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
//