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RPOC1_CARPA
ID   RPOC1_CARPA             Reviewed;         680 AA.
AC   B1A926;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE            Short=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
GN   Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323};
OS   Carica papaya (Papaya).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Caricaceae; Carica.
OX   NCBI_TaxID=3649;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SunUp;
RX   PubMed=18432245; DOI=10.1038/nature06856;
RA   Ming R., Hou S., Feng Y., Yu Q., Dionne-Laporte A., Saw J.H., Senin P.,
RA   Wang W., Ly B.V., Lewis K.L., Salzberg S.L., Feng L., Jones M.R.,
RA   Skelton R.L., Murray J.E., Chen C., Qian W., Shen J., Du P., Eustice M.,
RA   Tong E., Tang H., Lyons E., Paull R.E., Michael T.P., Wall K., Rice D.W.,
RA   Albert H., Wang M.L., Zhu Y.J., Schatz M., Nagarajan N., Acob R.A.,
RA   Guan P., Blas A., Wai C.M., Ackerman C.M., Ren Y., Liu C., Wang J.,
RA   Wang J., Na J.K., Shakirov E.V., Haas B., Thimmapuram J., Nelson D.,
RA   Wang X., Bowers J.E., Gschwend A.R., Delcher A.L., Singh R., Suzuki J.Y.,
RA   Tripathi S., Neupane K., Wei H., Irikura B., Paidi M., Jiang N., Zhang W.,
RA   Presting G., Windsor A., Navajas-Perez R., Torres M.J., Feltus F.A.,
RA   Porter B., Li Y., Burroughs A.M., Luo M.C., Liu L., Christopher D.A.,
RA   Mount S.M., Moore P.H., Sugimura T., Jiang J., Schuler M.A., Friedman V.,
RA   Mitchell-Olds T., Shippen D.E., dePamphilis C.W., Palmer J.D., Freeling M.,
RA   Paterson A.H., Gonsalves D., Wang L., Alam M.;
RT   "The draft genome of the transgenic tropical fruit tree papaya (Carica
RT   papaya Linnaeus).";
RL   Nature 452:991-996(2008).
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_01323}.
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_01323};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
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_01323}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_01323}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR   EMBL; EU431223; ABY86773.1; -; Genomic_DNA.
DR   RefSeq; YP_001671674.1; NC_010323.1.
DR   AlphaFoldDB; B1A926; -.
DR   SMR; B1A926; -.
DR   GeneID; 5878388; -.
DR   KEGG; cpap:5878388; -.
DR   OrthoDB; 774084at2759; -.
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:0000287; F:magnesium ion binding; 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; 1.10.274.100; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR034678; RNApol_RpoC1.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR   SMART; SM00663; RPOLA_N; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..680
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353479"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         493
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ   SEQUENCE   680 AA;  78505 MW;  1035A98E93BB0399 CRC64;
     MIDRYKHQQL RIGLVSPQQI SAWANRILPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI
     FGPIKSGICA CGNYRVIGDE KEDPKFCEQC GVEFVDSRIR RYQMGYIKLA CPVTHVWYLK
     RLPSYIANLL DKPLKELEGL VYCDFSFARP ITKKPTFLRL RGSFEYEIQS WKYSIPLFFT
     TQGFDTFRNR EISTGAGAIR EQLADLDLQI IIDYSFLEWK ELGEEGPTGN EWEDRKIGRR
     KDFLVRRMEL AKHFIRTNIE PEWMVLCLLP VLPPELRPII QIDGGKLMSS DINELYRRVI
     YRNNTLTDLL TTSRSTPGEL VMCQEKLVQE AVDTLLDNGI RGQPMRDGHN KVYKSFSDVI
     EGKEGRFRET LLGKRVDYSG RSVIVVGPSL SLHRCGLPRE IAIELFQTFV IRGLIRQHLA
     SNMGVAKSKI REKEPIIWEI LQEVMQGHPV LLNRAPTLHR LGIQAFQPIL VEGRAICLHP
     LVRKGFNADF DGDQMAVHVP LSLEAQAEAR LLMFSHMNLL SPAIGDPISV PTQDMLMGLY
     VLTSGTRRGI CANRYNPCNR KNYQNERIDD NNYKYTKEPF FCNSYDAIGA YRQKRINLDS
     PLWLRWQLDQ RVIASREAPI EVHYESLGTY HEIYGHYLIV RSVKKEILCI YIRTTVGHIS
     LYREIEEAIQ GFCRACSYDT
 
 
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