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Database: UniProt
Entry: G3N8W9_GASAC
LinkDB: G3N8W9_GASAC
Original site: G3N8W9_GASAC 
ID   G3N8W9_GASAC            Unreviewed;      1062 AA.
AC   G3N8W9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Transcription termination factor, RNA polymerase II {ECO:0000313|Ensembl:ENSGACP00000001756.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000001756.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000001756.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000001756.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G3N8W9; -.
DR   STRING; 69293.ENSGACP00000001756; -.
DR   Ensembl; ENSGACT00000001757.1; ENSGACP00000001756.1; ENSGACG00000001351.1.
DR   eggNOG; KOG4439; Eukaryota.
DR   GeneTree; ENSGT00940000165376; -.
DR   InParanoid; G3N8W9; -.
DR   OMA; IVSQWTN; -.
DR   TreeFam; TF316297; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000001351; Expressed in head kidney and 8 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18072; DEXHc_TTF2; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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   InterPro; IPR010666; Znf_GRF.
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   Pfam; PF06839; zf-GRF; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51999; ZF_GRF; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01343}.
FT   DOMAIN          6..47
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   DOMAIN          479..681
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          894..1052
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          99..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1062 AA;  115721 MW;  6610C3DB4791F601 CRC64;
     MEKVLCDVHG SVCMLKTGVK DGPNKGKSFY VCVDKQGCDF THVARISPSN CLQHEDSMVE
     LQALTYSLQQ QSHRLFYRCI VGKKAAQKWC GNVPWRAPEK EKRNPLSHAQ PSCLPPVRNP
     FKASGKTDAD SEWRRMQRGG GGEDRDGGES HGAEGGGRHQ KENVEGVAAG EREAESYRGK
     QLPPGMKLKK RVSNEEEKRP KASGGGEPSD ADEEPGEARQ PTERVKDTGE SDSDSRKNPP
     PSTQAAQPEP SRPPALQVHD DDEDDVVVVS VKPATQRTPP VSAVQKTLTA FAGFQPASKV
     KGQQQDPGGL HGLLTSRLQQ KKATLSAVNV AALPDKGERL KSQVKELQDA LESLNLAAPS
     PPAGSQGGSN RGETDLEVNP CRQGGTILLH APPGPSQQQD LHLSQGCTQV YGAGPQAFYG
     GRMTDDRLLA VKNATSETID HLHKSLESCP DPEAEFPDPK GIKVPLLAHQ RRALAWLLWR
     ENQNPCGGIL ADDMGLGKTL TIIALILAKK TKANKEAETK PQSWISKTDS SLVASTGTLI
     ICPASLVHHW KREIERHVKT GKLMVYLYHG PQREKRANVL ADFDVVVTTY SLVSKEVPVQ
     KGGAENSSKD ADEVPSRSAP LLRVAWARVV LDEAHNIKNP KVQTSMAVCQ LRARARWAVT
     GTPIQNNLLD MYSLLKFLCC SPFDEYKVWK AQVDNGSNRG RERLNILTRT LLLRRTKAQR
     DSEGKPLVSL PGRTCEVHRL ELSRDEQAVY DVVFAQSRST LQNYLKRHEG SDGKGDARSA
     NPFDKAPSVA QEFGVSQAAS TSQQASSTVH ILSLLLRLRQ CCCPLSLLQK TLDTSELQGD
     GVVLSLEEQL NALSLSSGPS PGSDPLPPGT VALNGTRFAS RLFEDTSEST KIAAIVSELK
     AIRQKGADQK SVIVSQWTSM LRIVAVHLRG MGLRYAVIDG TVAPKHRMDL VEEFNSNARG
     PQVMLVSLCA GGVGLNLIGG NHLFLIDMHW NPALEDQACD RIYRVGQSKD VTIHRFVCDG
     TVEEKISTLQ EKKKELAQNV LSGTGSTVSK LSLADLRIIF GV
//
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