RPOC2_MARPO
ID RPOC2_MARPO Reviewed; 1386 AA.
AC P06274;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=3197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX DOI=10.1038/322572a0;
RA Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT "Chloroplast gene organization deduced from complete sequence of liverwort
RT Marchantia polymorpha chloroplast DNA.";
RL Nature 322:572-574(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2974085; DOI=10.1016/0022-2836(88)90002-2;
RA Umesono K., Inokuchi H., Shiki Y., Takeuchi M., Chang Z., Fukuzawa H.,
RA Kohchi T., Shirai H., Ohyama K., Ozeki H.;
RT "Structure and organization of Marchantia polymorpha chloroplast genome.
RT II. Gene organization of the large single copy region from rps'12 to
RT atpB.";
RL J. Mol. Biol. 203:299-331(1988).
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; X04465; CAA28063.1; -; Genomic_DNA.
DR PIR; A00698; RNLVC2.
DR RefSeq; NP_039277.1; NC_001319.1.
DR AlphaFoldDB; P06274; -.
DR SMR; P06274; -.
DR GeneID; 2702535; -.
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; 1.
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..1386
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067930"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 289
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 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1386 AA; 160156 MW; 18BE458FC1A5C3F9 CRC64;
MAEPVNLIFY NKVMDRTAIK QLISRLIAHF GITYTTHILD QLKTLGFQQA TFGAISLGID
DLLTAPSKSW LIEDAEQYGN LSEKHHNYGS LHAVEKLRQL IETWYATSEY LKQEMNPNFR
ITDPLNPVHM MSFSGARGST SQVHQLVGMR GLMSDPQGQI IDLPIQSNFR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRKVDC GTLYGINVNN LSEKKNNFQQ
KLIGRVIAEN IYIDHRCIAP RNQDIGALLA NRLITLKTKQ IFLRSPLTCK SMNWICQLCY
GWSLSHGNLI EMGEAVGIIA GQSIGEPGTQ LTLRTFHTGG VFTGDIAEHV RTPFNGIIEF
NENFVYPTRT RHGHPAWMCH TNLFLVIKSK NKVHNLTIPP KSLLLVQNNQ YVESKQVIAE
IRAKTSPFKE KVQKYIYSNL EGEMHWSTKV RHASEYIHSN IHLILKTCHI WILSGNFHKK
NNDLSVLFYK NQDKIDFPIS LTKEKNEFSF VKNKTQLNLF LFHFYLYKKN KIFIKSQLTN
NILNKINNSK NYNFILQEYN IKKKKNFYFL KNKNLTCPLF LKIKKNGVLK NNEIFAILDD
PSYKVKNSGI LKYGNIKVDL INQNTNFEDP QTKLFRPRYS IIKEGNFFFI PEEVYVLTQS
LSSVFIKNNK FIQAGTLITS NIRSNTNGLV KIQKKGNNNY ELKILPGTIY YPNETYKISK
QISILIPPGK KLFNEFECKN WTYLQWIMPS KEKPFVLIRP AVEYKISKKL NKSTLFDLLK
KNKKVEIKTI NYLLYEDDEQ IQIINEKNIQ LIQTCLLVHW KKKYFFKEAN VSFLKIKTKN
NFKTFLQISL IEYSNLEKKK EKTISKNVLK KNYYDHFFSI SKNELKNKKQ GVIRIISNQN
NGMQSFIILS SSDLVKTFKF KKLTKNISIK TNTNTSTAKF FEFNKNFKIL NKKKKLNLTK
KNFSIGLLLF KKLGFLGNLH NIVTNSFSSF YLINYTKLIS NKYSIITKFQ HTCQNPKWYL
IDESKKINKL ILGKHINYNL FNWCFPLFSL LKKKIDFQTI KLGQLLFENF VISKYKTSYP
SGQIISININ YFIIRLAKPY LATGGATIHN NYGEFIKEGD TLITLIYERL KSGDIIQGLP
KVEQLLEARP INSVSINLEN GFEDWNNDMI KFIGNLWGFF LSTKISMEQG QINLVDQIQK
VYQSQGVQIS NKHIEIIVRQ MTSKVITLED GMTNVFLPGE LIEFSRTQKM NRALEEAVPY
KPILLGITKA SLNTQSFISE ASFQETTRVL AKAALKGRID WLKGLKENVI LGGLVPAGTG
SQEVIWQITL EKKKEIYLKK KKEFFTKKIN NVFLYQDTFS IFPTTEIIHN VLKESISQNN
KNNFSI
