ID A0A2T1CU05_9CYAN Unreviewed; 1341 AA.
AC A0A2T1CU05;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
DE Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324};
GN ORFNames=C7B76_22945 {ECO:0000313|EMBL:PSB11729.1};
OS filamentous cyanobacterium CCP2.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107700 {ECO:0000313|EMBL:PSB11729.1, ECO:0000313|Proteomes:UP000239512};
RN [1] {ECO:0000313|EMBL:PSB11729.1, ECO:0000313|Proteomes:UP000239512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP2 {ECO:0000313|EMBL:PSB11729.1,
RC ECO:0000313|Proteomes:UP000239512};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB11729.1, ECO:0000313|Proteomes:UP000239512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP2 {ECO:0000313|EMBL:PSB11729.1,
RC ECO:0000313|Proteomes:UP000239512};
RA Keele B.F.;
RL Submitted (MAR-2018) 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|ARBA:ARBA00004026, 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 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:0000256|ARBA:ARBA00025825,
CC ECO:0000256|HAMAP-Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSB11729.1}.
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DR EMBL; PVWD01000214; PSB11729.1; -; Genomic_DNA.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000239512; Unassembled WGS sequence.
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; 2.40.50.100; -; 2.
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; 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 NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000239512};
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}; Zinc {ECO:0000256|HAMAP-Rule:MF_01324}.
FT DOMAIN 7..70
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04983"
FT DOMAIN 99..177
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 180..544
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1099..1191
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT REGION 1282..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1341
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1341 AA; 147136 MW; A9C46BFF180F12DE CRC64;
MTAEQKTIQK SEKAMLFRNR IINKGQLKNL ITWAFTHYGT ARTAQMADEL KDLGFRFATK
AGVSISVDDL QVPPSKRGLL EAAEDEIKET EARYTRGEIT EVERFQKVID TWNGTSEELK
NEVVRHFKKN NPLNSVYMMA FSGARGNISQ VRQLVGMRGL MANPQGEIID LPIKTNFREG
LTVTEYIISS YGARKGLVDT ALRTADSGYL TRRLVDVSQD VIIRELDCNT ERGVMLRSMT
DGERVLIPLK EKLLGRVAAR DVLHPQTGEV LVARNQSISD DTAKLVADAG VEEVFVRSPL
TCNATRSVCQ LCYGWSLAHA SMVDLGEAVG IIAAQSIGEP GTQLTMRTFH TGGTFTGEVA
PQVRANFDGT VHTKPKQFRS RPFRTRHGED ALVAEVSVEV TVESGSKKES ATVPPGSILF
IRDGQSVKTG QMMVEMASAS RVRKVTEKAT KDVASDLAGE VKFADVVPEE KKDRQGNTTR
IAQRGGLIWI LSGEVYNLPP GAEPVVKNGE QVTSESILAE TKLVTENGGV VRIPQDSETK
SGREIEIITA SVLLDQARVL GESQQGREHY LIETKNNQRF SLIATPGTKV TNGQVVAELI
DDRYHTQTGG IIKYSGVDVA KKGKAKQGYE VVQGGTLLWI PEEAHEVNKD ISLLLVEDGQ
FVEAGTEVVK DIFCQSSGVV EVTQKNDILR EIVIKPGELH LADNPEAVMA KHETIVSPGQ
EAMPGLTVDE LRYVEYVDSP EGPALLLRPV TEFQIPDEPS VPSQESTSED ASRAIRLRAV
QRIPFKDGDR VKSVEGLELL RTQLVLEIDK DAPQLAADIE LVPDETDPDT LRLQLVILES
LVIRRDVSAD QTQGSTLTRL LVQDGDQIAP GAVVARTEIQ CKEAGVVRGI REGGEAIRRI
LVMREADLIR IDTQGKKPIV KDGHLLVSGT EVAPGVSAEE SGQVIDLSDS EVVLRIARPY
RVSAGAVLHI DDGDLVQRGD NLVLLVFERG KTGDIIQGLP RIEELLEARK PKEACILARR
PGTAQVVFGD DESVEVKIIE PDGVTTEYQL LPGQNVMVLD GQEVGVGEPL TDGPANPHEI
LEIYFEYYRE SLGTHEASLK SLQAVQTFLV NEVQSVYQSQ GIDISDKHIE VIVRQMTSKG
RIEDGGDTTM LPGELVELRQ IEQVNEAMSI TGGAPAQYVP MLLGITKASL NTDSFISAAS
FQETTRVLTE AAIEGKSDWL RGLKENVIIG RLIPAGTGFN AYEENNTSVE IDPIYEGTVF
EDDVDLSDVV LDDRTARTYE REGGFDVFPP GMRTPSEPGD FGRGYSLERN DDQEDDDSYS
SPAIIDDDFE DDNDFDDEDE D
//
