GenomeNet

Database: UniProt
Entry: D7N1M5_9NEIS
LinkDB: D7N1M5_9NEIS
Original site: D7N1M5_9NEIS 
ID   D7N1M5_9NEIS            Unreviewed;       500 AA.
AC   D7N1M5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   13-FEB-2019, entry version 57.
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:EFI24858.1};
GN   ORFNames=HMPREF9016_01038 {ECO:0000313|EMBL:EFI24858.1};
OS   Neisseria sp. oral taxon 014 str. F0314.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=641149 {ECO:0000313|EMBL:EFI24858.1, ECO:0000313|Proteomes:UP000002768};
RN   [1] {ECO:0000313|EMBL:EFI24858.1, ECO:0000313|Proteomes:UP000002768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0314 {ECO:0000313|EMBL:EFI24858.1,
RC   ECO:0000313|Proteomes:UP000002768};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA   White J., Yandava C., Izard J., Baranova O.V., Blanton J.M.,
RA   Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Neisseria sp. oral taxon 014 strain F0314.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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; GL349411; EFI24858.1; -; Genomic_DNA.
DR   RefSeq; WP_009174062.1; NZ_GL349411.1.
DR   STRING; 641149.HMPREF9016_01038; -.
DR   EnsemblBacteria; EFI24858; EFI24858; HMPREF9016_01038.
DR   eggNOG; ENOG4105CHV; Bacteria.
DR   eggNOG; COG0195; LUCA.
DR   BioCyc; GCF_000090875-HMP:HMPREF9016_RS05280-MONOMER; -.
DR   Proteomes; UP000002768; Unassembled WGS sequence.
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; 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   PANTHER; PTHR22648; PTHR22648; 1.
DR   Pfam; PF13184; KH_5; 1.
DR   Pfam; PF08529; NusA_N; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00322; KH; 3.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF47794; SSF47794; 2.
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; 2.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002768};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945};
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      140    208       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   COILED      109    129       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   500 AA;  56284 MW;  05496E4A10D84E01 CRC64;
     MSREMLQLAE ALASEKNVDT EVVFQALEFA LSTAAKKKAN REHMDVRVEI DRDTGEYRTF
     RRWLIVADED YTYPDVEKTI EEIQEEIPGT EIQIGEYYEE QLENEGFGRQ AAQTAKQIIL
     QRIRDAEREQ ILNEFLARKE DIVSGTVKRV ERHGIIVEVV SGKLDALIPR DQMIPRENFR
     SGDRIRALLL RVDEIGSTGR KQVILSRTDK NFLAKLYAME VPEIEDGSLE IRAVARDPGQ
     RAKVAVKAND QRIDPQGTCI GVRGSRVNAV SNELSGERID VVLWSPETAQ FVINALSPAE
     VTRIVIDEDK HAVDVVVAED QLALAIGRGG QNVRLASDLT EWQLNIMTVA EADERNEAED
     EAIRKLFTEH LNIDEETADI LLQEGFATLE EVAYVPAAEL LEIDGFDEEI VEVLRNRARD
     AILTLAIASE EKLEDVADDL RSLEGLDTEM LRDLAQAGII TRDDLAELAV DELIEITGVT
     EEEAKKVILA AREHWFTESN
//
DBGET integrated database retrieval system