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Database: UniProt
Entry: A0A0G2JZH9_RAT
LinkDB: A0A0G2JZH9_RAT
Original site: A0A0G2JZH9_RAT 
ID   A0A0G2JZH9_RAT          Unreviewed;      1396 AA.
AC   A0A0G2JZH9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=DExH-box helicase 57 {ECO:0000313|Ensembl:ENSRNOP00000071053.2};
GN   Name=Dhx57 {ECO:0000313|Ensembl:ENSRNOP00000071053.2,
GN   ECO:0000313|RGD:1310340};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000071053.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000071053.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000071053.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000071053.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000071053.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A0G2JZH9; -.
DR   STRING; 10116.ENSRNOP00000071053; -.
DR   PhosphoSitePlus; A0A0G2JZH9; -.
DR   jPOST; A0A0G2JZH9; -.
DR   PaxDb; 10116-ENSRNOP00000030935; -.
DR   Ensembl; ENSRNOT00000090688.2; ENSRNOP00000071053.2; ENSRNOG00000054272.2.
DR   AGR; RGD:1310340; -.
DR   RGD; 1310340; Dhx57.
DR   VEuPathDB; HostDB:ENSRNOG00000054272; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   GeneTree; ENSGT00940000156883; -.
DR   InParanoid; A0A0G2JZH9; -.
DR   OMA; PERVYVQ; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000054272; Expressed in cerebellum and 20 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:UP000002494};
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          183..228
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          307..334
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          563..730
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          840..1020
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   ZN_FING         307..334
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1396 AA;  156294 MW;  18E50A12C50830AF CRC64;
     MLGVKMSSSV RRKGKPGKGD GKGSSRGGRG GRGHVNKSHG GGGSGGGGCG GGGGGGSGSR
     KASNRIWDDG DDFCVFTESK RPSRPCDSNK SKGETRPKWK PKAKVPLQTL HMTSENQEKV
     KALLRDLQEQ GADAGSERGS SGEEEEDAPE GAAEQSWSAG PEPTFLPDCR PWEYIGPEEV
     EPPLPEFTVS PLAVQKLSRY GFHTEHCQLA LRICEGDLGA ALEHLLHQCF SETFGERMAL
     SEAAVSVSLD ECVEQRQEET LALKSICGEK FIERIQNRVW TIGLELEYLT NKFCKSKQKE
     SNKNVRDTSP ETCKFYLKGN CKFGSKCKFK HEVPPHQIIG RTERNVNDPH LDAENDTTFL
     YELQIRFSKD HKYPYQAPLV AFYSTNENLP LACRLHISEF LYGKALEFAK TSEPVVYSLI
     TLLEEESEIV KLLTHTQHKY SVPPINVPPA PSETRISKPA YRKPVIPSNT FLSNQMLEGE
     GLSELEEDAD EDEGPAPIVV ENESYVNLKK RSYRRCDRPA KSLFAENSKI CRQFQMKQAS
     RQFHAILQER QLLPAWEERE TILKLLSKHQ VVVISGMTGC GKTTQIPQFI LDNSLNGPPE
     RVANIICTQP RRISAISVAE RVAKERAERV GLTVGYQIRL ESVKSSATRL LYCTTGVLLR
     RLEGDATLQG VTHIIVDEVH ERTEESDFLL LVLKDIVMQR ATLQVILMSA TLDAGLFSKY
     FSYCPVITIP GRAFPVDQFF LEDALAVTRY VLQDGSPYMR SMKQIAKERL KARHNRTALE
     EVEEDLRLAL HLQDEEESVK DTIPDQQLDF KQLLVRYKGV SKSVIKTMSV MDFEKVNLEL
     IEALLEWIVD GKHSYPPGAI LVFLPGLAEI KMLYEQLQSN SLFNNRRSHR CVIHPLHSSL
     SSEEQQAVFV KPPLGVTKII ISTNIAETSI TIDDVVYVID SGKMKEKRYD AGKGMESLED
     TFVSQANALQ RKGRAGRVAS GVCFHLFTSH HYNHQLLKQQ LPEIQRVPLE QLCLRIKILE
     MFSTHNLQSV FSRLIEPPHV DSLRASKVRL RDLGALTPDE KLTPLGYHLA SLPVDVRIGK
     LMLLGSIFRC LDPALTIAAS LAFKSPFVSP WDKKEEANQK KLEFAFANSD YLALLCAYKG
     WQLSTKESAR ASYNYCRQNF LSGRTLQEMA SLKRQFTELL SDIGFVKEGL RAKEIEKRAQ
     GGDGVLDATG EEANTNAENP KLISAVLCAA LYPNVVQVKT PEGKFQKTSS GVVRLQPKSA
     ELKFVTKNDG YVHIHPSSVN YQVRHFDSPY LLYHEKIKTS RVFIRDCSMV SVYPLVLFGG
     GQVSVQLQRG AFVVSLDDGW IRFVAASHQV AELVKELRCE LDQLLQDKIK NPSMDLCTCP
     RGSRIISMIV KLITTQ
//
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