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Alpha N-terminal protein methyltransferase 1 (EC 2.1.1.244) (Translation associated element 1) (X-Pro-Lys N-terminal protein methyltransferase 1) (NTM1)

 NTM1_YEAST              Reviewed;         232 AA.
P38340; D6VQQ8;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
18-JUL-2018, entry version 134.
RecName: Full=Alpha N-terminal protein methyltransferase 1;
EC=2.1.1.244;
AltName: Full=Translation associated element 1;
AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1;
Short=NTM1;
Name=TAE1; Synonyms=NTM1; OrderedLocusNames=YBR261C; ORFNames=YBR1729;
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 204508 / S288c;
PubMed=8465606; DOI=10.1002/yea.320090210;
Doignon F., Biteau N., Crouzet M., Aigle M.;
"The complete sequence of a 19,482 bp segment located on the right arm
of chromosome II from Saccharomyces cerevisiae.";
Yeast 9:189-199(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[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]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
DISRUPTION PHENOTYPE.
PubMed=19055778; DOI=10.1186/1471-2164-9-583;
Alamgir M., Eroukova V., Jessulat M., Xu J., Golshani A.;
"Chemical-genetic profile analysis in yeast suggests that a previously
uncharacterized open reading frame, YBR261C, affects protein
synthesis.";
BMC Genomics 9:583-583(2008).
[7]
FUNCTION.
PubMed=20481588; DOI=10.1021/bi100428x;
Webb K.J., Lipson R.S., Al-Hadid Q., Whitelegge J.P., Clarke S.G.;
"Identification of protein N-terminal methyltransferases in yeast and
humans.";
Biochemistry 49:5225-5235(2010).
-!- FUNCTION: Alpha-N-methyltransferase that methylates the N-terminus
of target proteins containing the N-terminal motif [Ala/Pro/Ser]-
Pro-Lys when the initiator Met is cleaved. Specifically catalyzes
mono-, di- or tri-methylation of exposed alpha-amino group of Ala
or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-
methylation of Pro in the Pro-Pro-Lys motif. Responsible for the
N-terminal methylation of the ribosomal proteins RPL12A, RPL12B,
RPS25A and RPS25B. {ECO:0000269|PubMed:20481588}.
-!- CATALYTIC ACTIVITY: 3 S-adenosyl-L-methionine + N-terminal-
(A,S)PK-[protein] = 3 S-adenosyl-L-homocysteine + N-terminal-
N,N,N-trimethyl-N-(A,S)PK-[protein].
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + N-terminal-PPK-
[protein] = 2 S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-
N-PPK-[protein].
-!- INTERACTION:
Q9P2A4:ABI3 (xeno); NbExp=3; IntAct=EBI-21116, EBI-742038;
P60709:ACTB (xeno); NbExp=3; IntAct=EBI-21116, EBI-353944;
P63261:ACTG1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-351292;
Q6RW13-2:AGTRAP (xeno); NbExp=3; IntAct=EBI-21116, EBI-11522760;
Q13155:AIMP2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-745226;
Q13867:BLMH (xeno); NbExp=3; IntAct=EBI-21116, EBI-718504;
Q9BV19:C1orf50 (xeno); NbExp=3; IntAct=EBI-21116, EBI-2874661;
P35520:CBS (xeno); NbExp=3; IntAct=EBI-21116, EBI-740135;
Q9C0F1:CEP44 (xeno); NbExp=3; IntAct=EBI-21116, EBI-744115;
Q53EZ4:CEP55 (xeno); NbExp=3; IntAct=EBI-21116, EBI-747776;
Q8NHQ1:CEP70 (xeno); NbExp=3; IntAct=EBI-21116, EBI-739624;
Q8NHQ1-3:CEP70 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11526150;
Q8TAP6:CEP76 (xeno); NbExp=3; IntAct=EBI-21116, EBI-742887;
Q9Y281:CFL2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-351218;
Q96DZ9-2:CMTM5 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11522780;
P38432:COIL (xeno); NbExp=3; IntAct=EBI-21116, EBI-945751;
Q15038:DAZAP2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-724310;
Q96MA1:DMRTB1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-954466;
Q96EY1-3:DNAJA3 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11526226;
Q9ULA0:DNPEP (xeno); NbExp=3; IntAct=EBI-21116, EBI-748356;
Q86UW9:DTX2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-740376;
Q5JST6:EFHC2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-2349927;
