ID A0A401NIW9_SCYTO Unreviewed; 1443 AA.
AC A0A401NIW9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=scyTo_0004004 {ECO:0000313|EMBL:GCB60814.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB60814.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB60814.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB60814.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BFAA01001144; GCB60814.1; -; Genomic_DNA.
DR STRING; 75743.A0A401NIW9; -.
DR OMA; XDYRHSE; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17987; DEXHc_YTHDC2; 1.
DR CDD; cd06007; R3H_DEXH_helicase; 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; IPR034083; R3H_DEXH_helicase.
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; PF12796; Ank_2; 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; SM00248; ANK; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00393; R3H; 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; PS50297; ANK_REP_REGION; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 42..105
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT DOMAIN 203..369
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REPEAT 508..540
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 610..786
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1292..1422
FT /note="YTH"
FT /evidence="ECO:0000259|PROSITE:PS50882"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1443 AA; 162587 MW; E15C53E7790AEA22 CRC64;
MWLHFQRANM SRPTSVSPRP GSAQSSQAAS KAKGFKDIRI DEEVKIAVNI ALERFRYSDQ
KEMEFPSSLT STERAFIHRL AQSLGLISKS KGKGAHRFLT IKKKDGSEMA QAVMTCTLTH
SMKHAIRNLI QRFPVTNKER TDLLPKTERG NALTVEAENN REMNKTSGRL NNGIPQVPPK
RGDSELDAFR QSLPVFEKRD EIVKIIKENR VILIIGETGS GKTTQIPQFL LDDCYKNGIP
CRIFCTQPRR LAAIAVAERV AAERGEKIGQ TIGYQIRLES RVSPKTLLTF CTNGVLLRTL
MAGDGTLAAV THVIVDEVHE RDRFSDFLLT KLRDLMQKHP SLRLILSSAA LDVNLFIRYF
TGCPVIYIQG RPFEVKELFL EDILRTTGYT NKEMLKYKKE KQREEKQQTN LTEWYKAKET
SNASRSEYQR QRFIPSLTTE NDLLDDGGDS VFSQLNEKDF NSLEPWLIKE MDACLSDIWL
HKDVDAFAQL FHLILSENVS VDYRHSETSA TPLMIAAGRG FLSQVEQLLS MGANVSVKAS
NGWIALDWAK RFGQTDIVDL LESFNSSVEL GNLDECVLVQ SNGAELSQED KEVLSVYHHS
FDDEKVDLDL IMHLLYNIFQ SSDDGAVLIF LPGYDEIVGL RDRILYDDKR FADNSHKLQV
FMLHSNMQTS DQKKVLKNLP GGIRKIILST NIAETSITVN DVVFVIDSGK VKEKSFDALN
SVTMLKMVWI SKASAVQRKG RAGRCRPGIC FHLFSRLRFQ NLLEFQTPEL LRMPLQELCL
HTKLLAPINC PIADFLAKAP EPPPSLIVRN AVQMLKTIDA MDSWEDLTEL GYHLADLPVE
PHLGKMVLCA VVLKCLDPIL TIACTLAYRD PFVLPVQPSQ KRASMLCRKR FAAGTFSDHM
ALLRAFQAWQ KARSDGWERA FCEKNFLSQA TMEIIIGMRT QLLGQLRASG FVRARGGGDI
RDVNTNSENW AVVKAALVAG MYPNLIHVDR ENLMLTGSKE KKVRFHPTSV LSQPQYKKIP
PANGQAVAVQ ALPTDWLIYD EMTRAHRIAN IRCCSAVTPI SVALFGGPAR LSSSALQEPS
SPRGNTYIDG VTNDSSDSEM EDKSTSKMAT LKLEEWLNFR IDPEAASLIL QLRQKWHSLF
LRRMRAPSKP WTQVDEATIR AIIGVLSSEE QAAGLQQPSG IGQRPRPMSS EELPVSSSWR
SNSRKSSAET EFSDDSSSVE YRERVQLKSQ QQQQRYKERG FLHPKRSSED RSDQSSVKST
DSSNYPSPCA SPSPPPSGKG SKSPSPRPNV PVRFFILKSS NLRNLEISQQ KGIWSTTPSN
ERKLNRAFWE SSIVYLVFSV QGSGHFQGFA RMISEIGRER SQEWGSAGLG GVFRVEWIRK
ESLPFQYAHH LLNPWNDNKK VQISRDGQEL EPQVGEQLLQ LWERIPVGGK LPQTDRLGIF
GES
//
