP_114251.1; NC_002762.1.
DR   AlphaFoldDB; Q9XPS9; -.
DR   STRING; 4565.EPlTAEP00000010025; -.
DR   PRIDE; Q9XPS9; -.
DR   GeneID; 803165; -.
DR   KEGG; taes:803165; -.
DR   eggNOG; ENOG502QPYA; Eukaryota.
DR   HOGENOM; CLU_000524_1_0_1; -.
DR   Proteomes; UP000019116; Chloroplast.
DR   Genevisible; Q9XPS9; TA.
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; Reference proteome; Transcription;
KW   Transferase; Zinc.
FT   CHAIN           1..1479
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067953"
FT   REGION          618..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..706
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..746
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         303
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"
SQ   SEQUENCE   1479 AA;  170045 MW;  4DFB5363CB516FB2 CRC64;
     MAERANLVFH NKEIDGTGMK RLISRLIDHF GMGYTSHILD QLKTLGFHQA TTTSISLGIE
     DLLTIPSKGW LVQDAEQQSF LLEKHYYYGA VHAVEKLRQS VEIWYATSEY LKQEMNSNFR
     ITDPSNPVYL MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
     SCYGARKGVV DTAVRTADAG YLTRRLVEVV QHIIVRRRDC GTIRGISVSP QNGMTEKLFV
     QTLIGRVLAD DIYIGSRCIA ARNQDIGIGL VNRFITAFRA QPFRAQPIYI RTPFTCRSTS
     WICQLCYGRS PTHSDLVELG EAVGIIAGQS IGEPGTQLTL RTFHTGGVFT GGTADLVRSP
     SNGKIKFNEN LVHPTRTRHG QPAFLCYIDL HVTIQSQDIL YSVNIPSKSL ILVQNDQYVK
     SEQVIAEIRA GTSTLHFKER VQKHIYSESD GEMHWSTDVY HAPEYQYGNL RRLPKTSHLW
     ILSVSMCRSS IASFSLHKDQ DQMNTYGKKD REILDYSTSD RIMSNGHWNF IYPSIFQDNS
     DLLAKKRRNR FVIPLQYHQE QEKELISCFG ISIEIPLMGV LRRNTIFAYF DDPRYRKDKK
     GSGIVKFRYR TLEEEYRTRA EDSEEEYETL EDEYRTREDE YEYETLEESK YGILEDEYEY
     ETLEDEYGSP ENEYGNPENE YRTLEKDSEE EYGSPESKYR TQEDEYGTIE EDSEDEYGSP
     GESAEEKYGT LEEDSEEDSE DEYESPEEDS ILKKEGLIEH RGTKEFSLKY QKEVDRFFFI
     LQELHILPRS SSLKILDNSI IGVDTQLTKN TRSRLGGLVR VKRKKSHTEL KIFSGDIHFP
     EEADKILGGC LIPPERQKKD SKESKKRKNW VYVQRKKILK SKEKYFVSVR PTVAYEMDEG
     RNLATLFPQD LLQEENNLQI RLVNFISHEN SKLTQRIYHT NSQFVRTCLV VNWEQEEKEK
     AGASLVEVRA NDLIRDFLRI ELVKSTISYT RKRYDRTSAG PIPHNRLDRA NINSFYSKAK
     IESLSQHPEA IGTLLNRNKE YHSLMILSAS NCSRIGLFKN SKHPNAIKEW NPRIPIREIF
     GPLGAIVASI SHFSSSYYLL THNKILLKKY LFVDNLKQTF QVLQELKYSL IDENKRISNF
     DSNIMLDPFL LNCHFVHHDS WEETLAIIHL GQFICENVCL FKSHIKKSGQ IFIVNMNSFV
     IRAAKPYLAT TGATVNGHYG EILYKGDRLV TFIYEKSRSS DITQGLPKVE QIFEARSIDS
     LSPNLERRIE DWNERIPRIL GVPWGFLIGA ELTIAQSRIS LVNKIQKVYR SQGVQIHNRH
     IEIIIRQVTS KVRVSEDGMS NVFSPGELIG LLRAERAGRA LDESIYYRAI LLGITRASLN
     TQSFISEASF QETARVLAKA ALRGRIDWLK GLKENVVLGG IIPVGTGFQK FVHRSPQDKN
     LYFEIKKKNL FASEMRDFLF LHTELVSSDS DVTNNFYET
 
 
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