ID A0A1E5QM87_9CYAN Unreviewed; 442 AA.
AC A0A1E5QM87;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000256|HAMAP-Rule:MF_00945};
GN Name=nusA {ECO:0000256|HAMAP-Rule:MF_00945};
GN ORFNames=BH720_09460 {ECO:0000313|EMBL:OEJ75463.1};
OS Desertifilum tharense IPPAS B-1220.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Desertifilum.
OX NCBI_TaxID=1781255 {ECO:0000313|EMBL:OEJ75463.1, ECO:0000313|Proteomes:UP000095472};
RN [1] {ECO:0000313|EMBL:OEJ75463.1, ECO:0000313|Proteomes:UP000095472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPPAS B-1220 {ECO:0000313|EMBL:OEJ75463.1,
RC ECO:0000313|Proteomes:UP000095472};
RA Sinetova M.A., Bolakhan K., Zayadan B.K., Mironov K.S., Ustinova V.,
RA Kupriyanova E.V., Sidorov R.A., Skrypnik A.N., Gogoleva N.E., Gogolev Y.V.,
RA Los D.A.;
RT "Draft genome of thermotolerant cyanobacterium Desertifilum sp. strain
RT IPPAS B-1220.";
RL Submitted (SEP-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEJ75463.1}.
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DR EMBL; MJGC01000050; OEJ75463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5QM87; -.
DR STRING; 1781255.BH720_09460; -.
DR Proteomes; UP000095472; 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: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:UP000095472};
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 259..322
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 331..398
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 393..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 49210 MW; C693099834B3B3FB CRC64;
MVSLPGLKDM IDKISQERNL PKPAVQAALR EALMKGYERY RRTLRMNAPN FDDEYFNNFE
VELDAEEEGF RILATKTIVE EVSNSDHQIS LEEVKKVADE AQLGDTVLLD VTPDQGEFGR
MAAIQTKQVL AQKLRDQQRK LIQEEFQDLE GTVLQARVLR FERQSVIMAV SSSFGQPEVE
AELPKREQLP NDNYRANATF KVYLKKVGSG SHRGPQLVVS RADAGLVVYL FANEVPEIED
EVVRIVAVAR EANPPSRYVG PRTKIAVDTL EREVDPVGAC IGARGSRIQV VVNELRGEKI
DVIRWSPDPA TYIANALSPA RVDAVYLVDP DIRQAHVLVA ENQLSLAIGK EGQNVRLAAR
LTGWKIDIKD SANYDYDAET SKIAAAAEAR QQVAQAEAAD EEDSFLGDEE LEEDLATSEE
LEEYDEAIAQ ADALDRDPSE VS
//
