ID A0A1Z3HHU8_9CYAN Unreviewed; 510 AA.
AC A0A1Z3HHU8;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ASC69843.1};
GN ORFNames=XM38_007730 {ECO:0000313|EMBL:ASC69843.1};
OS Halomicronema hongdechloris C2206.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nodosilineales; Nodosilineaceae;
OC Halomicronema.
OX NCBI_TaxID=1641165 {ECO:0000313|EMBL:ASC69843.1, ECO:0000313|Proteomes:UP000191901};
RN [1] {ECO:0000313|EMBL:ASC69843.1, ECO:0000313|Proteomes:UP000191901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2206 {ECO:0000313|EMBL:ASC69843.1,
RC ECO:0000313|Proteomes:UP000191901};
RX PubMed=26514405; DOI=10.1016/j.bbabio.2015.10.009;
RA Li Y., Lin Y., Garvey C.J., Birch D., Corkery R.W., Loughlin P.C.,
RA Scheer H., Willows R.D., Chen M.;
RT "Characterization of red-shifted phycobilisomes isolated from the
RT chlorophyll f-containing cyanobacterium Halomicronema hongdechloris.";
RL Biochim. Biophys. Acta 1857:107-114(2016).
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; CP021983; ASC69843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z3HHU8; -.
DR STRING; 1641165.XM38_10745; -.
DR KEGG; hhg:XM38_007730; -.
DR OrthoDB; 9807233at2; -.
DR Proteomes; UP000191901; 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: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 CDD; cd02134; KH-II_NusA_rpt1; 1.
DR CDD; cd22529; KH-II_NusA_rpt2; 1.
DR Gene3D; 3.30.300.20; -; 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; 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; IPR013735; TF_NusA_N.
DR InterPro; IPR010213; Tscrpt_termination_fac_NusA.
DR NCBIfam; TIGR01953; NusA; 1.
DR PANTHER; PTHR22648; TRANSCRIPTION TERMINATION FACTOR NUSA; 1.
DR PANTHER; PTHR22648:SF0; TRANSCRIPTION TERMINATION_ANTITERMINATION PROTEIN NUSA; 1.
DR Pfam; PF13184; KH_5; 1.
DR Pfam; PF08529; NusA_N; 1.
DR SMART; SM00322; KH; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 2.
DR SUPFAM; SSF69705; Transcription factor NusA, N-terminal domain; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00945};
KW Reference proteome {ECO:0000313|Proteomes:UP000191901};
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|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 265..328
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 337..411
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 440..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..510
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 56325 MW; 36D4E3EB0A94F3A4 CRC64;
MSLVNLPNLQ ELIDHISRER NLPKHAVENA LREALLKGYE RYRRTQRMDG NVQFEEDYFD
NFDIELDTDE YGEQGFRVLA SKAIVEEVQS ADHEIALVEV QEVAPEAQLG DTVVLDVTPE
QREFGRMAAI QTKQVLAQKL RDQQRKMIQE EFQDLEGTIL NARVLRFERQ SVIMAVSSSL
GQPEVEAELL KRDQLPNDNY RANATFRVAL KKVSEGSHRG PQLLVSRADA SLVVELFSNE
VPEIEDEIVR IVAVAREANP PSRSVGPRTK IAVDTVERDV DPVGACIGAR GSRIQVVVNE
LRGEKIDVIR WSPDPATYIA NALSPARVDE VRLMNPEERQ AHVLVPEDQL SLAIGKEGQN
VRLAARLTGW KIDIKDAAKY DYAAEDEKQA EIQAQREAQQ QVALAATAAT ATDLEANLED
ENGAAEEALA PVTGPSLADA AMATEERATA REAGTPEAST PAESASEAVS DNAASAEDSL
EENTLAEDLE EDTVDETPVE SDEAYPREEE
//
