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RPOC_DESPS
ID   RPOC_DESPS              Reviewed;        1349 AA.
AC   Q6AP77;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=DP1118;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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_01322}.
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_01322};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01322};
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR   EMBL; CR522870; CAG35847.1; -; Genomic_DNA.
DR   RefSeq; WP_011188361.1; NC_006138.1.
DR   AlphaFoldDB; Q6AP77; -.
DR   SMR; Q6AP77; -.
DR   STRING; 177439.DP1118; -.
DR   PRIDE; Q6AP77; -.
DR   EnsemblBacteria; CAG35847; CAG35847; DP1118.
DR   KEGG; dps:DP1118; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_7; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000000602; 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; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 2.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
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; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 2.
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   SMART; SM00663; RPOLA_N; 1.
DR   TIGRFAMs; TIGR02386; rpoC_TIGR; 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..1349
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067740"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         801
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         875
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         882
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         885
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1349 AA;  149797 MW;  00057A92A572C7E3 CRC64;
     MEELFNFFQK PKGPVKFNKV KISLASPEQI IDWSHGEVKK PETINYRTFK PERDGLFCAK
     VFGPVKDFEC NCGKYKRMKH RGVVCEKCGV EVIQSKVRRE RLGHISLAAP VAHIWFLKSL
     PSKIGAVLDM TLKQLEKVLY FENYAVTQSE VEELPLGTLL TEEKYRQALS EYPAQFKVGI
     GAEAIRELLA AQDLIGLSRV LREEMASTSS QTKRQKLGKR LFVIEAFRDS GNKPEWMILQ
     VIPVLPPDLR PLVPLEGGRF ATSDLNDLYR RVINRNNRLK RLLELDAPDI IIRNEKRMLQ
     ESVDVLFDNG RRGRVITGAN KRPLKSLSDM LKGKQGRFRQ NLLGKRVDYS GRSVIVVGPH
     LRLHQCGIPK KMALELFKPF IYNRLERKGL VTTIKSARKM VEKGAKEVWD VLEEVVTEYP
     VILNRAPTLH RLGMQAFEAV LIEGKAIRLH PLVCMAFNAD FDGDQMAVHV PLSVEAQVEA
     RVLMMSTNNI LSPANGEPVI IPSQDIVLGL YYMTRERINV KGEGRVFSSV DEAIISYDYK
     ETDLQAKVKV RRPEGIVDTT MGRIILGELV PKSVPFVEVN KVMSKKALAA LIDYTYRHAG
     TKDTVILADR LKDTGYEYAT RAGISICIDD MKIPATKVGL VKKGEDEVLD VEQQYSDGLI
     TAGEKYNKVI DIWSKVSEDV ANEMMDEIKT ETFEDKDGNL VEGPSFNSIF VMADSGARGS
     RDQIRQLAGM RGLMAKPSGA IIETPIKANF REGLDVLEYF ISTHGARKGL ADTALKTANS
     GYLTRRLVDV AQEATIVEAD CQTLDGIVAE PLLDGGEVLV PLGDRILGRV ALEDVVDPFT
     GEVLVVAGEQ MEEDKVAILE EAGIDRVMIR SVLTCRSKRG VCAACYGRDL GRGHLINQGE
     AVGVIAAQSI GEPGTQLTMR TFHIGGTASR SVEQAEIRTH RGGKVAFNNL HYVENSSGVK
     IVMNRNAEIF VKDEFGRDRE KFKVNYGAQV LVKEGEDIER DTVLADWDAY TIPIVAEVGG
     IIRYGDIFNG ITMQEKVDPV TGKSSMVIVH SAGGVTLNPR ISVKNDRGKT LKLPDSEGFA
     RYSLPVGSLI SVEEGAEIKA GTIVGKIPRE TSKTKDITGG LPRVAELFEV RKPKDPAIIA
     RIDGKVSFGK ELKGKRRVVV TPEYGEQQEY LVPKAKHIIV HEGDYVQAGE PLMEGTIVPN
     DILSVLGVKA LAKFLVDEIQ EVYRLQGVKI NDKHIEVIVR QMLKRVHITR ANDSKFMIGE
     NVEWWKFEEE RDRLLAEGKK PGAAEPLLLG VTKASLSTES FISAASFQET TKVLTNAAMS
     GRVDELLGLK ENVIMGRLIS AGTGINRVD
 
 
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