AB140_YEAST
ID AB140_YEAST Reviewed; 628 AA.
AC Q08641; D6W2U2; Q08644;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=tRNA(Thr) (cytosine(32)-N(3))-methyltransferase;
DE EC=2.1.1.268 {ECO:0000269|PubMed:21518804, ECO:0000269|PubMed:21518805};
DE AltName: Full=Actin-binding protein of 140 kDa;
DE AltName: Full=tRNA methyltransferase of 140 kDa;
GN Name=ABP140; Synonyms=TRM140; OrderedLocusNames=YOR239W; ORFNames=YOR240W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972580;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1575::aid-yea45>3.0.co;2-e;
RA Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.;
RT "Sequence and analysis of a 26.9 kb fragment from chromosome XV of the
RT yeast Saccharomyces cerevisiae.";
RL Yeast 12:1575-1586(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 2-13; 39-73; 103-116;
RP 245-287; 561-575 AND 599-609, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=BJ5457;
RX PubMed=9467951; DOI=10.1038/sj.onc.1201487;
RA Asakura T., Sasaki T., Nagano F., Satoh A., Obaishi H., Nishioka H.,
RA Imamura H., Hotta K., Tanaka K., Nakanishi H., Takai Y.;
RT "Isolation and characterization of a novel actin filament-binding protein
RT from Saccharomyces cerevisiae.";
RL Oncogene 16:121-130(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-321 AND SER-326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-150 AND SER-326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-321; SER-326 AND
RP THR-347, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP MRNA TRANSLATION.
RX PubMed=21792172; DOI=10.1038/emboj.2011.247;
RA Kilchert C., Spang A.;
RT "Cotranslational transport of ABP140 mRNA to the distal pole of S.
RT cerevisiae.";
RL EMBO J. 30:3567-3580(2011).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21518804; DOI=10.1261/rna.2652611;
RA D'Silva S., Haider S.J., Phizicky E.M.;
RT "A domain of the actin binding protein Abp140 is the yeast
RT methyltransferase responsible for 3-methylcytidine modification in the tRNA
RT anti-codon loop.";
RL RNA 17:1100-1110(2011).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21518805; DOI=10.1261/rna.2653411;
RA Noma A., Yi S., Katoh T., Takai Y., Suzuki T., Suzuki T.;
RT "Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine
RT at position 32 of tRNAs in Saccharomyces cerevisiae.";
RL RNA 17:1111-1119(2011).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH SES1.
RX PubMed=28003514; DOI=10.1261/rna.059667.116;
RA Han L., Marcus E., D'Silva S., Phizicky E.M.;
RT "S. cerevisiae Trm140 has two recognition modes for 3-methylcytidine
RT modification of the anticodon loop of tRNA substrates.";
RL RNA 23:406-419(2017).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates N(3)-methylcytidine modification of residue 32 of the tRNA
CC anticodon loop of tRNA(Thr) and tRNA(Ser) (PubMed:21518804,
CC PubMed:21518805, PubMed:28003514). N(3)-methylcytidine methylation of
CC tRNA(Thr) requires the N6-threonylcarbamoylation of tRNA (t6A37) by the
CC EKC/KEOPS complex as prerequisite (PubMed:28003514). N(3)-
CC methylcytidine methylation of tRNA(Ser) requires the formation of N(6)-
CC dimethylallyladenosine(37) (i6A37) by MOD5 as prerequisite
CC (PubMed:28003514). Methylation of tRNA(Ser) is also stimulated by SES1
CC (PubMed:28003514). Binds F-actin and shows weak F-actin cross-linking
CC activity (PubMed:9467951). {ECO:0000269|PubMed:21518804,
CC ECO:0000269|PubMed:21518805, ECO:0000269|PubMed:28003514,
CC ECO:0000269|PubMed:9467951}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA(Thr) + S-adenosyl-L-methionine = H(+) +
CC N(3)-methylcytidine(32) in tRNA(Thr) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:50960, Rhea:RHEA-COMP:12850, Rhea:RHEA-COMP:12852,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74894, ChEBI:CHEBI:82748; EC=2.1.1.268;
CC Evidence={ECO:0000269|PubMed:21518804, ECO:0000269|PubMed:21518805,
CC ECO:0000269|PubMed:28003514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA(Ser) + S-adenosyl-L-methionine = H(+) +
CC N(3)-methylcytidine(32) in tRNA(Ser) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:50956, Rhea:RHEA-COMP:12849, Rhea:RHEA-COMP:12851,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74894, ChEBI:CHEBI:82748; EC=2.1.1.268;
CC Evidence={ECO:0000269|PubMed:21518804, ECO:0000269|PubMed:21518805,
CC ECO:0000269|PubMed:28003514};
CC -!- SUBUNIT: Interacts with SES1. {ECO:0000269|PubMed:28003514}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9467951}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9467951}. Note=Cytoplasmic
CC and cortical cytoskeleton. {ECO:0000269|PubMed:9467951}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=1;
CC Name=1;
CC IsoId=Q08641-1; Sequence=Displayed;
CC -!- MISCELLANEOUS: N- and C-terminal domains are encoded in separate ORFs
CC that are translated into one protein via a +1 frameshift
CC (PubMed:9467951). ABP140 mRNA translation follows a cotranslational
CC transport: mRNA is transported to the distal pole of the mother cell,
CC independently of the SHE machinery, and follows a translational
CC coupling, in which ABP140 mRNA is tethered to actin cables via its
CC nascent protein product and is transported to the distal pole by actin
CC retrograde flow (PubMed:21792172). {ECO:0000305|PubMed:21792172,
CC ECO:0000305|PubMed:9467951}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by ribosomal frameshifting between
CC codon Leu-277 and Gly-278.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC {ECO:0000305}.
