ID L5MEE3_MYODS Unreviewed; 1403 AA.
AC L5MEE3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative ATP-dependent RNA helicase DHX57 {ECO:0000313|EMBL:ELK36098.1};
GN ORFNames=MDA_GLEAN10015159 {ECO:0000313|EMBL:ELK36098.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK36098.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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DR EMBL; KB101799; ELK36098.1; -; Genomic_DNA.
DR eggNOG; KOG0920; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase 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; 1.20.120.1080; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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; IPR042615; DHX57_UBA.
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; 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; 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; PF05773; RWD; 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; SM00165; UBA; 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; 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, ECO:0000313|EMBL:ELK36098.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ELK36098.1};
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:UP000010556};
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 165..211
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 295..317
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 546..713
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 849..1027
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 295..317
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1403 AA; 157623 MW; A75CDB70A01A2066 CRC64;
MSSSVRRKGK PGKGSGKGSS RGGRGGRSNA SKSHGGGGSG GNRKASSRTW DDGDDFCIFS
ESRSSARPSN SNVRKGDTRP KWKPKAKVPL QTLHMTSENQ EKVKALLRDL QEQDADAGSE
RSISGEEEED EPDCDDAQYW LAGQEASLVP DADPSDYAGS GPVEPYNPEL IVSTVAVQKL
SRYGFNTERC QAALRVCDGD VGASLEYLLI QCFSETFGER MKISEAVAHM SEDECVEPRQ
EEAFALKSIC GEKFVERIQN RVWTIGLELE YLTSKFRKSK QKESTKNIQE TLLDTCKFYL
KGNCKFGSKC KFKHEVPPNQ IVGRVERSVD DSHLNAHEDK SFLYELEIRF SKDHKYPYEA
PLVAFYSTNE SLPLACRLHI SEFLYGKALT FAETAEPVVY SLITLLGEES EIVNLLINTH
HKYSDPPVNF LPVSSGIRIN NPFCRKPVIP HNSFVSSRIP EVEKESLPEE ETDEDEGPAP
VVVENESYVN LKKKISKRYD WQAKSVHAEN AKICKQFQIK QTSRQFQSIL QERQSLPAWE
ERETILKLLS KHQVLVISGM TGCGKTTQIP QFILDESLNG PPEKVANIIC TQPRRISAIS
VAERVAKERA ERVGLTVGYQ IRLESVKSSA TRLLYCTTGV LLRRLEGDTA LQGVTHIIVD
EVHERTEESD FLLLVLKDIV LQRPTLQVIL MSATLNAELF SEYFSSCPVI TIPGRTFPVD
QFFLEDAIAV TRYVIPDGSP YMRSMKQMSK EKLKARRSRT AFEEVEEDLR LSLHLQDQDS
VRDAVPDQQL DFKQLLARYK GVSKSVIKTM SIMDFEKVNL ELIEALLEWI VEGKHSYPPG
ASPENHRCQV TAARYSCIEC LPPGGAILVF LPGLAEIKML YEQLQSNSLF NNRRSYRCVV
HPLHSSLSSE EQQAVFIKPP VGVTKIIIST NIAETSITID DVVYVIDSGK MKEKRYDASK
GMESLEDTFV SQANALQRKG RAGRVASGVC FHLFTSHHFS HQLLKQQLPE IQRVPLEQLC
LRIKILEMFN THNLQSVFSR LIEPPHPDSL RASKIRLRDL GALTTDEKLT PLGYHLASLP
VDVRIGKLML FGSIFRCLDP ALTIAASLAF KSPFVSPWDK KEEANQKKLE FAFANSDYLA
LLQAYKGWQL SLKEGMRTSY NYCRQNFLSG RVLQEMASLK RQFTELLSDI GFAKEGLRAR
EIEKRALGGD GILEATGEEA NSNAENPKLI SAMLCAALYP NVVQVKSPEG KFQKTSTGAV
RMQPKSDELK FVTKNDGYVH IHPSSVNYQV RHFDSPYLLY HEKIKTSRVF IRDCSMVSVY
PLVLFGGGQV NVQLQRGEFV VSLDDGWIRF AAASHQVAEL VKELRCELDQ LLQDKIKNPS
IDLCMCPRGS RIISTIVKLV TTQ
//
