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tRNA(Thr) (cytosine(32)-N(3))-methyltransferase (EC 2.1.1.268) (Actin-binding protein of 140 kDa) (tRNA methyltransferase of 140 kDa)

 AB140_YEAST             Reviewed;         628 AA.
Q08641; D6W2U2; Q08644;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 149.
RecName: Full=tRNA(Thr) (cytosine(32)-N(3))-methyltransferase;
EC=2.1.1.268 {ECO:0000269|PubMed:21518804, ECO:0000269|PubMed:21518805};
AltName: Full=Actin-binding protein of 140 kDa;
AltName: Full=tRNA methyltransferase of 140 kDa;
Name=ABP140; Synonyms=TRM140; OrderedLocusNames=YOR239W;
ORFNames=YOR240W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8972580;
DOI=10.1002/(SICI)1097-0061(199612)12:15<1575::AID-YEA45>3.0.CO;2-E;
Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.;
"Sequence and analysis of a 26.9 kb fragment from chromosome XV of the
yeast Saccharomyces cerevisiae.";
Yeast 12:1575-1586(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PARTIAL NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 2-13; 39-73; 103-116;
245-287; 561-575 AND 599-609, FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=BJ5457;
PubMed=9467951; DOI=10.1038/sj.onc.1201487;
Asakura T., Sasaki T., Nagano F., Satoh A., Obaishi H., Nishioka H.,
Imamura H., Hotta K., Tanaka K., Nakanishi H., Takai Y.;
"Isolation and characterization of a novel actin filament-binding
protein from Saccharomyces cerevisiae.";
Oncogene 16:121-130(1998).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-321 AND SER-326,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-150 AND SER-326, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-321; SER-326 AND
THR-347, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[9]
MRNA TRANSLATION.
PubMed=21792172; DOI=10.1038/emboj.2011.247;
Kilchert C., Spang A.;
"Cotranslational transport of ABP140 mRNA to the distal pole of S.
cerevisiae.";
EMBO J. 30:3567-3580(2011).
[10]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=21518804; DOI=10.1261/rna.2652611;
D'Silva S., Haider S.J., Phizicky E.M.;
"A domain of the actin binding protein Abp140 is the yeast
methyltransferase responsible for 3-methylcytidine modification in the
tRNA anti-codon loop.";
RNA 17:1100-1110(2011).
[11]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=21518805; DOI=10.1261/rna.2653411;
Noma A., Yi S., Katoh T., Takai Y., Suzuki T., Suzuki T.;
"Actin-binding protein ABP140 is a methyltransferase for 3-
methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae.";
RNA 17:1111-1119(2011).
-!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
mediates 3-methylcytidine modification of residue 32 of the tRNA
anticodon loop of tRNA(Thr) and tRNA(Ser). Binds F-actin and shows
weak F-actin cross-linking activity. {ECO:0000269|PubMed:21518804,
ECO:0000269|PubMed:21518805, ECO:0000269|PubMed:9467951}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(32) in
tRNA(Thr) = S-adenosyl-L-homocysteine + N(3)-methylcytosine(32) in
tRNA(Thr). {ECO:0000269|PubMed:21518804,
ECO:0000269|PubMed:21518805}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(32) in
tRNA(Ser) = S-adenosyl-L-homocysteine + N(3)-methylcytosine(32) in
tRNA(Ser). {ECO:0000269|PubMed:21518804,
ECO:0000269|PubMed:21518805}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9467951}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9467951}.
Note=Cytoplasmic and cortical cytoskeleton.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=1;
Name=1;
IsoId=Q08641-1; Sequence=Displayed;
Note=Produced by ribosomal frameshifting between codon Leu-277
and Gly-278.;
-!- MISCELLANEOUS: N- and C-terminal domains are encoded in separate
ORFs that are translated into one protein via a +1 frameshift
(PubMed:9467951). ABP140 mRNA translation follows a
cotranslational transport: mRNA is transported to the distal pole
of the mother cell, independently of the SHE machinery, and
follows a translational coupling, in which ABP140 mRNA is tethered
to actin cables via its nascent protein product and is transported
to the distal pole by actin retrograde flow (PubMed:21792172).
{ECO:0000305|PubMed:21792172, ECO:0000305|PubMed:9467951}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. METL
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z75147; CAA99460.1; ALT_SEQ; Genomic_DNA.
EMBL; Z75147; CAA99461.1; ALT_SEQ; Genomic_DNA.
EMBL; BK006948; DAA11008.1; -; Genomic_DNA.
RefSeq; NP_014882.4; NM_001183658.6. [Q08641-1]
ProteinModelPortal; Q08641; -.
SMR; Q08641; -.
BioGrid; 34631; 34.
DIP; DIP-4117N; -.
IntAct; Q08641; 27.
MINT; MINT-493479; -.
STRING; 4932.YOR239W; -.
iPTMnet; Q08641; -.
MaxQB; Q08641; -.
PRIDE; Q08641; -.
EnsemblFungi; YOR239W; YOR239W; YOR239W. [Q08641-1]
GeneID; 854414; -.
KEGG; sce:YOR239W; -.
EuPathDB; FungiDB:YOR239W; -.
SGD; S000005765; ABP140.
GeneTree; ENSGT00520000055554; -.
HOGENOM; HOG000033747; -.
InParanoid; Q08641; -.
KO; K17053; -.
OMA; HEANNIV; -.
OrthoDB; EOG092C3LCG; -.
BioCyc; YEAST:G3O-33735-MONOMER; -.
BRENDA; 2.1.1.268; 984.
PRO; PR:Q08641; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0030479; C:actin cortical patch; IDA:SGD.
GO; GO:0005884; C:actin filament; IDA:SGD.
GO; GO:0032432; C:actin filament bundle; IDA:SGD.
GO; GO:0051015; F:actin filament binding; IDA:SGD.
GO; GO:0030674; F:protein binding, bridging; IDA:SGD.
GO; GO:0052735; F:tRNA (cytosine-3-)-methyltransferase activity; IDA:SGD.
GO; GO:0051017; P:actin filament bundle assembly; IDA:SGD.
GO; GO:0030488; P:tRNA methylation; IMP:SGD.
InterPro; IPR013217; Methyltransf_12.
InterPro; IPR026113; MeTrfase.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR22809; PTHR22809; 1.
Pfam; PF08242; Methyltransf_12; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Methyltransferase; Phosphoprotein;
Reference proteome; Ribosomal frameshifting; S-adenosyl-L-methionine;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9467951}.
CHAIN 2 628 tRNA(Thr) (cytosine(32)-N(3))-
methyltransferase.
/FTId=PRO_0000204458.
MOD_RES 93 93 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 150 150 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 347 347 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
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


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