RPOC2_NYMAL
ID RPOC2_NYMAL Reviewed; 1401 AA.
AC Q6EW58;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
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 Nymphaea alba (White water-lily) (Castalia alba).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Nymphaeales; Nymphaeaceae; Nymphaea.
OX NCBI_TaxID=34301;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15084683; DOI=10.1093/molbev/msh147;
RA Goremykin V.V., Hirsch-Ernst K.I., Woelfl S., Hellwig F.H.;
RT "The chloroplast genome of Nymphaea alba: whole-genome analyses and the
RT problem of identifying the most basal angiosperm.";
RL Mol. Biol. Evol. 21:1445-1454(2004).
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; AJ627251; CAF28583.1; -; Genomic_DNA.
DR RefSeq; YP_053145.2; NC_006050.1.
DR AlphaFoldDB; Q6EW58; -.
DR PRIDE; Q6EW58; -.
DR GeneID; 2896157; -.
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..1401
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067933"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 294
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"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1401 AA; 157965 MW; A0ADACF050E34875 CRC64;
MEVLMAERAD LVFHNKVIDG TAMKRLISRL IDHFGIAYTS HILDQVKTLG FQQATATSIS
LGIDDLLTTP SKRWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
LNFKMTDPSN PVHIMSYSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYTISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGSTRGI SVSFRKGMTE
RIFIQTLIGR VLANDVYLGL RCIATRNQDI GIGLVNRFMT SRAQPIYIRT PFTCRSASWI
CRLCYGRSPT HGDLVELGEA VGIIAGQSIG EPGTQLTLRT FHTGGVFTGG TAEHVRAPSN
GKIKFNEDLV HPTRTRHGHP AFLCYVDLYV TIESQDIIHS VNIPPKSFLL VQNDQYVESE
QVIAEIRAGT STFHFKERVR KHIYSDSEGE MHWSTGVYHA PEYTHGNVHF LPKTSHLWIL
SGGPCKSSLV PFSLHKDQDQ MNVQSLSVQE RSISDFSVNN NRVKHKLFGS DPLARKGRRI
SDYAAGSERV ISNGDGDFIY PAILRENSYL LAKRRRNRFI IPFQYDPEWE KELTPHSSTS
ITVEIPANGI LRRNSILAYF DDPRYRRSSS GITKYGIIEV DSIVKKEGLV EYRRPKESRP
KYQMKVDRFF VIPEEVHILP GSSSIMVRNN SIIGVDTRIT FNTRSQIGGL VRIEKKKKIE
LKIFSGGIHF PGETDKISRH IGILIPPGAR KKMDKGSKGK NWEGNNWVYV QRITPIKKKY
FVSVRPVVTY EIADGINLVT LFPGDMLQEK DNLRLQVVNY ILYGDGKPIR GISHTSIQLV
RTCLVLNWDQ DKKGSIEKVQ ASSAEVRAND LIRYFIRIDL VKSPILYTGK RNDRSGSVIP
DTGSYCANTN LFSSKVKIKS LSQHQGTVRT FLNRNKEGQS LIVFSSSNCS RINVSKYHNV
TKESIKEKED TPIPILNLLG PLGTVPKIHN FSPSYHSITH NEILLNKYLI LDNKNPKQTF
QLLKYYLVDE NGRISNANPC SDIIFNLFGS CFLPHDYCEG TSTTRIISLG QFICENVCLS
KHGTRIKSGQ VIMVYLDSFI IRSAKPYLAT RGATVHGDYG EIFYEGDTLV TFIYEKSRSG
DITHGLPKVE QVLEVRSIDS ISMNLEKRVE GWNEHITGIL GIPWGFLIGA ELTIAQSRVS
LVNKIQKVYR SQGVQIHNKH IEIIVRQITS KVLVSEDGMS NVFSPGELIG LLRAERAGRA
LEEAICYRAV LLGITRASLN TQSFISEASF QETARVLAKA ALRGRIDWLK GLKENVVLGG
MIPVGTGFKR FVHRSREYNN IPLEIQKKNF FGGEMRDILF HHRELFCSCI PKPKSFHNTS
EQPFYAMGSN PIVHKSGFII S
