ID A0A3Q3H2T8_9LABR Unreviewed; 1397 AA.
AC A0A3Q3H2T8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=DExH-box helicase 57 {ECO:0000313|Ensembl:ENSLBEP00000038013.1};
GN Name=DHX57 {ECO:0000313|Ensembl:ENSLBEP00000038013.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000038013.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000038013.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 56723.ENSLBEP00000038013; -.
DR Ensembl; ENSLBET00000039577.1; ENSLBEP00000038013.1; ENSLBEG00000028343.1.
DR GeneTree; ENSGT00940000156883; -.
DR InParanoid; A0A3Q3H2T8; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17985; DEXHc_DHX57; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF256; ATP-DEPENDENT RNA HELICASE DHX57-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 181..231
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 320..343
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 561..728
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 840..1020
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 320..343
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..153
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..498
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1397 AA; 155556 MW; 9BBE301E26628B3F CRC64;
MNARRRGGKP NRGGGRFNKS KGGGGRGGGG GGGGGGGGGK KGGAACWDDD DDFSLVFGAP
RSSRGGRDRD RDSSSKALPR SLARTRTYPQ SGESTRPEAS TMPLQRIFMT NENQEQLKEL
LRELQTQDFD ENYDESGSDY TGSEEEEVEF DELDHREDGQ FWATNDEPVE RAESPAYDPE
SGDERPTPEP VISLFAIAKL CRFGFDRERS KQALESGGGE FGTTLEQLLH QVYSERFGQK
ALSVDGLKSV PMDDCLSQRQ EEALALAAIY GERFSERIAN SVWTVTLDLS FLLDNADKNG
ERVWGRGGGG GRGVVNIRDV CKFFLKGQGC RFGDKCKFKH QLPTKERSGA GSPDLMGPSQ
PGVSSYSPPE YELQIPPIVA FSTTDDSVGA AGRLSVTERL FGEALAAAKS SEPVVYTLIT
ICEDENMMKD LLAVGHHKYS TPPPVVVVPP PPVAIAKSKS VRNATEENRG SSSSMKETTE
AEELDDQDEE DEEEAVPVES ESYVNLRKKM VNKHNLKLDN LLQENGKLCR EFQKKQSSRR
FRSMFEQRRK LPAWQERENI LDLLDRCQVL VVSGMTGCGK TTQIPQFILD STLKGRADEV
ANIICTQPRR ISAISVAQRV AEERAESLGN SVGYQIRLES VRTSATRLLY CTTGVLLRRL
EGEADLTGVT HVIVDEVHER TEESDFLLLV LKDLIVQRPD LKIILMSATL NANLFSEYFY
NCPTIHIPGR TFPVDQFFLE DAIAKSRYVI EDGSPYMRSG KQNSSSSSGR GSKADPRDLV
DDLGDDMWNY MSFCKKDFVK DSIPDQQLGL QELTLRYKDI KKPVLKTMAA MDLDKINMDL
VESLLEWIVD GKHGYPPGAV LVFLPGLAEI KMLYEQLKSN RMFNNRGPTR CEVYPLHSTL
SNEEQQAVFS RPPEGVTKII ISTNIAETSV TIDDVVYVID SGKMKEKRYD ASKSMESLED
SWVSRANALQ RKGRAGRVAS GVCFHLFTSH CFQHQLAEQQ LPEIQRVPLE QLCLRIKILD
VFAERTLESV FSRLIEPPAM ESLDAAKQRL CDLGALTADE KLTPLGYHLA CLPVDVRIGK
LMLFGAIFRC LDPALTIAAS LAFKSPFVSP WDKREEANEK KVAFAVAQSD HLALLQAYKG
WCCAAKNGNK AGFSYCRENF LSWRGLQEIA SLKRQFAELL SDIGFIKEGL RARVIDRMST
KGTDGVLEAT GPEANLNSEN IRLMSAMLCA ALYPNVVQVR APQGNFKMTS KGAMKMQPKA
NELRFMTKDD GCVHVHPSSV NYTVRHYNSP YLVYHEKVKT SRVFIRDCSM VSVYPLVLFG
GGQVNVELHK GEFVISLDDG WIRFAASSHQ VAELVKELRW ELDQLLEDKI RSPSMDLCSC
PRGSRIIRMI VHLITTQ
//
