ID D3EPB3_ATETH Unreviewed; 1303 AA.
AC D3EPB3;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 OrderedLocusNames=UCYN_05890 {ECO:0000313|EMBL:ADB95313.1};
OS Atelocyanobacterium thalassa (isolate ALOHA).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Atelocyanobacterium;
OC Candidatus Atelocyanobacterium thalassa.
OX NCBI_TaxID=1453429 {ECO:0000313|Proteomes:UP000001405};
RN [1] {ECO:0000313|EMBL:ADB95313.1, ECO:0000313|Proteomes:UP000001405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALOHA {ECO:0000313|Proteomes:UP000001405};
RX PubMed=20173737; DOI=10.1038/nature08786;
RA Tripp H.J., Bench S.R., Turk K.A., Foster R.A., Desany B.A., Niazi F.,
RA Affourtit J.P., Zehr J.P.;
RT "Metabolic streamlining in an open-ocean nitrogen-fixing cyanobacterium.";
RL Nature 464:90-94(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001842; ADB95313.1; -; Genomic_DNA.
DR RefSeq; WP_012953977.1; NC_013771.1.
DR STRING; 1453429.UCYN_05890; -.
DR KEGG; cyu:UCYN_05890; -.
DR PATRIC; fig|713887.8.peg.547; -.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000001405; 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: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; -; 3.
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; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001405};
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..56
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04983"
FT DOMAIN 85..164
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 166..1176
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT REGION 1236..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..108
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1240..1261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1303 AA; 143598 MW; 809D048892B5B444 CRC64;
MTFYNQIVDK RRLKKLIALA FRNYGSAHSS QVADDLKNLG FRYATKAGVS ISIDDLTVPP
AKRGMLQSAE QEISRTEARY ARGEITEVER FQKVIDTWNS TSEELKDEVV RNFRKTDPLN
SVYMMAFSGA RGNMSQVRQL VGMRGLMADP QGQIIDQPIK TNFREGLTVT EYVISSYGAR
KGLVDTALRT ADSGYLTRRL VDVSQDVIVR EIDCGTRRGL MVKAMKDGER VKIALGDRLL
GRVLAEDVIV GNDILAKRNQ AIDAELAAKI GASVEYVIVR SPLTCEAARS VCQSCYGWSL
ATGRFVDLGE AVGIIAAQSI GEPGTQLTMR TFHTGGVFTG EVAEQIKSPS EGIIRWNKGL
SARKVRTRHG EDAFQVEVGG ELNWCSSKND DKSSYSITPG SVLFVADGDS VQKDKMLAEV
TSAKTTCATE RATKDVSTDL AGEVFFASLV SEEKTDRQGN TTHIAQRGGL VWILSGEVYN
FPPGAEPTVS NGDQVVEEDV LAETKLVSMN GGIVRYLSES REIDIITASV SLDKAEIRRE
SSGGHEQYII YTAENQRFLL KATPETKVQN HAVIAELIDN RCETSTGGIL RYGGIEVAKG
SRKTGYEILG GGTLLWVPEE THEVNKDISL LIVEDGQYVE AGTEVVKDIF CQSSGVVEVV
QKNDILREII IKPGEFHLDV DPNEVVLKNE DLVPPGTEVL PGVVSTDLCQ VEWIESTEGQ
GLLLRPVEEY NINHKPKVPS QNSINGKDLE RHIELRTVQK LFYKDGERVK SVDGVHLLNT
QLVLEIETGN DQLSSTLVAD IELKDDDKKD CQRLQLVILE SLTLRRDLDT DPYGGIIKTS
VLVSNGDQIS PGDIVAKTQI RCKENGRIRG IKDGLEAVRR LLVVRNEDIQ VFTLNEEPKV
KENDLVVAGT ELASGVITAE SGLISSINKI SASNYKVTLR LARPYRVSAG AILHVDDGDL
VQRGDNLVLL VYERAKTGDI IQGLPRIEEL LEARKPKEAC ILARKPGVCQ IEYSDNEILS
MKVVEEDGAE TDYPILLNQN VIVSDNQKVD IGEHLTDGPA NPHELLEVFF NHYVDKKGVY
EAALIGLQEA QKFLVDQVQV VYQSQGIDIS DKHIEVIVRQ MTAKVRVDDG GDTTMLPGEL
VELRQIEQVN EAMSITGGAP AMYTPVLLGI TKASLNTDSF ISAASFQETT RVLTEAAIEG
KSDWLRGLKE NVIIGRLIPA GTGFNVHEEM LTGAVDASDD NSDNQHEKES KQNNKYDREH
SNRLLGSTLD KVDENMILDD NIARAYTKAE TPWNIYGKEK DDE
//
