RPOC2_TRIV2
ID RPOC2_TRIV2 Reviewed; 1355 AA.
AC Q3M5C8;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Ava_4209;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA23808.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3M5C8; -.
DR SMR; Q3M5C8; -.
DR STRING; 240292.Ava_4209; -.
DR EnsemblBacteria; ABA23808; ABA23808; Ava_4209.
DR KEGG; ava:Ava_4209; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR Proteomes; UP000002533; 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 Transcription; Transferase; Zinc.
FT CHAIN 1..1355
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353520"
FT REGION 1331..1355
FT /note="Disordered"
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 1355 AA; 147515 MW; 988A53AAFC5A4142 CRC64;
MTNEKMIFRN RVVDKGQLRN LISWAFTHYG TARTAVMADK LKDLGFRYAT RAGVSISVDD
LMVPPSKRSL LEAAEEEIRA TEVRYQRGEI TEVERFQKVI DTWNGTSEAL KDEVVTHFKQ
TNPLNSVYMM AFSGARGNIS QVRQLVGMRG LMADPQGEII DLPIKTNFRE GLTVTEYIIS
SYGARKGLVD TALRTADSGY LTRRLVDVSQ DVIIREIDCG TTRGIPVRPM TEGSKTLIKL
STRLLGRVVG EDVIHPKTKE VIAARNTPIS DDLAKEIEKA GVAEVVVRSP LTCEAARSVC
QHCYGWSLAH AKMVDLGEAV GIIAAQSIGE PGTQLTMRTF HTGGVFTGEV AQQVRSKMDG
TIKLPRKLRT RTHRTRHGED ALFVESNGIM ILEPRKEGSE TPAPQEIHVT QGSTIYIVDG
QQVKQGQLLA EVALGGRTTR TNTEKAVKDV ASDLAGEVKF AEVVPEQKTD RQGNTTTTAA
RGGLIWILSG EVYNLPPGAE LVVKNGDRVE TNGVLAETKL TTIHGGVVRL PEATPGKSTR
EIEIITASVV LDQATVTVQS SQGRNNYLIT TGNNQVFNLR ATPGTKVQNG QVVAELIDDR
YRTTTGGFLK FAGVEVQKKG KAKLGYEVVQ GGTLLWIPEE THEVNKDISL LLVEDGQFVE
AGTEVVKDIF CQNSGVVEVT QKNDILREVV VKPGELLMVD DPEAVIGRDN TLLQPGEELL
GQVATELRYI QYVESPEGPA LLSRPVVEFA VPSNPDVPST TSVSQQTGRS IQMRAVQRLP
YKDSERVKSV EGVELLRTQL VLEIEQEGEQ EHNASPLAAD IELIPDPEDA DVQRLQLVIL
ESLVLRRDIA ADATQGSTQT SLEVKDGDTI VPGSVVARTQ ILSKEGGIVR GVQKGSEAVR
RCLVLRHSDM TTLNTSAKPK VKAGDLIVAG TELAPGVFAE ESGQIVAVKN AGESTTTQDA
ALSTQNYAVT IRAGRPYRVS PGAVLQIEDG DLVQRGDNLV LLVFERAKTG DIIQGLPRIE
ELLEARKPKE ACILAKRGGE VKVVYGDGDE AIAIKVIESN GVVTDYPLGP GQNLAMPDGS
VVPAGQPLSD GPSNPHEILE VFFSLGSEDG VYACASHALQ KVQTFLVNEV QMVYQSQGID
IADKHIEVIV RQMTNKVRID DGGDTTMLPG ELVELRQVEQ VNEAMAITGG ARAQYTPVLL
GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGYNTYD
EPGMLEDYST LETTSVLDET DDPLDMVLDD RTARAYNLDS PGLAETGFSN RRSILDDDEL
IADEIHDLVE AEVEVDDEVD DDYEDDDEDD DDYED
