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RPOC2_PROMM
ID   RPOC2_PROMM             Reviewed;        1374 AA.
AC   Q7V5P3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324}; OrderedLocusNames=PMT_1505;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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_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:0000255|HAMAP-Rule:MF_01324};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01324}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR   EMBL; BX548175; CAE21680.1; -; Genomic_DNA.
DR   RefSeq; WP_011130873.1; NC_005071.1.
DR   AlphaFoldDB; Q7V5P3; -.
DR   STRING; 74547.PMT_1505; -.
DR   EnsemblBacteria; CAE21680; CAE21680; PMT_1505.
DR   KEGG; pmt:PMT_1505; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
DR   Proteomes; UP000001423; 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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 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   PANTHER; PTHR19376; PTHR19376; 4.
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   TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase; Zinc.
FT   CHAIN           1..1374
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067906"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1344..1374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         258
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         325
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1374 AA;  149538 MW;  BABF9347E67FCC17 CRC64;
     MTSTSPKSRK PSTKTTKSKS KSKSKSKAAK AAAAGASPAL ARTPPQFRNR VIDKKALKQL
     VAWAYKTHGT AVTASMADNL KDLGFRYATQ AAVSISVEDL KVPEAKQDLL GQAEAQITAT
     EECYRLGEIT EVERHTKVID TWTETNERLV DAVKKNFNQN DPLNSVWMMA NSGARGNMSQ
     VRQLVGMRGL MANPQGEIID LPIRTNFREG LTVTEYVISS YGARKGLVDT ALRTADSGYL
     TRRLVDVAQD VIVREDDCGT TRGIIVKAED GGFGSRLVGR LTAEQVVNVD GEILAERNTE
     IDPPLSKRFE KAAITEVMVR SPLTCEANRS VCRKCYGWAL AHNELADLGE AVGIIAAQSI
     GEPGTQLTMR TFHTGGVSTA ETGVVRSTVA GTVEFGPKAR VRGYRTPHGL EAQQSEVDFT
     LTVKPSGKGR AQRIDITTGS LLFVSDGQEI EADVTVVQIA AVAVKKSVEK ATKDVICDLA
     GQVRYEQVIQ PREVKDRQGN ITLKAQRLGR LWVLAGDVYN LPPNAEPVVQ GNVKVERGQV
     LAEASQASEF GGEVRLRDSI GDSREVQIVT TSMTMKDFKL LGESTHSGEL WHLEAKDGTR
     YRLNTIPGSK IGNGEVVAEL ADDRFRTQTG GLVRFAPGLA IKKARSAKNG FEVNKGGTLL
     WIPQETHEIN KDISLLMIED GQWIEAGTEV VKDIFSQTAG IVTVTQKNDI LREIIVRSGS
     FHLCTETKAL ERFTGDGQIV NPGETIAKGI NSEAMVFVQT VDTPEGTGLL LRPMEEYTIP
     NEAQLPELTH VKQPKGPHLG IKATQRLAFK DGELIKSVEG VELLKTQLIL ETFDTTPQMT
     VDVEAVRDKR AKTIERLRLV ILESILVRRD TISDSSHGST HTELQIEDGQ SVKASDVVAT
     TQILCKQEGI AQLPVVQEGD PVRRLIVERD EDTITVTTNG SPLVEVGQRL VDGDSLAKDE
     PSSCCGEVEE VDGKAITLRL GRPYMVSPDS VLHVRDGDLV QRGDGLALLV FERQKTGDIV
     QGLPRIEELL EARRPRESAV LCKKPGTVEI KQGEDDESIT VTVIEADDAI GEYPILLGRN
     VMVSNGQQVH AGELLTDGPI NPHELLDCFF EDLRGRKPLM DAAQEAIAKL QHRLVTEVQN
     VYKSQGVSID DKHIEVIVRQ MTSKVRIEDA GDTTLLPGEL IELRQVEDTN QAMAITGGAP
     SEFTPVLLGI TKASLNTDSF ISAASFQETT RVLTEAAIEG KSDWLRGLKE NVIIGRLIPA
     GTGFSGFQEE LRAEAGPHPD ILAEDPAGYR RMQNLRPDYT VDMPAAPAAS STAVLADPSD
     ADLEATRSRH GIDPAASNFA AFVRPTGENE LEEEQLPDPS ALEGLQQEGL LTEE
 
 
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