WDR4_DANRE
ID WDR4_DANRE Reviewed; 413 AA.
AC A4IGH4; B0UXG2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit wdr4 {ECO:0000255|HAMAP-Rule:MF_03056};
DE AltName: Full=WD repeat-containing protein 4 {ECO:0000255|HAMAP-Rule:MF_03056};
GN Name=wdr4; ORFNames=si:ch211-140m22.6;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-catalytic component of a methyltransferase complex
CC required for the formation of N(7)-methylguanine in a subset of RNA
CC species, such as tRNAs, mRNAs and microRNAs (miRNAs). In the
CC methyltransferase complex, it is required to stabilize and induce
CC conformational changes of the catalytic subunit. Required for the
CC formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. Also
CC required for the formation of N(7)-methylguanine at internal sites in a
CC subset of mRNAs. Also required for methylation of a specific subset of
CC miRNAs. {ECO:0000255|HAMAP-Rule:MF_03056}.
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03056}.
CC -!- SUBUNIT: Forms a heterodimer with the catalytic subunit mettl1.
CC {ECO:0000255|HAMAP-Rule:MF_03056}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03056}.
CC -!- SIMILARITY: Belongs to the WD repeat TRM82 family. {ECO:0000255|HAMAP-
CC Rule:MF_03056}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI35102.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR361548; CAQ13728.1; -; Genomic_DNA.
DR EMBL; BC135101; AAI35102.1; ALT_INIT; mRNA.
DR AlphaFoldDB; A4IGH4; -.
DR SMR; A4IGH4; -.
DR STRING; 7955.ENSDARP00000103752; -.
DR PaxDb; A4IGH4; -.
DR PeptideAtlas; A4IGH4; -.
DR ZFIN; ZDB-GENE-060810-10; wdr4.
DR eggNOG; KOG3914; Eukaryota.
DR InParanoid; A4IGH4; -.
DR PhylomeDB; A4IGH4; -.
DR TreeFam; TF105877; -.
DR UniPathway; UPA00989; -.
DR PRO; PR:A4IGH4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR GO; GO:0106004; P:tRNA (guanine-N7)-methylation; IEA:GOC.
DR GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03056; TRM82; 1.
DR InterPro; IPR028884; Trm82.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR16288; PTHR16288; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Repeat; tRNA processing; WD repeat.
FT CHAIN 1..413
FT /note="tRNA (guanine-N(7)-)-methyltransferase non-catalytic
FT subunit wdr4"
FT /id="PRO_0000370533"
FT REPEAT 101..140
FT /note="WD 1"
FT REPEAT 144..183
FT /note="WD 2"
FT REPEAT 187..227
FT /note="WD 3"
FT REPEAT 286..328
FT /note="WD 4"
FT REGION 386..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 89
FT /note="C -> G (in Ref. 2; AAI35102)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="G -> S (in Ref. 2; AAI35102)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="H -> N (in Ref. 2; AAI35102)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="A -> P (in Ref. 2; AAI35102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46240 MW; B888964D6AA983AA CRC64;
MAVVCSKADW FVTSCSTTLV AVNLKQSREP FVFDCSKAEK KPKEADVDNK SAGEGSEEKD
SDSILAFAIS ASGKHVALTD DHKRLVLFCT EPSWKCISTR WVVRRCTSLA FTQAEDELYV
ADKSGDVYSF SILEPHKAGE LKLGHLSMLL DVALSPDDKY IITADRDEKI RVSFRRSPYN
IQAFCLGHTE FVSSLLVPAG HPDWLLSGSG DGTVNVWHYE TGRRLHSVDM RKFGLDSENT
EKRFAVSRII SSPDGQHVAV QCEGFPSVQL FTVDCGTEGL LKPADTLTLP LSPWDVTFDS
ENQLWVLLES EDMKVLLYRH SEQHWRLCDS ESPELKKVTN ALQTQWHLFK GSVGLESQFK
HLYKVNFDNM ASYLQKKQER LDLEHKKRAA AANGSKPNKK SKTESGAVPQ STS
