ID G3U3M0_LOXAF Unreviewed; 1386 AA.
AC G3U3M0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=DExH-box helicase 57 {ECO:0000313|Ensembl:ENSLAFP00000022428.1};
GN Name=DHX57 {ECO:0000313|Ensembl:ENSLAFP00000022428.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000022428.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000022428.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022428.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000022428.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022428.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_003416137.1; XM_003416089.2.
DR RefSeq; XP_010594181.1; XM_010595879.1.
DR RefSeq; XP_010594182.1; XM_010595880.1.
DR RefSeq; XP_010594183.1; XM_010595881.1.
DR RefSeq; XP_010594184.1; XM_010595882.1.
DR RefSeq; XP_010594185.1; XM_010595883.1.
DR STRING; 9785.ENSLAFP00000022428; -.
DR Ensembl; ENSLAFT00000034368.1; ENSLAFP00000022428.1; ENSLAFG00000002497.4.
DR GeneID; 100656807; -.
DR KEGG; lav:100656807; -.
DR CTD; 90957; -.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000156883; -.
DR InParanoid; G3U3M0; -.
DR OMA; PERVYVQ; -.
DR OrthoDB; 1095660at2759; -.
DR TreeFam; TF324744; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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 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; 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; PF00642; zf-CCCH; 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};
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:UP000007646};
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 176..221
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 300..327
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..1010
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 300..327
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 155422 MW; 3832340E9299191F CRC64;
MSSSVRRKGK PGKGGGKGSS RGGRGGRSHS NKSHGGGGGG GGGGGGSGGG NRKASSRIWD
DGDDFCIFSE SRRSSRPSSS STSKGESRPK RRPEVKVPLQ TLHMTSENQE KVKALLRDLQ
EQDADAGSER GISGEEEEDE PPYRDDEQYW SAGQEASLVP DPNPLQYACP ALVEPQIPES
RFSPLAVQKL CRYGFNTERC QAALRICDGD IGASLEHLLT QCFSETFGER MKTSEAVAHI
SLDECVEQRQ EEALALKSIC GEKFVERIPN RVWTIGLELE YLASKFCKSK QRGSTKTVQE
TSLETCKFYL KGNCKFGSKC KFKHEVPPNQ IVGRIERIVD DSHLHEDASF LYELEIRFSK
DHKYPYQAPL VAFYSTNENL PLACRLHISE FLYDKALTSA ETSEPVVYSL ITLLEEESEI
AKLLTNTHHK YSVPPVNFLP APSGTKMNNL ACCKPVIPNK SFVSNQIAEV ENETEPEEEA
DEDEGPAPVI VENESYVNLK KKSSKRYDWQ AKSVHAENAK IRKQFRIKQA SRQFQSILQE
RQSLPAWEER ETILKLLSKH QVLVISGMTG CGKTTQIPQF ILDDSLNGPP EKVANIICTQ
PRRISAISVA ERVAKERAER VGLTVGYQIR LESVKSSATR LLYCTTGVLL RRLEGDTALQ
GITHIIVDEV HERTEESDFL LLVLKDMILQ RPSLQVILMS ATLNAELFSE YFNFCPVITI
PGRTFPVDQF FLEDAIAVTR YVLQDGSPYL RSMKQISKDK LKARRNRTAF EEVEEDLRLS
LYLQEQGSVK DQVPDQQLDF KQLLARYKGF SKSVIKTMSI MDFEKVNLEL IEALLEWIMD
GKHSYPPGAI LVFLPGLAEI KMLYEQLQSN PLFNNRRSNR CVIHPLHSSL SSEEQQAVFV
KPPVGVTKII ISTNIAETSI TIDDVVYVID SGKMKEKRYD ASKGMESLED TFVSQANALQ
RKGRAGRVAS GVCFHLFTSH HYSHQLLKQQ LPEIQRVPLE QLCLRIKILE MFSTHTLQSV
FSRLIEPPHT DSLRASKIRL RDLGALTQDE KLTPLGYHLA SLPVDVRIGK LMLFGSIFRC
LDPALTIAAS LAFKSPFVSP WDKKEEANQK KLEFAFANSD YLALLQAYKG WQLSTKEGVR
ASYNYCRQNF LSGRVLQEIA SLKRQFTELL SDIGFVMEGL RAREIEKRAQ GGDGVLDATG
EEANSNADNP KLISAMLCAA LYPNVVQVKS PEGKFQKTSI GAVRMKPKSE ELKFVTKNDG
YVHIHPSSVN YQVRHFDSPY LVYHEKIKTS RVFIRDCSMV SVYPLVLFGG GQVNVQLQRG
EFVVSLDDGW IRFAAASHQV AELVKELRGE LDQLLQDKIK NPSIDLCTCP RGSRIISMIV
KLVTTQ
//
