ID U3DSL5_CALJA Unreviewed; 1216 AA.
AC U3DSL5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=DHX8 {ECO:0000313|EMBL:JAB41683.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB41683.1};
RN [1] {ECO:0000313|EMBL:JAB41683.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skeletal muscle {ECO:0000313|EMBL:JAB41683.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GAMQ01000168; JAB41683.1; -; mRNA.
DR AlphaFoldDB; U3DSL5; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR CDD; cd21691; GH2-like_DHX8; 1.
DR CDD; cd05684; S1_DHX8_helicase; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044762; DHX8/Prp22_DEXHc.
DR InterPro; IPR049588; DHX8_GH2-like.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049621; S1_DHX8_helicase.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 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; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50126; S1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:JAB41683.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 261..332
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 571..734
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 752..932
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 153..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..222
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1216 AA; 138654 MW; 120B2C7C1560DA86 CRC64;
MAVAVAMAGS VIGSEPGPAE ELAKLEYLSL VSKVCTELDN HLGINDKDLA EFVISLAEKN
TTFDTFKASL VKNGAEFTDS LISNLLRLIQ TMRPPAKPST SKDPVVKPKT EKEKLKELFP
VLCQPDNPSV RTMLDEDDVK VAVDVLKELE ALMPSAAGQE KQRDTEHRDR TKKKKRSRSR
DRDRDRERNR DRDHKRRHRS RSRSRSRARE RNKAKSRCRS RSRSQSPPKD RKDRDKYGER
NLDRWRDKHV DRPPPEEPTI GDIYNGKVTS IMQFGCFVQL EGLRKRWEGL VHISELRREG
RVANVADVVS KGQRVKVKVL SFTGTKTSLS MKDVDQETGE DLNPNRRRNL VGETNEETSM
RNPDRPTHLS LVSAPEVEDD SLERKRLTRI SDPEKWEIKQ MIAANVLSKE EFPDFDEETG
ILPKVDDEED EDLEIELVEE EPPFLRGHTK QSMDMSPIKI VKNPDGSLSQ AAMMQSALAK
ERRELKQAQR EAEMDSIPMG LNKHWVDPLP DAEGRQIAAN MRGIGMMPND IPEWKKHAFG
GNKASYGKKN QMSIIEQRES LPICKLKEQL IQAVHDNQIL IVIGETGSGK TTQITQYLAE
AGYTSRGKIG CTQPRRVAAM SVAKRVSEEF GCCLGQEVGY TIRFEDCTSP ETVIKYMTDG
MLLRECLIDP DLTQYAIIML DEAHERTIHT DVLFGLLKKT VQKRQDMKLI VTSATLDAVK
FSQYFYEAPI FTIPGRTYPV EILYTKEPET DYLDASLITV MQIHLTEPPG DILVFLTGQE
EIDTACEILY ERMKSLGPDV PELIILPVYS ALPSEMQTRI FDPAPPGSRK VVIATNIAET
SLTIDGIYYV VDPGFVKQKV YNSKTGIDQL VVTPISQAQA KQRAGRAGRT GPGKCYRLYT
ERAYRDEMLT TNVPEIQRTN LASTVLSLKA MGINDLLSFD FMDAPPMETL ITAMEQLYTL
GALDDEGLLT RLGRRMAEFP LEPMLCKMLI MSVHLGCSEE MLTIVSMLSV QNVFYRPKDK
QALADQKKAK FHQTEGDHLT LLAVYNSWKN NKFSNPWCYE NFIQARSLRR AQDIRKQMLG
IMDRHKLDVV SCGKSTVRVQ KAICSGFFRN AAKKDPQEGY RTLIDQQVVY IHPSSALFNR
QPEWVVYHEL VLTTKEYMRE VTTIDPRWLV EFAPAFFKVS DPTKLSKQKK QQRLEPLYNR
YEEPNAWRIS RAFRRR
//