Q96A10:ERVK3-1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-10486892;
Q9NWS6:FAM118A (xeno); NbExp=3; IntAct=EBI-21116, EBI-8638992;
Q969F0:FATE1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-743099;
A0A0R4J2E4:FBF1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11525602;
O95073-2:FSBP (xeno); NbExp=3; IntAct=EBI-21116, EBI-10696047;
P02792:FTL (xeno); NbExp=3; IntAct=EBI-21116, EBI-713279;
O60547:GMDS (xeno); NbExp=3; IntAct=EBI-21116, EBI-746373;
Q14749:GNMT (xeno); NbExp=3; IntAct=EBI-21116, EBI-744239;
O15217:GSTA4 (xeno); NbExp=3; IntAct=EBI-21116, EBI-752440;
P07910:HNRNPC (xeno); NbExp=3; IntAct=EBI-21116, EBI-357966;
P07910-2:HNRNPC (xeno); NbExp=3; IntAct=EBI-21116, EBI-5280084;
Q9NSC5:HOMER3 (xeno); NbExp=3; IntAct=EBI-21116, EBI-748420;
P00492:HPRT1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-748210;
Q9BPX1:HSD17B14 (xeno); NbExp=3; IntAct=EBI-21116, EBI-742664;
P38646:HSPA9 (xeno); NbExp=3; IntAct=EBI-21116, EBI-354932;
P12268:IMPDH2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-353389;
Q96AA8:JAKMIP2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-752007;
Q8WVF5:KCTD4 (xeno); NbExp=3; IntAct=EBI-21116, EBI-741463;
Q5VWX1:KHDRBS2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-742808;
O75525:KHDRBS3 (xeno); NbExp=3; IntAct=EBI-21116, EBI-722504;
O95198:KLHL2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-746999;
P07195:LDHB (xeno); NbExp=3; IntAct=EBI-21116, EBI-358748;
Q8NDC0:MAPK1IP1L (xeno); NbExp=3; IntAct=EBI-21116, EBI-741424;
P20591:MX1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-929476;
Q99836:MYD88 (xeno); NbExp=3; IntAct=EBI-21116, EBI-447677;
Q7Z6G3-2:NECAB2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-10172876;
P23511-2:NFYA (xeno); NbExp=3; IntAct=EBI-21116, EBI-11061759;
P15531:NME1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-741141;
Q9HAN9:NMNAT1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-3917542;
Q8IXK0-5:PHC2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11527347;
Q9NRY6:PLSCR3 (xeno); NbExp=3; IntAct=EBI-21116, EBI-750734;
Q96CD2:PPCDC (xeno); NbExp=3; IntAct=EBI-21116, EBI-724333;
P60891:PRPS1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-749195;
P62333:PSMC6 (xeno); NbExp=3; IntAct=EBI-21116, EBI-357669;
P61289:PSME3 (xeno); NbExp=3; IntAct=EBI-21116, EBI-355546;
Q03393:PTS (xeno); NbExp=3; IntAct=EBI-21116, EBI-712344;
Q9UHX1-2:PUF60 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11529177;
Q9UHX1-5:PUF60 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11526420;
Q9UHX1-6:PUF60 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11085298;
A0A0A0MQS1:PYCR3 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11528247;
Q96PU8:QKI (xeno); NbExp=3; IntAct=EBI-21116, EBI-945792;
Q9UI14:RABAC1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-712367;
P38159:RBMX (xeno); NbExp=3; IntAct=EBI-21116, EBI-743526;
Q15415:RBMY1J (xeno); NbExp=3; IntAct=EBI-21116, EBI-8642021;
Q93062-3:RBPMS (xeno); NbExp=3; IntAct=EBI-21116, EBI-740343;
O95199:RCBTB2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-742404;
Q96HR9:REEP6 (xeno); NbExp=3; IntAct=EBI-21116, EBI-750345;
O75150:RNF40 (xeno); NbExp=3; IntAct=EBI-21116, EBI-744408;
Q99942:RNF5 (xeno); NbExp=3; IntAct=EBI-21116, EBI-348482;
P49247:RPIA (xeno); NbExp=3; IntAct=EBI-21116, EBI-744831;
Q9NQC3-3:RTN4 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11526335;
Q8N6K7-2:SAMD3 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11528848;
Q15427:SF3B4 (xeno); NbExp=3; IntAct=EBI-21116, EBI-348469;
Q9Y371:SH3GLB1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-2623095;
Q8IUQ4-2:SIAH1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11522811;
Q16637:SMN2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-395421;
Q16637-3:SMN2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-395447;
P04179:SOD2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-716989;