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DR EMBL; Z75147; CAA99460.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z75147; CAA99461.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006948; DAA11008.1; -; Genomic_DNA.
DR RefSeq; NP_014882.4; NM_001183658.6. [Q08641-1]
DR PDB; 7AD9; EM; 3.50 A; A/C/E/G/L=1-17.
DR PDB; 7BTE; EM; 4.20 A; L/M/N=1-17.
DR PDBsum; 7AD9; -.
DR PDBsum; 7BTE; -.
DR AlphaFoldDB; Q08641; -.
DR SMR; Q08641; -.
DR BioGRID; 34631; 39.
DR DIP; DIP-4117N; -.
DR IntAct; Q08641; 27.
DR STRING; 4932.YOR239W; -.
DR iPTMnet; Q08641; -.
DR MaxQB; Q08641; -.
DR PaxDb; Q08641; -.
DR PRIDE; Q08641; -.
DR EnsemblFungi; YOR239W_mRNA; YOR239W; YOR239W. [Q08641-1]
DR GeneID; 854414; -.
DR KEGG; sce:YOR239W; -.
DR SGD; S000005765; ABP140.
DR VEuPathDB; FungiDB:YOR239W; -.
DR eggNOG; KOG2361; Eukaryota.
DR GeneTree; ENSGT00940000171213; -.
DR HOGENOM; CLU_029724_1_2_1; -.
DR InParanoid; Q08641; -.
DR OMA; HEANNIV; -.
DR BioCyc; YEAST:G3O-33735-MON; -.
DR BRENDA; 2.1.1.268; 984.
DR PRO; PR:Q08641; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08641; protein.
DR GO; GO:0005884; C:actin filament; IDA:SGD.
DR GO; GO:0032432; C:actin filament bundle; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0052735; F:tRNA (cytosine-3-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IMP:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR026113; MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22809; PTHR22809; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methyltransferase; Phosphoprotein;
KW Reference proteome; Ribosomal frameshifting; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9467951"
FT CHAIN 2..628
FT /note="tRNA(Thr) (cytosine(32)-N(3))-methyltransferase"
FT /id="PRO_0000204458"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..230
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 399
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 403
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 441
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 466
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 492
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 493
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 515
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 347
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:7AD9"
SQ SEQUENCE 628 AA; 71486 MW; 74F9CA30BC5BCABF CRC64;
MGVADLIKKF ESISKEEGDA TVDTNSSSKP LKSNDETKEL HQQESTAVPQ EVDVNEEFEN
EPETINSSRT AEKPLETNLP KPETNEEDEE EGSMSENKIY SKGENADINV NDFQEYKEME
NTGAEVLASS VEESDAIQEG VAEETEGIAT PKQKENEKND ESEEESANNA SEPAEEYSQS
EEDADIEQSN GKETENAENA SQQANDGSTS TTTSKNKKKK NKKKNKKKRN GNVNTNANVD
DSTKTGENDD TTGDTTSSTT SAIQEVNDLE VVDDSCLGID QQHNREHLKA LTQDVKEETL
ENIAHEGRGD NTGDQNAVEK SDFEKSDTEG SRIGRDLPFE FGKRNLTEES DVWDHNAWDN
VEWGEEQVQQ AEEKIKEQFK HPVPEFDKKL YNENPARYWD IFYKNNKENF FKDRKWLQIE
FPILYASTRK DAEPVTIFEI GCGAGNTFFP ILKDNENENL RIIAADFAPR AVELVKNSEQ
FNPKYGHATV WDLANPDGNL PDGVEPHSVD IAVMIFVFSA LAPNQWDQAM DNLHKILKPG
GKIIFRDYGA YDLTQVRFKK NRILEENFYV RGDGTRVYFF SEEKLREIFT KKYFLENKIG
TDRRLLVNRK RQLKMYRCWV QAVFDVPQ
