RPOC1_PROMA
ID RPOC1_PROMA Reviewed; 634 AA.
AC P42076;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DNA-directed RNA polymerase subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
DE Short=RNAP subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=RNA polymerase subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=Transcriptase subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
GN Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323}; Synonyms=rpoC;
GN OrderedLocusNames=Pro_1639;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-244.
RC STRAIN=LG;
RX PubMed=1731224; DOI=10.1038/355265a0;
RA Palenik B., Haselkorn R.;
RT "Multiple evolutionary origins of prochlorophytes, the chlorophyll b-
RT containing prokaryotes.";
RL Nature 355:265-267(1992).
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_01323}.
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_01323};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
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_01323}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR EMBL; AE017126; AAQ00683.1; -; Genomic_DNA.
DR EMBL; Z11160; CAA77511.1; -; Genomic_DNA.
DR PIR; S20585; S20585.
DR RefSeq; NP_876030.1; NC_005042.1.
DR RefSeq; WP_011125789.1; NC_005042.1.
DR AlphaFoldDB; P42076; -.
DR SMR; P42076; -.
DR STRING; 167539.Pro_1639; -.
DR PRIDE; P42076; -.
DR EnsemblBacteria; AAQ00683; AAQ00683; Pro_1639.
DR GeneID; 54200963; -.
DR KEGG; pma:Pro_1639; -.
DR PATRIC; fig|167539.5.peg.1733; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_030022_2_0_3; -.
DR OMA; WGERTLP; -.
DR OrthoDB; 105573at2; -.
DR Proteomes; UP000001420; 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:0000287; F:magnesium ion binding; 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; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR InterPro; IPR012755; DNA-dir_RpoC1_gamma.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR034678; RNApol_RpoC1.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02387; rpoC1_cyan; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..634
FT /note="DNA-directed RNA polymerase subunit gamma"
FT /id="PRO_0000067845"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT CONFLICT 110
FT /note="N -> K (in Ref. 2; CAA77511)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="E -> A (in Ref. 2; CAA77511)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="K -> Q (in Ref. 2; CAA77511)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="V -> I (in Ref. 2; CAA77511)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..208
FT /note="DLQE -> ELPK (in Ref. 2; CAA77511)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="Q -> E (in Ref. 2; CAA77511)"
FT /evidence="ECO:0000305"
FT CONFLICT 218..219
FT /note="TG -> SS (in Ref. 2; CAA77511)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="R -> S (in Ref. 2; CAA77511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 71995 MW; 15A0EA5133742C5B CRC64;
MTNSNLRTEN HFDYVKITLA SPERVMSWGQ RTLPNGQVVG EVTKPETINY RTLKPEMDGL
FCEKIFGPSK DWECHCGKYK RVRHRGIVCE RCGVEVTESR VRRHRMGFIN LAAPVSHVWY
LKGIPSYVAI LLDMPLRDVE QIVYFNCYVV LDEGDHKDLK YKQLLTEDEW LEVEDEIYAE
DSTIENEPVV GIGAEALKQL LEDLDLQEVA EQLREEITGS KGQKRAKLIK RLRVIDNFIA
TNARPEWMVL NAIPVIPPDL RPMVQLDGGR FATSDLNDLY RRVINRNNRL ARLQEILAPE
IIVRNEKRML QEAVDALVDN GRRGRTVVGA NNRALKSLSD IIEGKQGRFR QNLLGKRVDY
SGRSVIVVGP KLKMHQCGLP KEMAIELFQP FVIHRLIRQN IVNNIKAAKK LIQRADDEVM
QVLQEVIEGH PILLNRAPTL HRLGIQAFEP KLVAGRAIQL HPLVCPAFNA DFDGDQMAVH
VPLAIEAQTE ARMLMLASNN ILSPATGEPI VTPSQDMVLG SYYLTALQPD AVKPDFGDQS
KTFAGLEDVI HAFEDKRINL HDWVWVRFNG EVEDDDELTS PLDTQILEDG TQIQQWTYRR
DRLDEEGALI SRFLLTTVGR VVMNNTIIDA VASG
