TYW4_NEUCR
ID TYW4_NEUCR Reviewed; 1213 AA.
AC Q9P3K9; Q1K8S2; V5INB9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=tRNA wybutosine-synthesizing protein 4;
DE Short=tRNA-yW synthesizing protein 4;
DE EC=2.1.1.290;
DE EC=2.3.1.231;
DE AltName: Full=Leucine carboxyl methyltransferase 2;
DE AltName: Full=tRNA(Phe) (7-(3-amino-3-(methoxycarbonyl)propyl)wyosine(37)-N)-methoxycarbonyltransferase;
DE AltName: Full=tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase;
GN Name=lcm-2; Synonyms=ppm2, tyw4; ORFNames=B15I20.020, NCU05392;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC that acts as a component of the wybutosine biosynthesis pathway.
CC Wybutosine is a hyper modified guanosine with a tricyclic base found at
CC the 3'-position adjacent to the anticodon of eukaryotic phenylalanine
CC tRNA. May methylate the carboxyl group of leucine residues to form
CC alpha-leucine ester residues (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-
CC adenosyl-L-methionine = 7-[(3S)-(3-amino-3-
CC methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:36903, Rhea:RHEA-COMP:10379, Rhea:RHEA-
CC COMP:11844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73543,
CC ChEBI:CHEBI:74275; EC=2.1.1.290;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in
CC tRNA(Phe) + CO2 + S-adenosyl-L-methionine = 2 H(+) + S-adenosyl-L-
CC homocysteine + wybutosine(37) in tRNA(Phe); Xref=Rhea:RHEA:37119,
CC Rhea:RHEA-COMP:11844, Rhea:RHEA-COMP:11847, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73544, ChEBI:CHEBI:74275; EC=2.3.1.231;
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000305}.
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DR EMBL; AL389900; CAB97456.1; -; Genomic_DNA.
DR EMBL; CM002237; ESA43542.1; -; Genomic_DNA.
DR PIR; T51032; T51032.
DR RefSeq; XP_011393570.1; XM_011395268.1.
DR AlphaFoldDB; Q9P3K9; -.
DR SMR; Q9P3K9; -.
DR STRING; 5141.EFNCRP00000006531; -.
DR EnsemblFungi; ESA43542; ESA43542; NCU05392.
DR GeneID; 3879634; -.
DR KEGG; ncr:NCU05392; -.
DR VEuPathDB; FungiDB:NCU05392; -.
DR HOGENOM; CLU_002761_1_0_1; -.
DR InParanoid; Q9P3K9; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0031591; P:wybutosine biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13621; Cupin_8; 1.
DR Pfam; PF04072; LCM; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..1213
FT /note="tRNA wybutosine-synthesizing protein 4"
FT /id="PRO_0000226143"
FT DOMAIN 1006..1166
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 289..290
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1213 AA; 132709 MW; 492FD9E2E53CECCA CRC64;
METTEEVVAP ATTQQPATEV GSAKPTTSTY SKKQKKPKAT TTTTTTDGTT PTHNEHASAK
DPRKAQDDQV MGTNNSSIVS KRSVEKLYYP NEPHFFRFFV KKFQRRAPLI NRGYHFRLHV
IDVLVRNFLQ EQRTGDAKGK RKVVVNLGCG SDVLPWQCLA RYPDACRSGE KDGAKFVDVD
FPDLIERKKR TVLETPELLG PLTNVVVPEF APVPSTPAAT TTAAATTTTT TELKTTAATA
SSTSTEAPQK PKKSPKPKDK SKAARAPAPT TAPTGIVFTS DQYVQIGCDL RDLATLQDSL
TRAVGGDLSS CTFLFVAEVS ITYMETPGAD AVIQWASSLG DSEFVLLEQL LPSGPTHPFA
STMLSHFHKL NTPIKSVDVY PTVASQVERF RSRGWGSGDV RVWTLWEAWA DAEDTFVNAA
ERRRLDEVEP FDEWEEFALF ASHYCVVRAR TVARDGQNKK KERGIPNGRE LGLPVEKVKV
RWDDVPGQRG QRRFAAGAVL TSSSPSSEKK EEVKLLNVMG LGTKSRLQNC DVYGRKKVGD
ADEADGTDEE KTAVPFTFRE GGPSTRMCHS LTDFGTAQLL VGGRASPSTP LKDCWLLEKT
NGSESEWAWK RTNDLPIPLY RHSVTRLGKT DMALLAGGRG VADIFPDWLL YEPKLGWIRC
EIAGDVKPTS VYGATLACLR QESDSFSGVF TGGLSDDGLI ADQLLAWNLD VSNSSRPVVT
FVPLQVKSGD DGREEALSRL LLTRFGASCL PQSRTDFLVF GGVIKDHLLD MEDEILLCSL
KGDGELTITR RLVPEAANAK SPSHPGPLLL VGTSPVVTPD DGSLMIVGGG ATCFSMGTFW
NKGISTLELA LPAAVENEAS PIPAYGWVHE KTVDIIPGEP RSLPLRNQAP NGAEGNANGS
VSVRIQPIPR VRLENAEDFA RIVREGRPVV LEGLNLGDCV SQWGNGDYVA KKVGTDRKVV
IHESTTPAMD FTTKNFRYVT TEFGDFMRRV EKGDRLYLRA LSTDKPTEKP AVLSDDFPSL
ATDFVLPPEL ALVGDRLFSS VLRVSGPVNM WLHYDVMANV YCQIGGSKRM ILFPPSDVEH
LGFAPGASSS SIDVFSTLFG ESSDSRYLAQ VTHPHEAVMT PGDVLFLPPL WLHTATPTSD
SSIAVNVFFR DLEGGCYAAG KDVYGNRDLA AYEKGRTDLT RIANSFQKLP AEAREFYLLR
LADELRRKAK GAQ
