ID H0YZZ9_TAEGU Unreviewed; 1418 AA.
AC H0YZZ9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=LOC100224554 {ECO:0000313|Ensembl:ENSTGUP00000003884.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000003884.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000003884.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000003884.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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};
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DR RefSeq; XP_012433153.1; XM_012577699.1.
DR RefSeq; XP_012433154.1; XM_012577700.1.
DR SMR; H0YZZ9; -.
DR STRING; 59729.ENSTGUP00000003884; -.
DR Ensembl; ENSTGUT00000003926.2; ENSTGUP00000003884.2; ENSTGUG00000003755.2.
DR GeneID; 100224554; -.
DR KEGG; tgu:100224554; -.
DR GeneTree; ENSGT00940000155826; -.
DR HOGENOM; CLU_001832_1_6_1; -.
DR InParanoid; H0YZZ9; -.
DR OMA; XDYRHSE; -.
DR OrthoDB; 1095660at2759; -.
DR TreeFam; TF318311; -.
DR Proteomes; UP000007754; Chromosome Z.
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; 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; 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 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; 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:UP000007754};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 36..104
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT DOMAIN 200..366
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REPEAT 503..535
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 609..781
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1282..1412
FT /note="YTH"
FT /evidence="ECO:0000259|PROSITE:PS50882"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1418 AA; 158648 MW; C3D6405190C5F838 CRC64;
MSRPRNGPPR QHGAGTVGSG APAAPGRGRG GKGLRDIRVD EEVEIAVNLA LERFRYGEDL
EMEFPSSFTR TERAFVHRLC HSLGLISKSK GKGANRYLTV RKKDGSELKR AVMTCALTPG
TKHAVCTLIR NFPVTNKERT ELLPKTEQGN AYGVESGNKE VKTSGRLSDG IPQVPVKRGE
SDLDFFRKSL PVFEKQEEIV KIIKDHKVLL IVGETGSGKT TQIPQFILDD CHKNGTPCRI
LCTQPRRLAA VAVAERVAAE RRENIGQTVG YQIRLESRVS PKTLVTFCTN GILLRSLMAG
DSTLSTVTHV IVDEVHERDR FSDFLLIKLR DVLQSQANLK LIISSAALDA DLFIRYFGCC
PVIHIQGRSF EVKEMFLEDI LRSTGYTNKD MVKYKKEKQK EEKQQSTLTE WCSARENSSK
LEPERPRFVP RATEECSLLG DDGDTVFNQL TEKDANCLEL WLIKEMDSCL SDIWLRKDID
AFAQVFHLIL TENVSVDYRH SETSATALMI ASGRGFLSQV EQLISMGANI HCRSSNGWMA
VDWAKHFGQT EVVDLLESYS ASAGFGNLDE SSLVQTSGSD LSAEDRELLT AYHHSFDDEK
VDLDLIMHLL YNICHNCETG AILIFLPGYD EIVSLRDRIL LDDRRFADNA HSYQVVILHS
NMQTLDQKKV LKSPPPGVRK IILSTNIAET SITVNDVVFV IDSGKVKEKS FDALSCVTML
KMVWISKASA LQRKGRAGRC QPGVCFRLFS RLRFENMLEF QTPELLRMPL QELCLHTKLL
APINCSVVDF LMKAPDPPPA LIVKNALQML KTIDAMDPWE DLTELGYHLT ELPVEPHLGK
MVLYAVVLKC LDPVLTIACA LAYRDPFVLP TLASQKRAAV LCRKRFAAGT FSDHMVLLRV
FQAWQKARSD GWERAFCEKN FLSQATMQII VGMRAQLLGQ LRASGFVRAR GGADIRDVNT
NSENWAVVKA ALVAGMYPNL VHVDRESLVL TAPKEKKVRF HPTSVLSQPQ YKKILPVNDQ
TAAVQALPTD WLIYDEMMRA HRIANIRCCS VVTPITVALF CGPARLPSSA LQASSSCQGD
RVPSDSSDSE MEDRTTSNVS LLKLDEWLHL KLDSEAAGLL LQLRQKWHSL FLRRMRAPSK
LWSQVDEATV RAVVAVLTAE EQSAGLEQPS RIGQRPRPVA SEDHLVPSTW RSANTRSTTE
TEFSDSSNAE KDLMRSARPI LHQPKKYKRK NTLHSKQTSD DRSDRSVKSA DSSSFPSPCA
SPSSPISGKA SKSPSPRQNT PVRYFIMKSS NLQNIDISQQ KGIWSTTPSN ERKLNGAFWE
SSMVYLIFSV QGSGHFQGFA RMGSSIGCEK SQDWGSAGFG GVFKVEWIRK ESIPFQFAHH
LLNPWNDNKK VQISRDGQEL EPQVGEQLLQ LWNQIPLE
//
