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RPOC2_NOSP7
ID   RPOC2_NOSP7             Reviewed;        1349 AA.
AC   B2J1A0;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Npun_F4987;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) 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; CP001037; ACC83331.1; -; Genomic_DNA.
DR   RefSeq; WP_012411286.1; NC_010628.1.
DR   AlphaFoldDB; B2J1A0; -.
DR   SMR; B2J1A0; -.
DR   STRING; 63737.Npun_F4987; -.
DR   EnsemblBacteria; ACC83331; ACC83331; Npun_F4987.
DR   KEGG; npu:Npun_F4987; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
DR   PhylomeDB; B2J1A0; -.
DR   Proteomes; UP000001191; Chromosome.
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; 2.
DR   TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase; Zinc.
FT   CHAIN           1..1349
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353523"
FT   REGION          1298..1349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1320..1349
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         293
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1349 AA;  146861 MW;  6D5F42903199A739 CRC64;
     MTNEKMIFRN RVVDKGQLRN LISWAFTNYG TARTAVMADK LKDLGFRYAT KAGVSISVDD
     LMIPPTKRLL LEAAEEEIRA TETRYQRGEI TEVERFQKVI DTWNGTSEAL KDEVVVHFKK
     TNPLNSVYMM AFSGARGNIS QVRQLVGMRG LMADPQGEII DLPIKTNFRE GLTVTEYIIS
     SYGARKGLVD TALRTADSGY LTRRLVDVSQ DVIIREFDCG TTRGLTIGPM TEGAKTLIPL
     ATRLMGRVIG EDVVHPVTKE LIAARNSPIP EDLAKKIEKS GVGEVVVRSP LTCEAARSVC
     QHCYGWSLAH AKMVDLGEAV GIIAAQSIGE PGTQLTMRTF HTGGVFTGEV AQQVRSKIDG
     TVKLPRKLKT RTYRTRHGED ALYVEANGIM LLEPTKVGDV TPENQEVHLT QGSTLYVFDG
     NKVKQGQLLA EVALGGRTTR TNTEKAVKDV ASDLAGEVQF AEVVPEQKTD RQGNTTTTAA
     RGGLIWILSG EVYNLPPGAE LVVKNGDAIA ANGVLAETKL ASLHGGVVRL PEATPGKSTR
     EIEIITASVV LDQATVTVQS SQGRNNYLVS TGNNQVFNLR ATPGTKVQNG QVVAELIDDR
     YRTTTGGFLK FAGVEVQKKG KAKLGYEVVQ GGTLLWIPEE SHEVNKDISL LLVEDGQFVE
     AGTEVVKDIF CQNSGVVEVT QKNDILREVV VKPGELLMVD DPESVIGRDN TFIQPGEEFQ
     GNVATELRYI QYVETPEGPA LLSRPVVEFA VPDNPDVPST TSVSQQTGRS IQLRAVQRLP
     YKDSERVKSV EGVELLRTQL VLEIEQEGEQ DHNASPLAAD IELVEDTENP EVQRLQLVIL
     ESLVIRRDIT ADATQGSTQT TLEVYDGLTI APGSVVARTQ ILCKEGGEVR GVRKGTENVR
     RCLVLRDVDR LTINTSTQPK VKVGDLLVEG TEVAPGVFAP ESGQVVDIKN AAAASGGESA
     LSTKNYVITT RIGRPYRVSP GAVLQIEDGD LVQRGDNLVL LVFERAKTGD IIQGLPRIEE
     LLEARKPKEA CILCRRGGEV KVVYAESGDE AIAIKVVESN GVVTDYPLGP GQNLIVPDGS
     IVLAGQPLTD GPSNPHEILE IFFSLGSEDG IYACASLALQ KVQTFLVNEV QMVYQSQGID
     ISDKHIEVIV RQMTNKVRID DGGDTTMLPG ELVELRQVEQ VNEAMAITGG ARAQYTPVLL
     GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGYNTYE
     EPGAIDDYAA EISSSVLDEV DDPLDMVLDD RTARTYNLDS PTLGESGFGS RRAERSVLDD
     EDELIADEVV DDDDFEEEEE DDEDDFDDE
 
 
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