ID A0A091QA43_LEPDC Unreviewed; 1325 AA.
AC A0A091QA43;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Putative ATP-dependent RNA helicase DHX57 {ECO:0000313|EMBL:KFQ06454.1};
DE Flags: Fragment;
GN ORFNames=N330_01072 {ECO:0000313|EMBL:KFQ06454.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ06454.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ06454.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ06454.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK672846; KFQ06454.1; -; Genomic_DNA.
DR PhylomeDB; A0A091QA43; -.
DR Proteomes; UP000053001; 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; 2.30.30.1190; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 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; IPR016135; UBQ-conjugating_enzyme/RWD.
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; 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:KFQ06454.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KFQ06454.1};
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:UP000053001};
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 114..164
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 245..272
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 493..660
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 768..948
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 245..272
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 25..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..428
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ06454.1"
FT NON_TER 1325
FT /evidence="ECO:0000313|EMBL:KFQ06454.1"
SQ SEQUENCE 1325 AA; 150442 MW; 4B5EC7F6E32E0C00 CRC64;
GGNRKCSAKI WDDGDDFCVF EEPRLESRSN APARREGQMK QRPEARMPLQ TIHMTSENQR
RVKELLQELQ GQELAPESEL AGCGEDDEPD CLDDEQCWST DQEVSDIIPR SSAEADEHRI
VESEVSSFAV HKLSRYGFDI EHCRTVLRSC NGNIGASLEY LLWQCFTERY GEKMQVSSAA
AEASQEECLE QRQEEAFALR SIYGEKFVER IQNRVWTFSL ELGYLANRLS KSKQKDGCSR
DTAKQTSKEI CKFYLQGGCR FGSKCRFGHE FPPKHPLKPA RNSVDDSHLR PNGDGPIYEL
EVRFPEENKY PLQAPLVAFY STDENLPRAC RLHVAEFLFG KALIAAEANE PVVYTLVTCL
EDEFEISELL KNTHHKYSVP PVSLLATPSV KLQTESTSGS NRMCEVSEPQ EEEEVTEDEE
EEDEPEQVVV ENESYVNLRK KLSKKYDVQA KSLYNENVKI CTQFRLKKSS RHFQSLLYER
QKLPAWQERE TILDLLKSHQ VLVVSGMTGC GKTTQIPQFI LDASLQESPS RVANIICTQP
RRISAISVAE RVAKERTERI GLTVGYQIRL ESVKSSATRL LYCTTGVLLR RLEGDLTLQG
ITHVIVDEVH ERTEESDFLL LVLKDIMVQR PDLRIILMSA TLNAELFSQY FHSCPIINIP
GRTFPVDQFF LEDVIAMTRY VLEDSSPYRR KTKQENKQNG RHKRTAFEEV EEDLRRAGIL
EGSDTVVRDS DPDQKLTLKQ LLARYKGVNK TVLKTMFVMD LDKVNLELIE ALLEWIVAGR
HSYPPGAVLI FLPGLAEIKM LYEQLQCNAL FNNRHSKRCV VYPLHSSLSS EEQQSVFLRP
PAGVIKIIIS TNIAETSVTI DDVVYVIDSG KMKEKRYDPS KGMESLEDTF VSKASALQRK
GRAGRVASGV CFHLFSSHHY NHQLIKQQLP EIQRVPLEQL CLRIKILEMF SAQSLHSVLS
RLIEPPRTES LRASKLRLQD LGALTPDEKL TPLGYHLASL PVDVRIGKLM LFGAIFRCLD
PALTIAASLA FKSPFVSPWD KREEANKKKL EFAVGNSDYL ALLQAYKGWS LSIKEGSQAS
YNYCRENFLS GRVLQEIASL KRQFTELLSD IGFVKEGLRA RDIEKKWSQG GDGVLDATGE
EANSNAENIK LISAMLCAAL YPNVVQVKKP EGKYQKTSTG AVKMQPKAEE LKFITKNDGY
VYIHPSSVNY QTRHFESPYL VYHEKIKTSR VFIRDCSMVS VYPLVLLGGG QVHMQLQKGE
FVISLDDGWI RFVAASHQVA ELVKELRCEL DQLLQDKIKN PTMDLCMCPR RSQIIGMIVK
LVTTQ
//
