ID H0YV23_TAEGU Unreviewed; 1256 AA.
AC H0YV23;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=DExH-box helicase 57 {ECO:0000313|Ensembl:ENSTGUP00000002144.2};
GN Name=DHX57 {ECO:0000313|Ensembl:ENSTGUP00000002144.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000002144.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000002144.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000002144.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; H0YV23; -.
DR STRING; 59729.ENSTGUP00000002144; -.
DR Ensembl; ENSTGUT00000002164.2; ENSTGUP00000002144.2; ENSTGUG00000002076.2.
DR GeneTree; ENSGT00940000156883; -.
DR HOGENOM; CLU_001832_4_1_1; -.
DR InParanoid; H0YV23; -.
DR OMA; PERVYVQ; -.
DR TreeFam; TF324744; -.
DR Proteomes; UP000007754; Chromosome 3.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
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; 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; 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};
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:UP000007754};
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 156..200
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 279..306
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 527..694
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 800..980
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 279..306
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..462
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1256 AA; 141653 MW; F6251D55A87355FF CRC64;
MSWLGRKKGK PNRGGGRGRG GSGRRGGSSG HSNKPQLGGS RKCSSKIWDD GDDFCLFEEP
RLESRSSAPA RRGGQMKQRP EAKMPLQTIH MTSENQRRVK ELLQELQGQE LAPESDVAGE
DDDEPDYLDD EQCWSTEQEA SDVMPRLSAE PAEHRIVDSE VSSFAVHKLS RYGFDCERCR
AVLRSCNGNI GASLEYLLLQ CFSERYGEKM QISEAAAEAS QEECLEQRQE EAFALRSIYG
EKFIERIKNR VWTFNLELGY LAHRFSKSKQ KSTRDTAKQT SKEICKFYLQ GGCRFGSKCR
FRHEFPPNHP LNTSKNSVDD AHLRCSDGPI YELEVRFPDE NKYPLQAPLV AVYSTDENLP
LACRLHIAEF LFGKALAAAE SHEPVVYTLV TCLEDEHEIS ELLSNTHHKF SVPPVSLLAA
PPVKPQTENA PASNQQAEAS TVSEPQEEEV VAEEEEEEPE QVVVENESYV NLKKKLSKKY
DVQAKSLYNE NVKICAQFRQ KKSSRHFQSM LYERQKLPAW QERENILGLL ESHQVLVVSG
MTGCGKTTQI PQFILDASLQ GSPSRVANII CTQPRRISAI SVAERVAKER TERIGLTVGY
QIRLESVKSS ATRLLYCTTG VLLRRLEGDL TLQGVTHVIV DEVHERTEES DFLLLVLKDI
MVQRPDLRII LMSATLNAEL FSQYFHSCPI INIPGRTFPV DQFFLEDVIA MTRYVLEDSS
PYRKKVKHEQ SGRHKRTAFE EVEEDLRRAG LLETTDTVVR DSDPDQQLTL KQLLTRYKGV
SKSVLKTMSV MDLDKVNLEL IEALLEWIVA GRHSYPPGAV LIFLPGLAEI KMLYEQLQTN
ALFNNRHSKR CVVYPLHSSL SSEDQQSVFL RPPAGVTKII ISTNIAETSV TIDDVVYVID
SGKMKEKRYD PSKGMESLED TFVSKANALQ RKGRAGRVAS GVCFHLFSSH HYNHQLVKQQ
LPEIQRVPLE QLCLRIKILE MFSEQSLHSV LSRLIEPPRT ESLQASKVRL RDLGALTPEE
KLTPLGYHLA SLPVDVRIGK LMLFGTIFRC LDPALTIAAS LAFKSPFVSP WDKREEANKK
KLEFAVGNSD YLALLQAYKG WRLSIKEGSQ ASYNYCRENF LSGRVLQEIA SLKRQFAELL
SDIGFVKEGL RARDIEKKWS QGGDGVLDAT GEEANSNAEN IKLISAMLCA ALYPNVVQVK
KPEGKYQKTS TGAVKMQPKA EELKFVTKND GYVHIHPSSV NYQVRMLLSA KHALFL
//
