GenomeNet

Database: UniProt
Entry: I3TRJ0_TISMK
LinkDB: I3TRJ0_TISMK
Original site: I3TRJ0_TISMK 
ID   I3TRJ0_TISMK            Unreviewed;       519 AA.
AC   I3TRJ0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000256|HAMAP-Rule:MF_00945};
GN   Name=nusA {ECO:0000256|HAMAP-Rule:MF_00945,
GN   ECO:0000313|EMBL:AFK55378.1};
GN   OrderedLocusNames=TMO_3540 {ECO:0000313|EMBL:AFK55378.1};
OS   Tistrella mobilis (strain KA081020-065).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK55378.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK55378.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK55378.1,
RC   ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
CC   -!- FUNCTION: Participates in both transcription termination and
CC       antitermination. {ECO:0000256|HAMAP-Rule:MF_00945}.
CC   -!- SUBUNIT: Monomer. Binds directly to the core enzyme of the DNA-
CC       dependent RNA polymerase and to nascent RNA. {ECO:0000256|HAMAP-
CC       Rule:MF_00945}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945}.
CC   -!- SIMILARITY: Belongs to the NusA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00945}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003236; AFK55378.1; -; Genomic_DNA.
DR   RefSeq; WP_014747055.1; NC_017956.1.
DR   AlphaFoldDB; I3TRJ0; -.
DR   STRING; 1110502.TMO_3540; -.
DR   KEGG; tmo:TMO_3540; -.
DR   PATRIC; fig|1110502.3.peg.3630; -.
DR   eggNOG; COG0195; Bacteria.
DR   HOGENOM; CLU_029242_1_2_5; -.
DR   Proteomes; UP000005258; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-UniRule.
DR   GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-UniRule.
DR   CDD; cd02134; KH-II_NusA_rpt1; 1.
DR   CDD; cd22529; KH-II_NusA_rpt2; 1.
DR   CDD; cd04455; S1_NusA; 1.
DR   Gene3D; 3.30.300.20; -; 2.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.30.1480.10; NusA, N-terminal domain; 1.
DR   HAMAP; MF_00945_B; NusA_B; 1.
DR   InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR025249; KH_dom_NusA-like.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR030842; NusA_bac.
DR   InterPro; IPR036555; NusA_N_sf.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR013735; TF_NusA_N.
DR   InterPro; IPR010214; Tscrpt_termin_fac_NusA_C_rpt.
DR   InterPro; IPR010213; Tscrpt_termination_fac_NusA.
DR   NCBIfam; TIGR01953; NusA; 1.
DR   NCBIfam; TIGR01954; nusA_Cterm_rpt; 1.
DR   PANTHER; PTHR22648; TRANSCRIPTION TERMINATION FACTOR NUSA; 1.
DR   PANTHER; PTHR22648:SF0; TRANSCRIPTION TERMINATION_ANTITERMINATION PROTEIN NUSA; 1.
DR   Pfam; PF14520; HHH_5; 2.
DR   Pfam; PF13184; KH_5; 1.
DR   Pfam; PF08529; NusA_N; 1.
DR   SMART; SM00322; KH; 2.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 2.
DR   SUPFAM; SSF47794; Rad51 N-terminal domain-like; 2.
DR   SUPFAM; SSF69705; Transcription factor NusA, N-terminal domain; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00945};
KW   Elongation factor {ECO:0000313|EMBL:AFK55378.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:AFK55378.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00945};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00945};
KW   Transcription antitermination {ECO:0000256|ARBA:ARBA00022814,
KW   ECO:0000256|HAMAP-Rule:MF_00945};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00945};
KW   Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW   ECO:0000256|HAMAP-Rule:MF_00945}.
FT   DOMAIN          144..208
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   519 AA;  57689 MW;  63A4B646442B26E9 CRC64;
     MDINFNTGPV RHELLQVADA VAREKSIDRD AVLEAMEQAI QTAGRRKYGQ DHDIRATIDR
     KTGEIRLYRY TQVVDEVEDE ATQMSVADAR HRKPDAAPGD FLVDPLPPID FGRIAAQTAK
     QVIVQKVREA ERQRQFDEFK DRVGEIINGI VKRAEYGSVV VDLGRAEAVM RRDELLPRES
     FRVGDRVRAY IYAVREEPRG PQIFLSRTHP QFMAKLFAQE VPEIYDGIIE IKGCARDPGS
     RAKIAVTSHD SSIDPVGACV GMRGSRVQAV VAELQGEKID IIPWSPDPAT FLVNALAPAE
     VAKVVMDEDT QRIEVVVPDE QLSLAIGRRG QNVRLASQLT GWDIDIVTET EESERRQEEF
     RERSRLFIEA LNVDEVIAQL LVTEGFESIE EIAFVAEDEL SGIEGFDPDV AAELQNRAQI
     FLEARDRQMD DKRRELGVED AVAEIDGMTP VMLASLGEKG IKTLDDLADL AGDELIELLP
     AGTIDEAEAN RIIMAARAHW FEGEDAPEAD AAPAGDSEA
//
DBGET integrated database retrieval system