ID   RPOC2_TRIEI             Reviewed;        1415 AA.
AC   Q110H3;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324}; OrderedLocusNames=Tery_2937;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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: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 cyanobacteria the RNAP catalytic core is composed of 2
CC       alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC       factor is associated with the core the holoenzyme is formed, which can
CC       initiate transcription. {ECO:0000255|HAMAP-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; CP000393; ABG52101.1; -; Genomic_DNA.
DR   RefSeq; WP_011612459.1; NC_008312.1.
DR   AlphaFoldDB; Q110H3; -.
DR   STRING; 203124.Tery_2937; -.
DR   EnsemblBacteria; ABG52101; ABG52101; Tery_2937.
DR   KEGG; ter:Tery_2937; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
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; IPR007066; RNA_pol_Rpb1_3.
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; 4.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   TIGRFAMs; TIGR02388; rpoC2_cyan; 2.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Transcription; Transferase; Zinc.
FT   CHAIN           1..1415
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353541"
FT   REGION          1335..1390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1335..1355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1415 AA;  155548 MW;  3A899BF343C18284 CRC64;
     MIFYNRVINK GQLKKLISWS FNNYGTAITA QMANKLKDLG FRYATKAGVS ISVDDLQVPP
     SKRQLLDEAE QEIRNTTERY TKGKITEVER FQKVIDTWNS TSENLKNEVV RNFRSTDPLN
     SVYMMAFSGA RGNISQVRQL VGMRGLMADP QGEIIDLPIK TNFREGLTVT EYIISSYGAR
     KGLVDTALRT ADSGYLTRRL VDVSQDVIVR EADCGTKRGV MVTSMKDGDR VLIPVKDRLL
     GRVLADDVKD PKTGEIVTQG HIQAVKNQVL TEDLAKAIGK AGVENVFVRS PLTCESPRSV
     CQTCYGWSLA HGHMVDMGEA IGIIAAQSIG EPGTQLTMRT FHTGGVFTGE VARQFVASFG
     GVVKYPSNVR TRSFRTRHGD EAMIAENNFD MIILGVDGRK ETIPIAQGSI LMVQNNQQVS
     AGIVLAEVPK VGQVRKTTEK VTKEVASDLA GELKFAQLVQ EEKVDKQGTT TRIAQRGGLI
     WILEGEVYNL PPGAEAMVKN GTRININSVL AETKLVTEHG GVIRISSSPL YSPEKQNETN
     VLAQATQEST IDELEASMTG TSAQLPINTE MPDNLPREIE VITASVRLDQ AKVRLESISN
     REQYIIETQN DQRFALKVTP GSKVGNHEVI AELLDENYQT STGGIIKYAG VEVLKRGKAK
     QGYEVVKGGT LLWIPEECHE VNKDISLLLV EDGQYVEAGT EIVKDIFCQS NGVTEVHQKN
     DILREVVIKP GKLHSGNYEI DLGDLTLMDG QIATPGEEVI PGLVTSELKY IEYIETPEGP
     GLLLRPVTEF HVPDEPGVPS QKSINSSIEL RAVQRIPFKD GERVKSVEGI ELLRTQLVLE
     IGEEAPQLAA DIELLPDLEE EGIMRLQLVI LESLVIRRDV VADTTQGSTS TRLLVKDGDV
     IEAGGVVSRT QILSKKSGEV RGIREGSEAI RRILIVREAD LVKIPVNTLP SVVEGDLLVA
     GTEIAPGIVI PRSGLVSKVE ETVLNDGSKG YQVILRKGRP YRVSTGAVLL TMDGDLVQRG
     DILVLLVFER TKTGDIIQGL PRIEELLEAR KPKESCILVK YPGQAQVNVN DDNVEVSVVS
     SDGTITDYPL GHGQNVIVAD GQNVNVGEAL TDGPQNPHEI LETFFNYYRE HESAYEACLR
     SFEACQRFLV NQVQAVYQSQ GIDISDKHIE VIVRQMTAKV RIDDGGDTTM LPGELIELRQ
     VEQVNEAMSI TGGATAQYTP MLLGITKASL NTDSFISAAS FQETTRVLTE AAIEGKSDWL
     RGLKENVIIG RLIPAGTGFN AYEDALSAEI NRLEQNWDDD LDIFEEGDLQ SVVLDDQTAR
     SLEFENSLNL SSANQNFVDS QGKPQSQSSF IDDSMSEFSP VKDKSGSVLD DSDFPPGNFD
     SDFPADNYDL EHEIDLEDDV YDGYDDFDEN TPDLI