ID U5U8E3_9CHLO Unreviewed; 1498 AA.
AC U5U8E3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324,
GN ECO:0000313|EMBL:AGZ19382.1};
GN ORFNames=CH29B_p112 {ECO:0000313|EMBL:AGZ19382.1};
OS Chlorella sp. ArM0029B.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AGZ19382.1}.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=1415603 {ECO:0000313|EMBL:AGZ19382.1};
RN [1] {ECO:0000313|EMBL:AGZ19382.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ArM0029B {ECO:0000313|EMBL:AGZ19382.1};
RX PubMed=24735464; DOI=10.1186/1471-2164-15-286;
RA Jeong H., Lim J.M., Park J., Sim Y.M., Choi H.G., Lee J., Jeong W.J.;
RT "Plastid and mitochondrion genomic sequences from Arctic Chlorella sp.
RT ArM0029B.";
RL BMC Genomics 15:286-286(2014).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {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 plastids the minimal PEP RNA polymerase catalytic core is
CC composed of four subunits: alpha, beta, beta', and beta''. When a
CC (nuclear-encoded) sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000256|HAMAP-Rule:MF_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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DR EMBL; KF554427; AGZ19382.1; -; Genomic_DNA.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; 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; 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; 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 Chloroplast {ECO:0000313|EMBL:AGZ19382.1};
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};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:AGZ19382.1};
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 115..191
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 195..1390
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT BINDING 243
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 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1498 AA; 170636 MW; 40FBAA6C7FA2DA7A CRC64;
MTNLNKIKST MSSPIPKNDI FWEEKKSSQK IFFNTCFDKN HLKTLIAWFL EQYGEKVTVD
LVETLKQVGF HQATRAGVSL GVDDLKIPPQ KNTLLSQASM KMNAVTNSIQ TGNLTSVEKS
QRLIDTWNQT SETLRQTAVH NFRTTNPVNP VYMMAFSGAR GNISQVRQLV AMRGLMADPQ
GAILEFPIQS NFREGLTVTE YLISCYGARK GLVDTALRTA TSGYLTRRLV DAVQHVVVHV
ADCQSKKGLV IKDKNLEQRL IGRVLFQDIT LDRKTIIKKN TLISHRLAKQ IASKYKEIVV
RSPLTCQTEK SVCQLCYGLD LSQGKLVSIG EAVGILAAQS IGEPGTQLTM RTFHTGGVGV
FSEQAMKSFT APFEGKIEFL DPLSGLFVRT PHGNIVYLLK HKTFHENNPI LKLTSFEPTH
KPTVYEIMHS DVPSGSLLWV KQGECVKSGQ LLLQASRLQT TTQEMPESSH PVRAPLSGEV
FFQSMSIRVV EEEKRIVQKT KKKKQPNGIF SQSNQKEISP KFPTLLELGN FWVFSSFIQK
EATFCNSFFL NGDLVSSETP IQQYNLHFLK IGQLKKVNSF IVFGRNGFDF LFSNIQYSGL
FYFLQEQKEE KNKSNLIGYT SNSKYTVLTW YPFFRKLALP SLGYCSILHF DNDFSGVKNL
EFSESFSPKS KMFPKSIIAS KSQIAPNSDN LGKGTGSGSG TINQKQDITK CQDLNYVWSP
HPVFQLKPNL TLMKLFGKDS GFKQKQFYQS SFVISQTFKS FSKTGIFQFE SKNKLNWILK
TQFDENFSQN FHQNSINNIV SRNSKLFGRG STQSKIYLDF VKKALCFSHK KIFFYSCAKV
IEKKQVWVYV PEMSLTESVS SQLPGILLEP GKKFENLRFN HSYVSTNFIN QKNLVFVKSK
SKNSFFFYSL SNLLEIRSQN PPEFSRIQKD FEKTELTVSQ VWGFNQQIRK IFCFYKQQGN
FDSKIVSFET KRKRRLSHIL FIQKSSHQFV SNTEFLKQNW LFQKKVPADI SIKSPLFTKQ
YKTSNTKFLT NNEISPLFDG FGKVSDFGNA SKQNLKPYLK ILSPSRSGWF SLTSFLRLEL
KFHSSQSFHK TEQLKQNQIL ATSFISGKRF NQHKHLLIKT TNLEHSQTLV VPGFSLFFYQ
GVKLQNSNQF KFLTFRNGWV LPEWKITEAF LTANKLGEFR GAQEKQKQTA FSIFRTQDRT
TIKLLGQQAN NCLSLVEVGT QVRWGQELLT GFAIPVSGQI IKTTLKKVTL RKGIPLLASI
RGLVHISHKD LVEKNDLLIT LRSRRLQTED IVQGIPKIEQ LFEARETQGG EIIQNNMHTL
LNRFFIRARQ VRPIEEAVQV SLMYIQKFLV ENILEAYSNQ GVSIAEKHVE VVVRQMTARV
RITYGGDTGF LPGEFVQLRW IEKMNLALRQ LGRREAHYEP VILGITKSVL QSESFLVAAS
FQQVSKVLVR SALAKKTDFL RGLHENILVG QPIPAGTGMI TLTDSREQTQ ESLDVPNF
//
