ID   G0NQ20_CAEBE            Unreviewed;      1136 AA.
AC   G0NQ20;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Transcription termination factor 2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CAEBREN_29674 {ECO:0000313|EMBL:EGT35430.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL379922; EGT35430.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0NQ20; -.
DR   STRING; 135651.G0NQ20; -.
DR   EnsemblMetazoa; CBN29674.1; CBN29674.1; WBGene00191639.
DR   eggNOG; KOG4439; Eukaryota.
DR   HOGENOM; CLU_010816_0_0_1; -.
DR   InParanoid; G0NQ20; -.
DR   Proteomes; UP000008068; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45626:SF54; TRANSCRIPTION TERMINATION FACTOR 2; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008068}.
FT   DOMAIN          530..751
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          970..1125
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1136 AA;  128774 MW;  BCB3E05D3014FCDE CRC64;
     MSTTRRTRVM IDTSSDESND EEKSGQSKSE QNTGSQLEEN MSTNIPEFPS DADDSVVEES
     MRSIRSPTTP EANGSLRVHS NLSRSIVTST PKSRSVASAK IESSYGSSKS SSHNNDHDRS
     RSFIENDENA PMTPITKKLT QATDMRSKAL LRQRLLRKAM KKPDDDANRG CSSNSIGAWG
     SASTESLPES SELFNSVLSP IVRTAPRQFQ FDSDTFVNIP KVAASTAIND IGGGIQEQID
     TKKDDDRLEN RIFGNTKQEY NRGIVDKTPD KQSAKPSTSN KVQEEIVTIV LDDSDIIDVT
     PQKPQRIAVP EEEHPPWLVS RKPPPRAPSP EKEDYSKLSY KELVAKKNQV MGLISHFEHL
     PDKGKRVLRQ FQDLDDEVER RKDLGLDILS DQDDDDDIIV IDDEDEEPKR VAPIFPSGSV
     MTQNGLLPTR RIVDPVPAVQ MDFNAILDRN NKKLMAGKMT DQKYRNVNLI TDRVVQQLAE
     YVPLLVYYIY LIFFSATHTI PAETDLTDTP KGFKIELMPH QKGGLTWMIW RETQPQPGGI
     LADDMGLGKT LSMISLIAHQ KAARIARKEA GENQVDKDRR ALVKEKGLVP TNCTLIVAPA
     SLIHQWEAEI ERRLEDNALS VYMFHGTKKQ RNIEARRLAR YDVVITTYTL VANELIEKIR
     TKSKADVSSD EESDESNHGI RRAVGKDDSV LAQICWARVI LDEAHAIKNR LSLASKAVCR
     LSAFSRWCLS GTPIHNNLWD LYSLIRFLRV LPFSEDKYWK ESIMPMKPIM ADRVNLLMKN
     LLLRRTKEQT CAVTNKKIVD LPPKTVEIYD LEFDLEEAQA YEIMMEAAKK FVKKMLEQSD
     DMRNLGFVRR RRAKKGGEEE FLNPFNFGPR NLENGSNFEK MSHVLMFLLR LRQACVHFHI
     TRSGMDLEAF KLIGGEDDED VDLEKLGDLM EKTMHMMDGS DDEDDDRHGR KKRSSQIFEP
     DYLSCKIKKT LEILGTITEK NEKVVIVSQW TSVLNLVEQH IKTNRINYTT ITGNVLVKDR
     QERVDSFNRE FGGAQVMLLS LTAGGVGLNL TGGNHLIMID LHWNPALEQQ AFDRIYRMGQ
     KKPVFIHRLV TKGTIEQRVA LLQKEKLTLA SNILDGTATR KMNKLTTADI KMLFQL
//