RPOC2_MORIN
ID RPOC2_MORIN Reviewed; 1389 AA.
AC Q09X27;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 49.
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}; OrderedLocusNames=MoinCp011;
OS Morus indica (Mulberry).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Morus.
OX NCBI_TaxID=248361;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. K2;
RA Ravi V., Khurana J.P., Tyagi A.K., Khurana P.;
RT "The chloroplast genome of mulberry: structural features and comparative
RT analysis.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; DQ226511; ABB20948.1; -; Genomic_DNA.
DR RefSeq; YP_762251.1; NC_008359.1.
DR AlphaFoldDB; Q09X27; -.
DR PRIDE; Q09X27; -.
DR GeneID; 4290594; -.
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..1389
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000277195"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1389 AA; 158034 MW; C92B11A7F40F5510 CRC64;
MEVLMAERAD LVFRNKVIDG TAIKRLISRL IDHFGMAYTS HILDQVKTLG FRQATATSIS
LGIDDLLTIP SKGWLVQDAE QQRLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
PNFRMTDPFN PVHMMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTIQGI SVSPPNGMMP
ERIFIQTLIG RVLADYIYIG SRCIAVRNQD IGIGLVNRFI TFQTQPISIR TPFTCKSTSW
ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
NGKIKFNEDL VHPTRTRHGH PAFLCSIDLY VTIESEDIIH NVTIPPKSFI LVQNDQYVES
EQVIAEIRAG TYTFHFKERV RKHIYSDSEG EMHWSTDVYH APDFTYSNVH LLPKTSHLWI
LSGGSYKSSV VPFSIHKDQD QTNVYFLSAA KGKARNSFSV NNDQDQGKHK FFTSGLSGKK
ESGIPDYSEF NRILDTDHSN LIFPSILHKD SDLFLLAKRR RNRFIIPFQW IQEREKELWP
RSSISIEIPI NGIFRKNSIL AYFDDLQYRR KGSGITKYGA IGLHSILKKE DLIEYGGVKE
FKPKYQTKVD QFFFIPEEVH ILPESFSIMV RNNSIIGVDT RITLNTRSRV GGLVRVEKKN
KRIELKIFSG DIHFPVEMDK IFRHSGILIP PGRVKKEFKE SKKWKNWIYV QSITPTKKKY
FVLVRPVIIY EIADGINLET LFPQDPLQEK DNLELRVVNY ILYGNGKPIL GISGTCIQLV
RTCLVLNWDQ GNKSSSSEET HASFVEVSTR DLIRDFLRIN LVKSHISYIR KRNDPLGSVL
ISDNRSDRTN PFYSIYSKEK IRQLLKENQG TIHTLLNRSK ESQSLIILSS SNCFEMGPFN
DVKHYNVIKE SIKRDPLIPI RNSLGPLGTA CQVANFYYIL KTHNQISVTK NLQLENLKQT
FQVLKYYLMD ENGRIYNSDP CSNILFNPFN LNWHFLHHNY CEKKSTIISL GQFFFENVCI
TKHGPHLKSG QVIIVQIDSV VIRSAKSYLA TPGATVHGHY GEILSEGDTL VTFIYEKSRS
GDITQGLPKV EQVLEVRSID SISMNLEKRV EGWNERITRI LGIPWGFLIG AELTIVQSRI
SLVNKIQKVY RSQGVQIHNR HIEIIVRQIT SKVLVSEDGM SNVFLPGELI GLFRAERTGR
ALKEAICYQA ILLGITKASL NTQSFISEAS FQETARVLAK AALRGRIDWL KGLKENVVLG
GMIPVGTGFK GLVHRSKQHN NIPLETKKKN LFECEMRDIL FHHKELFDFC ISTNIHDTSE
HLFLGFNDS
