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RPOC2_NOSS1
ID   RPOC2_NOSS1             Reviewed;        1355 AA.
AC   P22705;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 118.
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=alr1596;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
RX   PubMed=1904436; DOI=10.1128/jb.173.11.3446-3455.1991;
RA   Bergsland K.J., Haselkorn R.;
RT   "Evolutionary relationships among eubacteria, cyanobacteria, and
RT   chloroplasts: evidence from the rpoC1 gene of Anabaena sp. strain PCC
RT   7120.";
RL   J. Bacteriol. 173:3446-3455(1991).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB77962.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000019; BAB77962.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M60831; AAA22034.1; -; Genomic_DNA.
DR   PIR; AF2005; AF2005.
DR   PIR; C42361; C42361.
DR   RefSeq; WP_044521003.1; NZ_RSCN01000041.1.
DR   AlphaFoldDB; P22705; -.
DR   SMR; P22705; -.
DR   STRING; 103690.17135416; -.
DR   EnsemblBacteria; BAB77962; BAB77962; BAB77962.
DR   KEGG; ana:alr1596; -.
DR   eggNOG; COG0086; Bacteria.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
DR   Proteomes; UP000002483; 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..1355
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067902"
FT   REGION          1331..1355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         293
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1355 AA;  147583 MW;  761EE9D92870C961 CRC64;
     MTNEKMIFRN RVVDKGQLRN LISWAFTHYG TARTAVMADK LKDLGFRYAT RAGVSISVDD
     LMVPPSKRSL LEAAEEEIRA TEVRYQRGEI TEVERFQKVI DTWNGTSEAL KDEVVTHFKQ
     TNPLNSVYMM AFSGARGNIS QVRQLVGMRG LMADPQGEII DLPIKTNFRE GLTVTEYIIS
     SYGARKGLVD TALRTADSGY LTRRLVDVSQ DVIIREIDCG TTRGIPVRPM TEGSKTLIKL
     STRLLGRVVG EDVIHPKTKE VIAPRNTPIS DDLAKEIEKA GVAEVVVRSP LTCEAARSVC
     QHCYGWSLAH AKMVDLGEAV GIIAAQSIGE PGTQLTMRTF HTGGVFTGEV AQQVRSKMDG
     TIKLPRKLRT RTHRTRHGED ALFVESNGIM ILEPRKEGSE TPAPQEIHVT QGSTIYIVDG
     QQVKKGQLLA EVALGGRTTR TNTEKAVKDV ASDLAGEVKF AEVVPEQKTD RQGNTTTTAA
     RGGLIWILSG EVYNLPPGAE LVVKNGDRVE TNGVLAETKL TTIHGGVVRL PEATPGKSTR
     EIEIITASVV LDQATVTVQS SQGRNNYLIT TGNNQVFNLR ATPGTKVQNG QVVAELIDDR
     YRTTTGGFLK FAGVEVQKKG KAKLGYEVVQ GGTLLWIPEE THEVNKDISL LLVEDGQYVE
     AGTEVVKDIF CQNSGVVEVT QKNDILREVV VKPGELLMVD DPEAVIGRDN TLLQPGEELL
     GQVATELRYI QYVESPEGPA LLSRPVVEFA VPSNPDVPST TSVSQQTGRS IQMRAVQRLP
     YKDSERVKSV EGVELLRTQL VLEIEQEGEQ EHNASPLAAD IELIPDLEDA DVQRLQLVIL
     ESLVLRRDIA ADATQGSTQT SLEVKDGDTI VPGSVVARTQ ILSKEGGIVR GVQKGSEAVR
     RCLVLRHSDM ATLNISAKPK VKAGDLIVAG TELAPGIFAE ESGQIVGVKN AGESTTTQDA
     ALSTQNYAVT IRAGRPYRVS PGAVLQIEDG DLVQRGDNLV LLVFERAKTG DIIQGLPRIE
     ELLEARKPKE ACILAKRGGE VKVVYGDGDE AIAIKVIESN GVVTDYPLGP GQNLAMPDGS
     VVPAGQPLSD GPSNPHEILE VFFSLGSEDG VYACASHALQ KVQTFLVNEV QMVYQSQGID
     IADKHIEVIV RQMTNKVRID DGGDTTMLPG ELVELRQVEQ VNEAMAITGG ARAQYTPVLL
     GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGYNTYD
     EPGMLEDYST LETTSVLDET DDPLDMVLDD RTARAYNLDS PGLAETGFNN RRSILDDDEL
     IADEIHDLVE AEVEVDDEVD DDYEDDDEDD DDYED
 
 
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