ID M7CHW9_CHEMY Unreviewed; 1322 AA.
AC M7CHW9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=UY3_02275 {ECO:0000313|EMBL:EMP40537.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP40537.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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; KB509732; EMP40537.1; -; Genomic_DNA.
DR STRING; 8469.M7CHW9; -.
DR eggNOG; KOG0922; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
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; 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; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EMP40537.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 367..438
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 677..840
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 858..1038
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..312
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 149807 MW; C1A621F8E1F4BA40 CRC64;
MVFHPLELPS ATPSVTDYSS PESARQDGHG CGVETNDLMA SFGLKISWQA AGDHAELISR
GDHDGVPESQ KSSSMDQTGG GSATTTRAVL FDSFNGDGGN MEAGFGDEED DSSQQASEET
GFPDSQELFL TLDLEPVLPE LTQGCLLEKG RRRDLWSVNE HPKGKAEFVI NLAEKNTTFD
TFKTALTKNG AEFTDSLISN LLRLIQTMRP PAKPSTGKEV VVKPKTEKEK LKDLFPALCR
PDNPTIRTML DEDDVKVAVD ALKELEALMP SAGGQEKQRN NDRRAKKKRR SRSHSRDRDR
KRRHRSHSRS RSRTLDKNKG KSRYRSRSRS LSPSRDRKDR EKYAEKSNDR WRDKHVDRPP
PEEPSIGEIY NGKVTSIMQF GCFVQLEGLR KRWEGLVHIS ELRREGRVAN VADVVSKGQR
VKVKVLSFTG SKTSLSMKDV DQETGEDLNP NRRRNLVGET NEETSMRNPD RPSHLSLVNA
PEVEDDSLER KRLTRISDPE KWEIKQMIAA NVLSKEEFPD FDEETGILPK VDDEEDEDLE
IELVEEEPPF LRGHTKQSMD MSPIKIVKNP DGSLSQAAMM QSALAKERRE LKQAQREAEM
DSIPMGLNTH WVDPLPDVDG RQIAANMRGI GMMPNDIPEW KKHAFGGNKA SYGKKTQLSI
IEQRESLPIF RLKEQLIQAV HDNQILIVIG ETGSGKTTQI TQYLAEAGYT SRGKIGCTQP
RRVAAMSVAK RVSEEFGCCL GQEVGYTIRF EDCTSPETVI KYMTDGMLLR ECLIDPDLTQ
YAIIMLDEAH ERTIHTDVLF GLLKKTVQKR QDMKLIVTSA TLDAVKFSQY FYEAPIFTIP
GRTYPVEILY TKEPETDYLD ASLITVMQIH LTEPPGDILV FLTGQEEIDT ACEILYERMK
SLGPDVPELI ILPVYSALPS EMQTRIFDPA PPGSRKVVIA TNIAETSLTI DGIYYVVDPG
FVKQKVYNSK TGIDQLVVTP ISQAQAKQRA GRAGRTGPGK CYRLYTERAY RDEMLTTNVP
EIQRTNLAST VLSLKAMGIN DLLSFDFMDA PPMETLITAM EQLYTLGALD DEGLLTRLGR
RMAEFPLEPM LCKMLIMSVH LGCSEEMLTI VSMLSVQNVF YRPKDKQALA DQKKAKFHQT
EGDHLTLLAV YNSWKNNKFS NPWCYENFIQ ARSLRRAQDI RKQMLGIMDR HKLDVVSCGK
ATVRVQKAIC SGFFRNAAKK DPQEGYRTLI DQQVVYIHPS SALFNRQPEW VVYHELVLTT
KEYMREVTTI DPRWLVEFAP AFFKVSDPTK LSKQKKQQRL EPLYNRYEEP NAWRISRAFR
RR
//
