ID B4DKW2_HUMAN Unreviewed; 932 AA. AC B4DKW2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 75. DE SubName: Full=cDNA FLJ56001, highly similar to Putative ATP-dependent RNA helicase DHX57 {ECO:0000313|EMBL:BAG59324.1}; DE Flags: Fragment; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG59324.1}; RN [1] {ECO:0000313|EMBL:BAG59324.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Tongue {ECO:0000313|EMBL:BAG59324.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T., RA Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK296739; BAG59324.1; -; mRNA. DR AlphaFoldDB; B4DKW2; -. DR PeptideAtlas; B4DKW2; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; 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 CDD; cd14317; UBA_DHX57; 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; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR042615; DHX57_UBA. 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; IPR006575; RWD_dom. DR InterPro; IPR015940; UBA. DR InterPro; IPR009060; UBA-like_sf. 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; PF00271; Helicase_C; 1. DR Pfam; PF05773; RWD; 1. DR Pfam; PF18044; zf-CCCH_4; 1. DR SMART; SM00487; DEXDc; 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 SUPFAM; SSF46934; UBA-like; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 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 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:BAG59324.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU00723}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; 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 180..220 FT /note="UBA" FT /evidence="ECO:0000259|PROSITE:PS50030" FT DOMAIN 299..326 FT /note="C3H1-type" FT /evidence="ECO:0000259|PROSITE:PS50103" FT DOMAIN 554..721 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 830..932 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT ZN_FING 299..326 FT /note="C3H1-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723" FT REGION 1..106 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 120..147 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 55..69 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 71..85 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 932 FT /evidence="ECO:0000313|EMBL:BAG59324.1" SQ SEQUENCE 932 AA; 104488 MW; 07BA35AF585F0C17 CRC64; MSSSVRRKGK PGKGGGKGSS RGGRGGRSHA SKSHGSGGGG GGGGGGGGGN RKASSRIWDD GDDFCIFSES RRPSRPSNSN ISKGESRPKW KPKAKVPLQT LHMTSENQEK VKALLRDLQE QDADAGSERG LSGEEEDDEP DCCNDERYWP AGQEPSLVPD LDPLEYAGLA SVEPYVPEFT VSPFAVQKLS RYGFNTERCQ AVLRMCDGDV GASLEHLLTQ CFSETFGERM KISEAVNQIS LDECMEQRQE EAFALKSICG EKFIERIQNR VWTIGLELEY LTSRFRKSKP KESTKNVQEN SLEICKFYLK GNCKFGSKCR FKHEVPPNQI VGRIERSVDD SHLNAIEDAS FLYELEIRFS KDHKYPYQAP LVAFYSTNEN LPLACRLHIS EFLYDKALTF AETSEPVVYS LITLLEEESE IVKLLTNTHH KYSDPPVNFL PVPSRTRINN PACHKTVIPN NSFVSNQIPE VEKASESEES DEDDGPAPVI VENESYVNLK KKISKRYDWQ AKSVHAENGK ICKQFRMKQA SRQFQSILQE RQSLPAWEER ETILNLLRKH QVVVISGMTG CGKTTQIPQF ILDDSLNGPP EKVANIICTQ PRRISAISVA ERVAKERAER VGLTVGYQIR LESVKSSATR LLYCTTGVLL RRLEGDTALQ GVSHIIVDEV HERTEESDFL LLVLKDIVSQ RPGLQVILMS ATLNAELFSD YFNSCPVITI PGRTFPVDQF FLEDAIAVTR YVLQDGSPYM RSMKQISKEK LKARRNRTAF EEVEEDLRLS LHLQDQDSVK DAVPDQQLDF KQLLARYKGV SKSVIKTMSI MDFEKVNLEL IEALLEWIVD GKHSYPPGAI LVFLPGLAEI KMLYEQLQSN SLFNNRRSNR CVIHPLHSSL SSEEQQAVFV KPPAGVTKII ISTNIAETSI TIDDVVYVID SG //