ID   WDR4_BOVIN              Reviewed;         414 AA.
AC   A7E3S5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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 {ECO:0000255|HAMAP-Rule:MF_03056};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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, such as let-7. Acts as a regulator of embryonic stem cell self-
CC       renewal and differentiation. Independently of METTL1, also plays a role
CC       in genome stability: localizes at the DNA replication site and
CC       regulates endonucleolytic activities of FEN1. {ECO:0000255|HAMAP-
CC       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       Interacts with FEN1; the interaction is direct. {ECO:0000255|HAMAP-
CC       Rule:MF_03056}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03056}.
CC       Chromosome {ECO:0000255|HAMAP-Rule:MF_03056}. Note=Localizes at the
CC       site of nascent DNA synthesis. {ECO:0000255|HAMAP-Rule:MF_03056}.
CC   -!- SIMILARITY: Belongs to the WD repeat TRM82 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03056}.
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DR   EMBL; BT030696; ABS45012.1; -; mRNA.
DR   RefSeq; NP_001093790.1; NM_001100320.1.
DR   AlphaFoldDB; A7E3S5; -.
DR   SMR; A7E3S5; -.
DR   STRING; 9913.ENSBTAP00000028643; -.
DR   PaxDb; A7E3S5; -.
DR   PRIDE; A7E3S5; -.
DR   GeneID; 508051; -.
DR   KEGG; bta:508051; -.
DR   CTD; 10785; -.
DR   eggNOG; KOG3914; Eukaryota.
DR   HOGENOM; CLU_054270_1_0_1; -.
DR   InParanoid; A7E3S5; -.
DR   OrthoDB; 937275at2759; -.
DR   TreeFam; TF105877; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
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   Acetylation; Chromosome; DNA damage; Nucleus; Reference proteome; Repeat;
KW   tRNA processing; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P57081"
FT   CHAIN           2..414
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase non-catalytic
FT                   subunit WDR4"
FT                   /id="PRO_0000370532"
FT   REPEAT          60..99
FT                   /note="WD 1"
FT   REPEAT          101..140
FT                   /note="WD 2"
FT   REPEAT          144..184
FT                   /note="WD 3"
FT   REPEAT          187..227
FT                   /note="WD 4"
FT   REGION          377..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P57081"
SQ   SEQUENCE   414 AA;  45858 MW;  938C8AA264982F5D CRC64;
     MASSAGLALC GHALVVRGGS RLLATSTSSS DGDSLFIYDC SAAEKKSQEN KGEDGQPVDQ
     GSDTVLASTF SKSGSYFVLT DDSKRLILFR TNPWQCLSVR TVVRRCTALT FTASEEKILV
     ADKSGDVYSF SVLEPHGGGR LELGHLSMLL DVAVSPDDRF VLTADRDEKI RVSWAAAPHS
     IESFCLGHTE FVSRIFVVPN HPELLLSSSG DCTLRLWEYR SGRELHCCPL TSLQEPTEPW
     SDKRFAVSRI TYWSQEDCVA LSCDGLPVVY IFQLDAAQRQ LVPRQLLTFQ HRVWDAAFEE
     GHGLWVLQDC REDPLVLYRP VGGQWQSAPE SAELRRVCAH VRVNWAMLEG CAGVDSGFSS
     LYKATCDNMT TYLKKKEERL QQQLEKKRRQ APPPGPNGPT KKMRAGELAQ GCSS