ID A0A3B3SL04_9TELE Unreviewed; 1067 AA.
AC A0A3B3SL04;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Transcription termination factor 2 {ECO:0000313|Ensembl:ENSPKIP00000031028.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000031028.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000031028.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B3SL04; -.
DR Ensembl; ENSPKIT00000011867.1; ENSPKIP00000031028.1; ENSPKIG00000011691.1.
DR GeneTree; ENSGT00940000164746; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT TRANSMEM 1040..1062
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..48
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 560..760
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 971..1067
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 101..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 118127 MW; D528912FC17B9C20 CRC64;
MEEVFCDTHG TRCLLKTGVK DGPTKGKSFY LCSVRGAPCD FTRTADIPPS HCLHHEDSLV
ELQAVAPRDQ KHCYRLLFRC IVGKKEGLKW CGSLPWKEKK ATEKKHSDRE ESQIPDCPRE
RNPFKVPSKT DEASEWRILQ NGGSGRQEKT AEQREENTGG GTEDEGGKKH CRTYQLPPGA
RVKKKSSGEG RREDDLGRES AEVTNDPTGT WVKEARSGRE EKRGQNRGRK SEEALGKEEV
AGHGGVCEEV QSHKDAKKRV SQEGERRNDR KDTPSQDNEG QRPRKTEKDT AQVLPADGTV
VPCSTGAKED QCSKPVQQKG GRTDSQEEED NDVLLVSVQL GTKQIPLTEM GKAVAPVQKT
LTSFPGFHLA SHAKAPQEDP QTLHNQLSTQ LKQKKATLST VNLSALPDKG ERLKNQVKEL
EEALESLSLN TGDLSQPEPQ SAGDDTKLGI IPSQTNTVSR LGGTILLPGP CVPVQAGPSP
LGLDLSQGHS GVNPQVHAFY GGRMTESRML VVRNVTTEAI DHLHHSLESC PGPDSEEKDP
RGIKVPLLPH QRRALAWLRW RETQKPCGGI LADDMGLGKT LTMIALILAR KQKEKKDDKL
EEWISKNDSS LVASQGTLII CPASLVHHWK NEIEKRVKGG HLSVYLYHGP NRQRSTRVLA
DHDMVVTTYS LVSKEIPVEK EDPQKPSQDV ADVPAKLPPL MRVVWARVIL DEAHNIKNPK
AQTSIAVCRL RAQARWAVTG TPVQNNLLDM YSLLKFLRCS PFDEYKLWKA QVDNGSKRGG
ERLNILTQSL LLRRTKGELD SDGKPLVALP DRVCEVHHLK LSEDEQAVYD VIFTQSKSTL
QSYLKRHERD DSTAEVKTNP FQKVAREFGV PSDTVASSQP ASSSASSAVH ILSLLLRLRQ
CCCHLSLLKK TLDQSELQGD GITLSLEEQL GALSLSEPTP DPNPEDMVSL NGNRFRSSLF
EDTSCSTKIA AILSELRKIR EAHSAQKCVI VSQWTSMLHI VAVHLRELGL RFAVIDGTVN
PKRRMDLVEE FNNDPKGPQV MLVSLCAGGV GINLVGGNHL FLMDMHW
//