Q8NA61-2:SPERT (xeno); NbExp=3; IntAct=EBI-21116, EBI-11524851;
O43791:SPOP (xeno); NbExp=3; IntAct=EBI-21116, EBI-743549;
O60232:SSSCA1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-741415;
Q9Y2D8:SSX2IP (xeno); NbExp=3; IntAct=EBI-21116, EBI-2212028;
Q96MF2:STAC3 (xeno); NbExp=3; IntAct=EBI-21116, EBI-745680;
Q8N0S2:SYCE1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-6872807;
P48775:TDO2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-743494;
Q12800:TFCP2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-717422;
Q9NVV9:THAP1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-741515;
Q8WW34-2:TMEM239 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11528917;
Q15025:TNIP1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-357849;
Q9BUZ4:TRAF4 (xeno); NbExp=3; IntAct=EBI-21116, EBI-3650647;
O00463:TRAF5 (xeno); NbExp=3; IntAct=EBI-21116, EBI-523498;
Q13049:TRIM32 (xeno); NbExp=3; IntAct=EBI-21116, EBI-742790;
O00635:TRIM38 (xeno); NbExp=3; IntAct=EBI-21116, EBI-2130415;
Q9BYV6-2:TRIM55 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11522718;
Q86WT6-2:TRIM69 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11525489;
P63279:UBE2I (xeno); NbExp=3; IntAct=EBI-21116, EBI-80168;
Q5T124-6:UBXN11 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11524408;
E7EUC7:UGP2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11528286;
O95045-2:UPP2 (xeno); NbExp=3; IntAct=EBI-21116, EBI-11528386;
P98170:XIAP (xeno); NbExp=3; IntAct=EBI-21116, EBI-517127;
O96006:ZBED1 (xeno); NbExp=3; IntAct=EBI-21116, EBI-740037;
Q9HCK0:ZBTB26 (xeno); NbExp=3; IntAct=EBI-21116, EBI-3918996;
Q96BR9:ZBTB8A (xeno); NbExp=3; IntAct=EBI-21116, EBI-742740;
Q9UDV6:ZNF212 (xeno); NbExp=3; IntAct=EBI-21116, EBI-1640204;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
-!- DISRUPTION PHENOTYPE: Defects in both translation efficiency and
fidelity. {ECO:0000269|PubMed:19055778}.
-!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1
family. {ECO:0000305}.
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EMBL; X70529; CAA49926.1; -; Genomic_DNA.
EMBL; Z36130; CAA85224.1; -; Genomic_DNA.
EMBL; BK006936; DAA07378.1; -; Genomic_DNA.
PIR; S32963; S32963.
RefSeq; NP_009820.1; NM_001178609.1.
ProteinModelPortal; P38340; -.
SMR; P38340; -.
BioGrid; 32957; 217.
DIP; DIP-4951N; -.
IntAct; P38340; 150.
STRING; 4932.YBR261C; -.
iPTMnet; P38340; -.
MaxQB; P38340; -.
PaxDb; P38340; -.
PRIDE; P38340; -.
EnsemblFungi; YBR261C; YBR261C; YBR261C.
GeneID; 852564; -.
KEGG; sce:YBR261C; -.
EuPathDB; FungiDB:YBR261C; -.
SGD; S000000465; TAE1.
GeneTree; ENSGT00390000008371; -.
InParanoid; P38340; -.
KO; K16219; -.
OMA; PVYMIAC; -.
OrthoDB; EOG092C2UR7; -.
BioCyc; YEAST:G3O-29185-MONOMER; -.
PRO; PR:P38340; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IDA:SGD.
GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
GO; GO:0018016; P:N-terminal peptidyl-proline dimethylation; IDA:SGD.
InterPro; IPR008576; MeTrfase_NTM1.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR12753; PTHR12753; 1.
Pfam; PF05891; Methyltransf_PK; 1.
PIRSF; PIRSF016958; DUF858_MeTrfase_lik; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Methyltransferase; Reference proteome;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 232 Alpha N-terminal protein
methyltransferase 1.
/FTId=PRO_0000119292.
REGION 123 124 S-adenosyl-L-methionine binding.
{ECO:0000250}.
BINDING 71 71 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
BINDING 76 76 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 139 139 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
SEQUENCE 232 AA; 26068 MW; 66699F37B0013088 CRC64;
MDVPADSHIK YEDAIDYWTD VDATVDGVLG GYGEGTVVPT MDVLGSNNFL RKLKSRMLPQ
ENNVKYAVDI GAGIGRVSKT MLHKHAAKID LVEPVKPFIE QMHVELAELK DKGQIGQIYE
VGMQDWTPDA GKYWLIWCQW CVGHLPDAEL VAFLKRCIVG LQPNGTIVVK ENNTPTDTDD
FDETDSSVTR SDAKFRQIFE EAGLKLIASE RQRGLPRELY PVRMYALKPM PN


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