ID H2CPM7_COLES Unreviewed; 1381 AA.
AC H2CPM7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:AEK48482.1};
OS Colocasia esculenta (Wild taro) (Arum esculentum).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AEK48482.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Aroideae; Colocasieae;
OC Colocasia.
OX NCBI_TaxID=4460 {ECO:0000313|EMBL:AEK48482.1};
RN [1] {ECO:0000313|EMBL:AEK48482.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RR {ECO:0000313|EMBL:AEK48482.1};
RX PubMed=23204304;
RA Ahmed I., Biggs P.J., Matthews P.J., Collins L.J., Hendy M.D.,
RA Lockhart P.J.;
RT "Mutational dynamics of aroid chloroplast genomes.";
RL Genome Biol. Evol. 4:1316-1323(2012).
RN [2] {ECO:0000313|EMBL:AXR93983.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=20A {ECO:0000313|EMBL:AXR93983.1}, 20B
RC {ECO:0000313|EMBL:AXR94067.1}, 20E {ECO:0000313|EMBL:AXR94151.1}, and
RC Colocasia_esculenta_20D {ECO:0000313|EMBL:AXR94901.1};
RX PubMed=29928291; DOI=10.1186/s13007-018-0300-0;
RA Zeng C.X., Hollingsworth P.M., Yang J., He Z.S., Zhang Z.R., Li D.Z.,
RA Yang J.B.;
RT "Genome skimming herbarium specimens for DNA barcoding and phylogenomics.";
RL Plant Methods 14:43-43(2018).
RN [3] {ECO:0000313|EMBL:QYL70553.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhu Q.;
RT "Complete chloroplast genomes of three morphotypes of Colocasia esculenta
RT species: Comparative analysis, positive selection and novel molecular
RT marker development.";
RL Submitted (MAY-2020) 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: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; JN105690; AEK48482.1; -; Genomic_DNA.
DR EMBL; MH394419; AXR93983.1; -; Genomic_DNA.
DR EMBL; MH394420; AXR94067.1; -; Genomic_DNA.
DR EMBL; MH394421; AXR94151.1; -; Genomic_DNA.
DR EMBL; MH394430; AXR94901.1; -; Genomic_DNA.
DR EMBL; MT447084; QYL70553.1; -; 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:AEK48482.1};
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:AEK48482.1};
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 93..157
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 172..388
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1185..1270
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1381 AA; 156452 MW; B5B21D247B753A08 CRC64;
MAERADLVFH NKVIDGAAMK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TATSISLGID
DLLTIPSKGW LVQDAEQQSL ILERHHHYGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
MTDPSNPVHL MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIIVRRTDC GTIRSISVSP RNGMTERIFI
QTLIGRVLAD DIYIGLRCIA ARNQDIGIGL VNRFITFRAQ PIYIRTPFTC RSTSWICQLC
YGRSPTHGDL VELGEAVGII AGQSIGEPGT QLTLRTFHTG GVFTGGTAEH VRAPFNGKIK
FNEDLVHPTR TRHGHPAFLC SIDLYVTIES QDIIHNVNIT PKSLILVQND QYVESEQVIA
EIRAGASTLT FKEKVRKHIY SESEGEMHWS TDVYHAPEYT YGNVHLLPKT SHLWILAVGT
CRSSIVCFSL HKDQDQINVH SFSLEERYIS DLSVTNDPTR HKLFSLDSSS KKKEGALDYS
RPDRSISNGH RNLKYPSILH EYSDFLAKRR RNRLIIPLQY DQEREKELIP RFGVSIEIPI
NGILRRNSIL AYFDDPRYRR NSSGITKYGT VEVDSIVKKE DLIEYRGAKE FSPKYQMKVD
RFFFIPEEVH VLPGSSLIMV RNNSIIGVDT PLTLNTRSRV GGLVRVERKK KSIELKIFSG
DIHFPGETDK ISRHSGILIP PGTGKKNSKE STKLKNWIYV QRITPTKKKY FVSVRPVVTY
EIADGINLAT FFPQDLLQEG DNVQLRVVNY ILYGNGKPIR GLYHTSIQLV RTCLVLDWNH
ERNGSIEGVR ASFVEIRTND LICNFIRIEV VKSPIPYTGK RNCTVSSGLI NHNSNRLDYT
NINPFYSKAK IQSLTKHKGT SGTLLNQNKE CQSLKILLSS NYSRIGPFNG LKYNNATKES
IKADPIIPIR NSLGPLGTVV LKIANFYSSY HLITYNQILL KKYLLLNKFS QTFQVLKYFL
IDENRGISNP DPCSNIILNP FDLNWRFLHH DYCDETSTII SLGQFFCENV CLFKYGSQKK
SGQVLIVHVD YLVIRSAKPY LATPGATVHG HYGEILHEGD TLVTFIYEKS RSGDITQGLP
KVEQVLEVRS IDSISINLEK RVKGWNERIS RILGIPWGFL ISTELTIAQS RISLVNKIQK
VYRSQGVQIH NRHIEIIVRQ VTSKVLVSED GMSNVFSPGE LIGLLRAERA GRVLDEAICY
RAILLGITRA SLNTQSFISE ASFQETARVL AKAALRGRID WLKGLKENVV LGGIIPVGTG
FKKLVHHSKQ HKNIHLEIKK KNLFEGKMRD ILFHHREFLS SCVPNNFYET SEQSLTRFND
S
//
