ID L5ME34_MYODS Unreviewed; 1365 AA.
AC L5ME34;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Putative ATP-dependent RNA helicase YTHDC2 {ECO:0000313|EMBL:ELK36515.1};
GN ORFNames=MDA_GLEAN10021774 {ECO:0000313|EMBL:ELK36515.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK36515.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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DR EMBL; KB101591; ELK36515.1; -; Genomic_DNA.
DR RefSeq; XP_006755342.1; XM_006755279.2.
DR GeneID; 102774915; -.
DR KEGG; myd:102774915; -.
DR CTD; 64848; -.
DR eggNOG; KOG0920; Eukaryota.
DR eggNOG; KOG0922; Eukaryota.
DR eggNOG; KOG1902; Eukaryota.
DR OrthoDB; 1095660at2759; -.
DR Proteomes; UP000010556; 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; 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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ELK36515.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
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 DOMAIN 549..721
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1223..1353
FT /note="YTH"
FT /evidence="ECO:0000259|PROSITE:PS50882"
FT REGION 1101..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1365 AA; 153696 MW; 4790A281159531A7 CRC64;
MEFPSSLTST ERAFIHRLSQ SLGLVSKSKG KGANRYLTVK KKDGSETAHA MMTCNLTHNT
KHAVRSLIQR FPVTNKERTE LLPKTERGNV FAVEAENREM SKTSGRLNNG IPQIPVKRGE
SEFDSFRQSL PVFEKQEEIV KIIKENKVVL IVGETGSGKT TQIPQFLLDD CFKNGIPCRI
FCTQPRRLAA IAVAERVAAE RRERIGQTIG YQIRLESRVS PKTLLTFCTN GVLLRTLMAG
DSTLSAVTHV IVDEVHERDR FSDFLLTKLR DLLQKHPTLK LILSSAALDV NLFIRYFGSC
PVIYIQGRPF EVKEMFLEDI LRTTGYTNKE MLKYKKEKQR EEKQQTTLTE WYSAQENTVK
PESQRQRTIP NVTEEYDLLD DGGDAVFSQL TEKDVNCLEP WLIKEMDACL SDIWLNKDVE
AFAQIFHLIL TENVSVDYRH SETSATVLMV AAGRGFSSQV EQLISMGANV HSKASNGWMA
LDWAKHFGQT EVVDLLESYS ASLEFGNLDE SSLVQTNGSD LNAEDRELLK AYHHSFDDEK
VDLDLIMHLL YNICHSCDAG AILIFLPGYD EIVGLRDRIL FDDKRFADNT HRYQVFMLHS
NMQTSDQKKV LKNPPAGVRK IILSTNIAET SITVNDVVFV IDSGKVKEKS FDALNFVTML
KMVWISKASA IQRKGRAGRC RPGICFRLFS RLRFQNMLEF QTPELLRMPL QELCLHTKLL
APVNCPIADF LMKAPEPPPA LIVRNAVQML KTIDAMDAWE DLTELGYHLA DLPVEPHLGK
MVLCAVVLKC LDPILTIACT LAYRDPFVLP TQASQKRAAM LCRKRFTAGT FSDHMALLRA
FQAWQKARSD GWERAFCEKN FLSQATMEII IGMRTQLLGQ LRASGFVRAR GGGDIRDVNT
NSENWAVVKA ALVAGMYPNL VHVDRENLVL TGSKEKKVRF HPTSVLSQPQ YKKIPPANGQ
AAAIQALPTD WLIYDEMTRA HRIANIRCCS AVTPVTVLVF CGPARLASNA LQESSSFRAD
GIPNDSSDSE MEDRTTANLA ALKLDEWLNF KLEPEAASLL LQLRQKWHSL FLRRMRAPSK
PWSQVDEATI RAIIAALSTE EQSAGLQQPS GIGQRPRPMS SEELPLASSW RSNNSRKSSA
DTEFPDESTT AERVLMKSPS PALHPPQKYK DRGILHPKRS TDDRPDQASA KSTEDYPSPC
ASPSPPSSGK GSKSPSPRPN MPIRYFIMKS SNLRNLEISQ QKGIWSTTPS NERKLNRAFW
ESSMVYLVFS VQGSGHFQGF SRMSSEIGKE KSQDWGSAGL GGVFKVEWIR KESLPFQFAH
HLLNPWNDNK KVQISRDGQE LEPQIGEQLL QLWERLPSGE KMTTD
//
