RPOC2_HORVU
ID RPOC2_HORVU Reviewed; 1477 AA.
AC A1E9I3;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
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 Hordeum vulgare (Barley).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Morex;
RX PubMed=17534593; DOI=10.1007/s00122-007-0567-4;
RA Saski C., Lee S.-B., Fjellheim S., Guda C., Jansen R.K., Luo H.,
RA Tomkins J., Rognli O.A., Daniell H., Clarke J.L.;
RT "Complete chloroplast genome sequences of Hordeum vulgare, Sorghum bicolor
RT and Agrostis stolonifera, and comparative analyses with other grass
RT genomes.";
RL Theor. Appl. Genet. 115:571-590(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; EF115541; ABK79405.1; -; Genomic_DNA.
DR RefSeq; YP_874645.1; NC_008590.1.
DR AlphaFoldDB; A1E9I3; -.
DR PRIDE; A1E9I3; -.
DR GeneID; 4525122; -.
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..1477
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353563"
FT REGION 617..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..744
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 1477 AA; 169662 MW; 7EFD4AFCFF459826 CRC64;
MAERANLVFH NKEIDGTGMK RLISRLIDHF GMGYTSHILD QLKTLGFYQA 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
SNGKIQFNEN LVHPTRTRHG QPAFLCYIDL HVTIQSQDIL YSVNIPSKSL ILVQNDQYVK
SEQVIAEIRA GTSTLHFKER VQKHIYSESD GEMHWSTDVY HAPEYQYGNL RRLPKTSHLW
ILSVSMCRSS IASFSLHKDQ DQMNTYGKKD REILDYSTSD RIMSNGHWNL IYPSIFQDNS
DLLAKKRRNR FVIPLQYHQE QEKELISCFG ISIEIPFMGV LRRNTIFAYF DDPRYRKDKK
GSGIVKFRYR TLEEEYRTRA EDSEEEYETL EHEYRTREDE YETLEESKYG ILEDEYEYET
LENEYGSPEN KYGNPENEYR TLEKDSEEEY GNPESKYRTQ EDEYGTLEED SEDEYGSPGE
SGEEKYGTLE EDSEEDSEDE YESPEEDSIL KKEGLIEHRG TKEFSLKYQK EVDRFFFILQ
ELHILPRSSS LKILDNSIIG VDTQLTKNTR SGLGGLVRVK RKKSHTELKI FSGDIHFPEE
ADKILGGCLI PPERQKKDSK ESKKKKNWVY VQRKKILKSK EKYFVSVRPT VAYEMDEGRN
LATLFPQDLL QEENNLQIRL VNFIYHENSK LTQRIYHTNS QFVRTCLVVN WEQEEKEKAG
ASLVEVRAND LIRDFLRIEL VKSTISYTRK RYDRTSGGPT PHNRLDRANS NSFYSKAKIE
SLSQHQEAIG TLLNRNKEYQ SLMILSASNC SRIGLFKNSK HPNAIKEWNP RIPILEIFGP
LGAIVASISH FSSSYYLLTH NKILLKKYLF VDNLKQTFQV LQELKYSLID ENKRISNFDS
NIMLDPFLLN CHFVHHDSWE ETLAIIHLGQ FICENVCLFK SHIKKSGQIF SVNMDSFVIR
AAKPYLATTG ATVNGHYGEI LYKGDRLVTF IYEKSRSSDI TQGLPKVEQI FEARSIDSLS
PNLERRIEDW NERIPRILGV PWGFLIGAEL TIAQSRISLV NKIQKVYRSQ GVQIHNRHIE
IIIRQVTSKV RVSEDGMSNV FSPGELIGLL RAERAGRALD ESIYYRAILL GITRASLNTQ
SFISEASFQE TARVLAKAAL RGRIDWLKGL KENVVLGGII PVGTGFQKFV HRSPQDKNLY
FEIKKKNLFA SEMRDFLFLH TELVSSDSDV TNNFYET