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RPOC2_SACHY
ID   RPOC2_SACHY             Reviewed;        1534 AA.
AC   Q6L3A5;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324}; OrderedLocusNames=PS108;
OS   Saccharum hybrid (Sugarcane).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Saccharinae; Saccharum;
OC   unclassified Saccharum.
OX   NCBI_TaxID=15819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RC   STRAIN=cv. SP-80-3280;
RX   PubMed=15526204; DOI=10.1007/s00294-004-0542-4;
RA   Calsa T. Jr., Carraro D.M., Benatti M.R., Barbosa A.C., Kitajima J.P.,
RA   Carrer H.;
RT   "Structural features and transcript-editing analysis of sugarcane
RT   (Saccharum officinarum L.) chloroplast genome.";
RL   Curr. Genet. 46:366-373(2004).
RN   [2]
RP   CORRECTION OF EDITING SITE.
RA   Carrer H.;
RL   Unpublished observations (FEB-2006).
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 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:0000255|HAMAP-Rule:MF_01324}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_01324}.
CC   -!- RNA EDITING: Modified_positions=932 {ECO:0000269|PubMed:15526204};
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; AE009947; AAT44687.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q6L3A5; -.
DR   SMR; Q6L3A5; -.
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: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; 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; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR   TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Plastid; RNA editing; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..1534
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067945"
FT   REGION          644..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..666
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..789
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         296
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"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1534 AA;  177061 MW;  2C0370A7AEDB8777 CRC64;
     MAERANLVFH NKEIDGTAIK RLISRLIDHF GMGYTSHILD QIKTLGFHQA TTTSISLGIE
     DLLTIPSKGW LVQDAEQQSF LLEKHYYYGA VHAVEKLRQS VEIWYATSEY LKQEMNSNFR
     ITDPSNPVYL MSFSGARGNA SQVHQLVGMR GLMADPQGQM IDLPIQSNLR EGLSLTEYII
     SCYGARKGVV DTAVRTADAG YLTRRLVEVV QHIIVRRRDC GTIQGISVSP QNGMTEKLFV
     QTLIGRVLAD DIYIGSRCIA SRNQDIGIGL VNRFITAFRA QPFRAQPIYI RTPFTCRSTS
     WICQLCYGRS PTHGDLVELG EAVGIIAGQS IGEPGTQLTL RTFHTGGVFT GGTADLIRSP
     SNGKIQFNED LVHPTRTRHG QPAFLCYIDL HVTIQSQDIL HSVNIPLKSL ILVQNDQYVE
     SEQVIAEIRA GMSTLHFKEK VQKHIYSESD GEMHWSTDVY HAPEYQYGNL RRLPKTSHLW
     ILSVSMCRSS IASFSLHKDQ DQMNTYSFSV DGRYIFDFSM ANDQVSHRLL DTFGKKDREI
     LDYLTPDRIV SNGHWNCFYP SILQDNSDLL AKKRRNRFVV PLQYHQEQEK ERISCLGISM
     EIPFMGVLRR NTIFAYFDDP RYRKDKRGSG IVKFRYRTLE EEYRTQEEEY RTREEEYRTR
     EEEYRTREED SEDEYESPEN KYRTREGEGE YEILEDEYRT LEDEYETLED EYGILEDEYR
     TLEKDSEEEY GSLENKYRTR EGEGEYEILE EDSEEEYGSS EDGSEKEYGT LEEDSEEDSE
     EDSEDEYGSP EENSILKKEG FIEHRGTKEF SLKYQKEVDR FFFILQELHI LPRSSSLKVL
     DNSIIGVDTQ LTKNTRSRLG GLVRVKRKKS HTELKIFSGD IHFPEEADKI LGGSLIPPER
     EKKDSKESKK RKNWVYVQRK KILKSKEKYF VLVRPAVAYE MDEGRNLATL FPQDLLQEED
     NLQLRLVNFI SHENSKLTQR IYHTNSQFVR TCLVVNWEQE EKEGARASLV EVRTNDLIRD
     FLRIELVKST ISYTRRRYDR TSVGLIPNNR LDRNNTNSFY SKAKIQSLSQ HQEVIGTLLN
     RNKEYPSLMI LLASNCSRIG LFKNSKYPNA VKESNPRIPI RDIFGLLGVI VPSISNFSSS
     YYLLTHNQIL LKKYLFLDNL KQTFQVLQGL KYSLIDENKR ISNFDSNIML EPFHLNWHFL
     HHDSWEETLA IIHLGQFICE NLCLFKSHIK KSGQIFIVNM DSFVLRAAKP YLATIGATVH
     GHYGKILYKG DRLVTFIYEK SRSSDITQGL PKVEQIFEAR SIDSLSPNLE RRIEDWNERI
     PRILGVPWGF LIGAELTIAQ SRISLVNKIQ KVYRSQGVQI HNRHIEIIIR QVTSKVRVSE
     DGMSNVFLPG ELIGLLRAER AGRALDESIY YRAILLGITR ASLNTQSFIS EASFQETARV
     LAKAALRGRI DWLKGLKENV VLGGIIPVGT GFQKFVHRSP QDKNLYFEIQ KKNLFASEMR
     DILFLHTELV SSDSDVTNNF YETSETPFTP IYTI
 
 
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