ID H2F855_9ASPA Unreviewed; 1382 AA.
AC H2F855;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324,
GN ECO:0000313|EMBL:AEX94838.1};
OS Brodiaea californica.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AEX94838.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC Brodiaeoideae; Brodiaea.
OX NCBI_TaxID=244021 {ECO:0000313|EMBL:AEX94838.1};
RN [1] {ECO:0000313|EMBL:AEX94838.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22291168; DOI=10.3732/ajb.1100491;
RA Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
RA Pires J.C.;
RT "Quality and quantity of data recovered from massively parallel sequencing:
RT Examples in Asparagales and Poaceae.";
RL Am. J. Bot. 99:330-348(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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DR EMBL; JQ275003; AEX94838.1; -; Genomic_DNA.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
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 NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR PANTHER; PTHR48355; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR PANTHER; PTHR48355:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:AEX94838.1};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01324};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01324}; Plastid {ECO:0000313|EMBL:AEX94838.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01324}.
FT DOMAIN 97..161
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 176..368
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1186..1271
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1382 AA; 156772 MW; 560E7AAAC6E71E0B CRC64;
MEVLMAERAD LFFHNKVIDG TAMKRLISRL IDHFGMAYTS HILDQVKTLG FQQATATSIS
LGIDDLLTIP SKGWLVQDAE QQSFILEKHH NYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
PNFRMTDPSN PVHLMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIIVR RTDCGTIRGI SLSPRNGMAG
KIFVQTLIGR VLADDIYTGI RCIATRNQDI GIGLANRFTT FRAQPIYIRT PFTCRNTSWI
CQLCYGRSPT HGDLVELGEA VGIIAGQSIG EPGTQLTLRT FHTGGVFTGG TAEHVRAPSN
GKIKFNEYLV HPTRTRHGHP AFLCSIDLYV TIESRDIIHN VNIPPKSLIL VQNDQHVESE
QVIAEIRAGT STFHFKEKVR KHIYSESEGE MHWSTDVYHA PEYTYSNVHL LPKTSHLWIL
AGGPRRSSRL VSSSLHKDQD QINVHSFSVD EIGISDLSIT NDRVRHKLLL DPSGKKDREI
LDYSRLDRII SNGRWNFIYP SILQESFDFL AKRRRNGFLI PLQYDQEREK ELIPSFGISI
EIPINGILRR NSILAFFDDP RYRRKSSGIT KYGTVEVNSI VKKEDLIEYR GAKEFSPKYQ
MKVDRFFFIP EEVHILPGSS SIMVRNNSII GVDTQLALNT RSRVGGLVRV ERKKKSIELK
IFSGNIHFPG ETDKISRHSG ILIPPGTENS NESKKLKNWI YVQRITPTKK KYFVLVRPVV
TYEIADGINL EKLFPQDLLQ EKDNVQLRVV NYILYGNGKS IRGISQTSIQ LVRTCLVLNW
DQEKNGSIEE VHASFVEVRA NDLIRDFIRI ELVKSIISYT GKRYDTAGSG LIPNNGLDRT
NINPFYSKAR IPLVTQHQGT IATLLNRNKE SQSLIILSSF NCFRVGPFNG SKYNNVTKES
NPRNPIKDLS SLLGTIVPKI VNFYSSYHLI THNQILLNKY WLLDNFKQTF QVLEVLKYCL
IDENRRIYNP GPCNNIILNP FHLNWYFLHH NYCEKTSTII SIGQFICENI CLLKYGLHIK
KSGQILIVHV DSLIIRSAKP YLATPGATVH GHYGETLSEG DTLVTFIYEK SRSGDITQGL
PKVEQILEVR SIGSISMNLE RRVEGWNERI PRILGIPWGF LIGAELTIAQ SRISLVNKIQ
KVYRSQGVQI HNRHIEIIVR QVTSKVLVSE DGMSNVFLPG ELIGLLRAER AGRALDEAIC
YRATLLGITR ASLNTQSFIS EASFQETARV LAKAALRGRI DWLKGLKENV VLGGVIPVGT
GFKKLVHRSK QDKNVYFEIK KKNLFELEMR DILLHHREIF CSCTPSNFYD TSEKSFTQIQ
NS
//
