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RPOD_XANAC
ID   RPOD_XANAC              Reviewed;         625 AA.
AC   Q8PG33;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=RNA polymerase sigma factor RpoD {ECO:0000255|HAMAP-Rule:MF_00963};
DE   AltName: Full=Sigma-70 {ECO:0000255|HAMAP-Rule:MF_00963};
GN   Name=rpoD {ECO:0000255|HAMAP-Rule:MF_00963}; OrderedLocusNames=XAC3788;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. This sigma factor is the primary sigma factor during
CC       exponential growth. {ECO:0000255|HAMAP-Rule:MF_00963}.
CC   -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core.
CC       {ECO:0000255|HAMAP-Rule:MF_00963}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00963}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00963}.
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DR   EMBL; AE008923; AAM38630.1; -; Genomic_DNA.
DR   RefSeq; WP_005921936.1; NC_003919.1.
DR   AlphaFoldDB; Q8PG33; -.
DR   SMR; Q8PG33; -.
DR   STRING; 190486.XAC3788; -.
DR   EnsemblBacteria; AAM38630; AAM38630; XAC3788.
DR   GeneID; 66912809; -.
DR   KEGG; xac:XAC3788; -.
DR   eggNOG; COG0568; Bacteria.
DR   HOGENOM; CLU_014793_7_2_6; -.
DR   OMA; RDAKKEM; -.
DR   Proteomes; UP000000576; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 2.
DR   Gene3D; 1.10.220.120; -; 1.
DR   HAMAP; MF_00963; Sigma70_RpoD_SigA; 1.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR000943; RNA_pol_sigma70.
DR   InterPro; IPR009042; RNA_pol_sigma70_r1_2.
DR   InterPro; IPR007627; RNA_pol_sigma70_r2.
DR   InterPro; IPR007624; RNA_pol_sigma70_r3.
DR   InterPro; IPR007630; RNA_pol_sigma70_r4.
DR   InterPro; IPR007631; RNA_pol_sigma_70_non-ess.
DR   InterPro; IPR007127; RNA_pol_sigma_70_r1_1.
DR   InterPro; IPR042189; RNA_pol_sigma_70_r1_1_sf.
DR   InterPro; IPR013325; RNA_pol_sigma_r2.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR   InterPro; IPR012760; RNA_pol_sigma_RpoD_C.
DR   InterPro; IPR028630; Sigma70_RpoD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF04546; Sigma70_ner; 1.
DR   Pfam; PF03979; Sigma70_r1_1; 1.
DR   Pfam; PF00140; Sigma70_r1_2; 1.
DR   Pfam; PF04542; Sigma70_r2; 1.
DR   Pfam; PF04539; Sigma70_r3; 1.
DR   Pfam; PF04545; Sigma70_r4; 1.
DR   PRINTS; PR00046; SIGMA70FCT.
DR   SUPFAM; SSF88659; SSF88659; 2.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02393; RpoD_Cterm; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Sigma factor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..625
FT                   /note="RNA polymerase sigma factor RpoD"
FT                   /id="PRO_0000093931"
FT   DNA_BIND        584..603
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   REGION          194..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..460
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   REGION          469..545
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   REGION          558..611
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT   MOTIF           414..417
FT                   /note="Interaction with polymerase core subunit RpoC"
FT   COMPBIAS        197..218
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  70084 MW;  6B7032460884C850 CRC64;
     MANERPAQQS DIKLLISKGL EQGYLTYAEV NDHLPDDLVD PEQIEDIISM INGMGIDVHE
     VAPDAETLLL NDGNTGNREV DDTAAEEAAA ALTALDTEGG RTTDPVRMYM REMGTVELLT
     REGEIAIAKR IEEGLSQVQA ALGVFPLSTE MLLADYEAHK EGKKRLAEIV VGFNDLIEEA
     DAAAAALAAA GPVAVSDDEA VDEDDDEDGD DEAAEEEAGP TGPDPVEVAT RMENLANEYA
     KFKKVYAKNG AEHKLVVKAR EDMAAIFTTL KLPLPLTDAL VTQLRGVVNG IKDHERKVLH
     LATTVARMPR KDFIRSWEGN QTNLEWVEDA LKRKQKWSSA LRDVKDQIIS EQQGSIEMEK
     ANYLTLGEIK EISRAMAYGE AKARKAKKEM VEANLRLVIS IAKKYTNRGL QFLDLIQEGN
     IGLMKAVDKF EYRRGYKFST YATWWIRQAI TRSIADQART IRIPVHMIET INKLNRISRQ
     MLQQFGREAT PEELAKEMDM PEDKIRKVMK IAKEPISMET PIGDDEDSHL GDFIEDTNVE
     SPIDNTTNIN LSETVRDVLA GLTPREAKVL RMRFGIDMNT DHTLEEVGKQ FDVTRERIRQ
     IEAKALRKLR HPSRSEQLRS FLDID
 
 
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