ID A0YLV3_LYNSP Unreviewed; 1366 AA.
AC A0YLV3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=L8106_05560 {ECO:0000313|EMBL:EAW37865.1};
OS Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX NCBI_TaxID=313612 {ECO:0000313|EMBL:EAW37865.1, ECO:0000313|Proteomes:UP000000737};
RN [1] {ECO:0000313|EMBL:EAW37865.1, ECO:0000313|Proteomes:UP000000737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC8106 {ECO:0000313|Proteomes:UP000000737};
RA Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-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: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:EAW37865.1}.
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DR EMBL; AAVU01000007; EAW37865.1; -; Genomic_DNA.
DR RefSeq; WP_009783457.1; NZ_AAVU01000007.1.
DR eggNOG; COG0086; Bacteria.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000000737; 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; 2.
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:UP000000737};
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 6..61
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04983"
FT DOMAIN 90..168
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 171..396
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1150..1241
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT REGION 547..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..998
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:0000256|HAMAP-Rule:MF_01324"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 306
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"
SQ SEQUENCE 1366 AA; 150164 MW; 16F38EE663665082 CRC64;
MTDNKKIFRN QIIDKKQLKK LISWSFTHYG TARTAQIADV LKDMGFRYAT RAGVSISVED
LQVPPSKRGL LDEAQEEIRR TERRYTKGEI TEVERFQKVV DTWNGTSEAL KDEVVRNFKA
TNPLNSVYMM AFSGARGNIS QVRQLVGMRG LMANPQGEII DLPIKTNFRE GLTVTEYIIS
SYGARKGLVD TALRTADSGY LTRRLVDVAQ DVILREIDCS TEKGIWLRSM TDGERILIPL
QDRLFGRVLG ADVIHPETGE IVSFEGKKAV RNQAICADLA TAIGQSKVKE VFLRSPLTCE
ATRSVCRHCY GWSLAHADMV DLGEAIGIIA AQSIGEPGTQ LTMRTFHTGG VFTAEAAEII
KAPFDGVVHL PKTLRLRAFR TRHGDDSFYI ESNGKITVEN GDRTQSLNVS QGSSLVVKEG
QSVKADQVLV EIPAGGRTAR KTTEKATKDV ATDLAGEVKF ADVVAEEKTD RQGNMTRIAA
RGGLIWILSG EVYNLLPGAE PTVKNGDRVG IDSVLAQTRL VSEHGGIVRI HEREPDTTTP
EVLEPSIPPL AEPTGAGVVT PTTTPKSDLP REIEIITASV LLDQALVRIQ QLQGREQYVI
ETTNNNRFLL KVTPGSKVEN HEVIAELIDD SYRTATGGII KYAGVEVAKR NKAKQGYEVI
QGGTLLWIPE ECHEVNKDIS LLLVEDGQYV EAGTEVVKDI FCQSNGVIEV TQKNDILREI
VIKPGELHLV DDPEMVMAID GKIVNPGEEA IPGIVATELH YIEYVETPEG PALLLRPVTE
FKVPEMPPIP SQESLNESIS LQAVQRLTYK DGERVRSVEG VELLRTQLVI NIGTEAPQLA
ADIELIPHEE DPELMRLQLV ILESLVIRRD IVADATQGST RTRLLVKDGD EIKPGSVVSR
TEILCKETGI VSGIRSGTEI LRRILVVRDA DQMKIDLPPG VTTNVKPGQL VVESSELAPG
VTLPESGEII AVHPGSSGTA EEKSVSEGSE DDSQLAPSGT TQVIMRLGRP YRVSSGAILH
LNDGDLVQRG DNLVLLVFER AKTGDIIQGL PRIEELLEAR KPKEACILAK HPGTAQVNVT
DEIVDLRVME NDGNISEYPL LPGQTVIVSD GQMVEVGQAL TDGPANPHEI LEVFFNYHQH
LEGIYDAALR SFQQCQTFLV NEVQSVYQSQ GIDISDKHIE VIVRQMTSKV RIDDGGDTTM
LPGELVELRQ VEQVNEAMSI TGGAPARYTP MLLGITKASL NTDSFISAAS FQETTRVLTE
AAIEGKSDWL RGLKENVIIG RLIPAGTGFN AYEELGVGDF SLENNDMSYL EDEEMELKDV
VLDDRTARKM DRGDLNDTQE SDELIKDNSL FLDDELIDDD SFEEDK
//
