ID M7BPS1_CHEMY Unreviewed; 1378 AA.
AC M7BPS1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Putative ATP-dependent RNA helicase YTHDC2 {ECO:0000313|EMBL:EMP39906.1};
GN ORFNames=UY3_02857 {ECO:0000313|EMBL:EMP39906.1};
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:EMP39906.1, 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).
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DR EMBL; KB515362; EMP39906.1; -; Genomic_DNA.
DR STRING; 8469.M7BPS1; -.
DR eggNOG; KOG0920; Eukaryota.
DR eggNOG; KOG0922; Eukaryota.
DR eggNOG; KOG1902; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR CDD; cd17987; DEXHc_YTHDC2; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR CDD; cd21134; YTH; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.10.590.10; ph1033 like domains; 1.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR007275; YTH_domain.
DR PANTHER; PTHR18934:SF213; 3'-5' RNA HELICASE YTHDC2; 1.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 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; PF01424; R3H; 1.
DR Pfam; PF04146; YTH; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS50882; YTH; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EMP39906.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 1..43
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT DOMAIN 140..306
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REPEAT 443..475
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 549..732
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1236..1366
FT /note="YTH"
FT /evidence="ECO:0000259|PROSITE:PS50882"
FT REGION 350..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 155012 MW; DD794DE9A6C529BF CRC64;
MEFPSSLTST ERAFIHRLSQ SLGLISKSKG KGANRYLTIK KKDGSELAHT VMACSLTPNT
KHAIRSLIQR FPVTNKERTE LLPKTERGNV FAVEAENREM SKTSGRLNNG IPQIPVKRGE
SEFDSFRQSL PVFEKHEEIV RIIKENKVVL IVGETGSGKT TQIPQFLLDD CYKNGIPCRI
FCTQPRRLAA IAVAERVAAE RREKIGQTIG YQIRLESRVS PKTLLTFCTN GVLLRTLMAG
DSTLSTVTHV IVDEVHERDR FSDFLLTKLR DILQKQTTLK LILSSAALDV NLFIRYFGSC
PVIHIQGRPY EVKEMFLEDI LRSTGYTNKE MVKYKKEKQR EEKQQTTLTE WYSAQDNTSK
PESQRQRSVP SVAEEYDLLD DGGDTVFSQL TEKDVNCLEP WLIKEMDSCL SDIWLHKDVD
AFAQVFHLIL TENVSVDYRH SETSATALMI ASGRGFLSQV EQLIGMGANV HSKSSNGWMA
LDWAKHFGQT EIVDLLESYS ASLEFGNLDE SSLVQANGGD LSAEDRELLK AYHHSFDDEK
VDLDLIMHLL YNICHSCDAG AVLIFLPGYD EIVGLRDRIL FDDKRFADNA HRYQVFMLHS
NMQTSDQKKV LKTPPPGIRK IAITIKKTLL LQILSTNIAE TSITVNDVVF VIDSGKMKEK
SFDALNCVTM LKMVWISKAS AIQRKGRAGR CRPGICFRLF SRLRFQNMLE FQTPELLRMP
LQELCLHTKL LAPINCPIAD FLMKAPDPPP SLIVRNAVQM LKTIDAMDTW EDLTELGYHL
ADLPVEPHLG KMVLCAVVLK CLDPILTIAC TLAYRDPFVL PTQASQKRAA MLCRKRFTAG
TFSDHMALLR AFQAWQKARS DGWERAFCEK NFLSQATMEI IIGMRTQLLG QLRASGFVRA
RGGGDIRDVN TNSENWAVVK GALVAGMYPN LVHVDRENLV LTGPKEKRVR FHPTSVLSQP
QYKKIPPANG QAAAIQALPT DWLIYDEMTR AHRIANIRCC SAVTPVTVSL FCGPARLPSN
ALQEPSSFRV DGVLNDSSDS EMEDRTTANL AALKLDEWLH FKLDPEAASL LLQLRQKWHS
LFLRRMRAPS KPWSQVDEAT IRAIIAVLST EEQSAGLQQP SGIGQRPRPM SSEELPLASS
WRSNSSRKSS AETEFSDDSS NAEKVLMKST SPAFHPPQKY KERGILHSKR SSDDRSDQSS
VKSTDSSSYP SPCASPSPPS SGKGSKSPSP RPNMPIRYFI MKSSNLRNLD ISQQKGIWST
TPSNERKLNR AFWESSMVYL VFSVQGSGHF QGFARMSSEI GREKSQDWGS TGLGGVFKVE
WIRKESLPFQ FAHHLLNPWN DNKKVQISRD GQELEPLVGE QLLQLWDRIP LGEKNTTD
//
