ID W8C3S0_CERCA Unreviewed; 1372 AA.
AC W8C3S0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:JAC03909.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAC03909.1};
RN [1] {ECO:0000313|EMBL:JAC03909.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAC03909.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(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; GAMC01002647; JAC03909.1; -; mRNA.
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:0000313|EMBL:JAC03909.1};
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 417..488
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 726..889
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 907..1087
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 109..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..368
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1372 AA; 156719 MW; B77352F83A778857 CRC64;
MEELRRLEYL SLVSKICTEL ENHLGLNDKD LAEFIIDLEE KNPTFDSFRK ALHENGAEFP
DSFVTNLQRI INLMKPGRGE EEPEGISSVK SAKADQLTRM FPGLALPNDK FSKSYSSGGE
SENASSESDS EHERSNNEGK KVKTKKRDEI EDVMDELEAL APSKRIHVEN KNDLDDTMAE
LEALAPSQRI KVHKSKDEDT DDAMAELEAL APSKQLKKEH KPKKSDIDDA MDKLEALAPS
AQKKYEDTKV KTEKKRKLDR HSRSRSKERT SRHERSSRRD RSRDKRSRSY SPSEKRNSDR
RRRSRSKSRH RDRDHERIKD RERERDRSDR RRRSRSRSHG HSTSSSSRRR SRSRSRDRHR
RSRSRDRGDR SGRKRSRSRE RNERSARKRS RSNSGERHGR NEKMPPPATL PDDPEPGKIY
TGKVANIVPF GCFVQLFGLR KRWEGLVHIS QLRSEGRVTD VTEVVQRNSN VKVKVMSIAG
QKVSLSMKEV DQATGRDLNP LSHVAPEDEM RDRNPDRPYS GTSLLNLQGG SMDNDESDSR
KRVTRISSPE RWEIKQMISS GVIDRSEMPD FDEETGLIQK EEDDEADIEI EIVEEEPPFL
SGHGRALHDL SPVRIVKNPD GSLAQAAMMQ SALSKERREQ KMLQREQDAV APTNMSRNWI
DPLPDEDESR TMTNTRGIGS GATIEVPEWK KHVIGGKKSS FGKKTDMSLL EQRQSLPIYK
LRDDLIKAVS DNQILIVIGE TGSGKTTQIT QYLAESGFTA RGKIGCTQPR RVAAMSVAKR
VAEEFGCRLG QEVGYTIRFE DCTSPETVIK YMTDGMLLRE CLMESDLKSY SVIMLDEAHE
RTIHTDVLFG LLKGAVQKRP ELKLIVTSAT LDAVKFSQYF FEAPIFTIPG RTFPVEVLYT
KEPETDYLDA SLITVMQIHL REPPGDILLF LTGQEEIDTA CEILYERMKS LGPDVPELII
LPVYSALPSE MQTRIFDPAP AGSRKVVIAT NIAETSLTID GIFYVVDPGF VKQKVYNSKT
GMDSLVVTPI SQAAAKQRAG RAGRTGPGKC YRLYTERAYR DEMLPTPVPE IQRTNLAMTV
LQLKTMGIND LLHFDFMDAP PVESLVMALE NLHSLSALDD EGLLTRLGRR MAEFPLEPNL
SKMLIMSVAL QCSDEVLTIV SMLSVQNVFY RPKDKQALAD QKKAKFNQPE GDHLTLLAVY
NSWKNNKFSN AWCYENFVQI RTLKRSQDVR KQLLGIMDRH KLDVVSAGKN SVRIQKAICS
GFFRNAAKKD PQEGYRTLVD SQVVYIHPSS ALFNRQPEWV VYHELVQTTK EYMREVTTID
PKWLVEFAPS FFRFSDPTKL SKFKKNQRLE PLYNKYEEPN AWRISRVRRR RN
//
