(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWL2_RUEPO

ID   Q5LWL2_RUEPO            Unreviewed;       541 AA.
AC   Q5LWL2;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 100.
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:AAV93394.1};
GN   OrderedLocusNames=SPO0063 {ECO:0000313|EMBL:AAV93394.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93394.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93394.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93394.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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}.
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DR   EMBL; CP000031; AAV93394.1; -; Genomic_DNA.
DR   RefSeq; WP_011045836.1; NC_003911.12.
DR   STRING; 246200.SPO0063; -.
DR   EnsemblBacteria; AAV93394; AAV93394; SPO0063.
DR   KEGG; sil:SPO0063; -.
DR   eggNOG; ENOG4105CHV; Bacteria.
DR   eggNOG; COG0195; LUCA.
DR   HOGENOM; HOG000006394; -.
DR   KO; K02600; -.
DR   OMA; SRTTPKM; -.
DR   OrthoDB; 384865at2; -.
DR   BioCyc; RPOM246200:G1G48-64-MONOMER; -.
DR   Proteomes; UP000001023; 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:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-UniRule.
DR   GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1480.10; -; 1.
DR   Gene3D; 3.30.300.20; -; 2.
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; IPR022967; S1_dom.
DR   InterPro; IPR013735; TF_NusA_N.
DR   InterPro; IPR010214; Tscrpt_termin_fac_NusA_C_rpt.
DR   InterPro; IPR010213; Tscrpt_termination_fac_NusA.
DR   PANTHER; PTHR22648; PTHR22648; 1.
DR   Pfam; PF13184; KH_5; 1.
DR   Pfam; PF08529; NusA_N; 1.
DR   SMART; SM00322; KH; 2.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF47794; SSF47794; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54814; SSF54814; 2.
DR   SUPFAM; SSF69705; SSF69705; 1.
DR   TIGRFAMs; TIGR01953; NusA; 1.
DR   TIGRFAMs; TIGR01954; nusA_Cterm_rpt; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWL2.
DR   SWISS-2DPAGE; Q5LWL2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00945};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00945};
KW   Transcription antitermination {ECO:0000256|HAMAP-Rule:MF_00945};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00945};
KW   Transcription termination {ECO:0000256|HAMAP-Rule:MF_00945}.
FT   DOMAIN      141    207       S1. {ECO:0000259|SMART:SM00316}.
FT   DOMAIN      237    310       KH. {ECO:0000259|SMART:SM00322}.
FT   DOMAIN      311    426       KH. {ECO:0000259|SMART:SM00322}.
SQ   SEQUENCE   541 AA;  60256 MW;  F2D7C7968E27BC18 CRC64;
     MAITSANQLE LLQTAEAVAR EKMIDPGLVI EAMEESLARA AKSRYGAEMD IRVSIDRKTG
     KATFTRVRTV VADEELENYQ AEFTVDQAKQ YMENPQIGDT FVEEVPPVEM GRIAAQSAKQ
     VILQKVREAE RDRQYEEFKD RAGTIINGLV KREEYGNVIV DVGAGEAILR RNEKIGRESY
     RPNDRIRCYI KDVRREPRGP QIFLSRTAPE FMAELFKMEV PEIYDGIIEI KAVARDPGSR
     AKIAVISYDN SIDPVGACVG MRGSRVQAVV NELQGEKIDI IPWNEDQPTF LVNALQPAEV
     SKVVLDEEAG KIEVVVPEEQ LSLAIGRRGQ NVRLASQLTG LDIDIMTEAE ESARRQKEFE
     SRTNLFMETL DLDEFFAQLL VSEGFTNLEE VAYVELDELL VIDGVDEGTA EELQARARDY
     LEAQAKAALD NARALGAEDS LIQFEGLTPQ MVEALAKDDV KTLEDFATCA DWELAGGWTT
     VDGQRVKDDG ILEPFGVSLE DAQDMVMTAR VMLGWVDPTE LLEEAEETEE GETATDEEAG
     A
//

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