NTA1_YEAST
ID NTA1_YEAST Reviewed; 457 AA.
AC P40354; D6VWN3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein N-terminal amidase;
DE Short=NT-amidase;
DE EC=3.5.1.-;
GN Name=NTA1; OrderedLocusNames=YJR062C; ORFNames=J1742;
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].
RX PubMed=7744855; DOI=10.1074/jbc.270.20.12065;
RA Baker R.T., Varshavsky A.;
RT "Yeast N-terminal amidase. A new enzyme and component of the N-end rule
RT pathway.";
RL J. Biol. Chem. 270:12065-12074(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Deamidates N-terminal Asn and Gln. Component of a targeting
CC complex in the N-end rule pathway.
CC -!- MISCELLANEOUS: Present with 1640 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC {ECO:0000305}.
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DR EMBL; L35564; AAB59320.1; -; Genomic_DNA.
DR EMBL; Z49562; CAA89590.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39288.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08849.1; -; Genomic_DNA.
DR PIR; S47938; S47938.
DR RefSeq; NP_012596.3; NM_001181720.3.
DR AlphaFoldDB; P40354; -.
DR SMR; P40354; -.
DR BioGRID; 33819; 48.
DR DIP; DIP-6478N; -.
DR IntAct; P40354; 23.
DR STRING; 4932.YJR062C; -.
DR iPTMnet; P40354; -.
DR MaxQB; P40354; -.
DR PaxDb; P40354; -.
DR PRIDE; P40354; -.
DR EnsemblFungi; YJR062C_mRNA; YJR062C; YJR062C.
DR GeneID; 853525; -.
DR KEGG; sce:YJR062C; -.
DR SGD; S000003823; NTA1.
DR VEuPathDB; FungiDB:YJR062C; -.
DR eggNOG; ENOG502QVBD; Eukaryota.
DR HOGENOM; CLU_009854_1_1_1; -.
DR InParanoid; P40354; -.
DR OMA; VKILCWD; -.
DR BioCyc; YEAST:G3O-31695-MON; -.
DR BRENDA; 3.5.1.121; 984.
DR BRENDA; 3.5.1.122; 984.
DR PRO; PR:P40354; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40354; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IDA:SGD.
DR GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; IDA:SGD.
DR GO; GO:0031365; P:N-terminal protein amino acid modification; IMP:SGD.
DR GO; GO:0030163; P:protein catabolic process; IMP:SGD.
DR GO; GO:0036211; P:protein modification process; IBA:GO_Central.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR039703; Nta1.
DR PANTHER; PTHR11750; PTHR11750; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..457
FT /note="Protein N-terminal amidase"
FT /id="PRO_0000204068"
FT DOMAIN 19..453
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 63
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 136
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 187
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 457 AA; 51897 MW; E6259FBBFB25A889 CRC64;
MLIDAIHGAK MSTKLLVSLK VLVIQLNPQI GQVDQTIKRT WSILDKVTKS ATYVKPDIIL
FPEFALTGYS FHARKDILPY VTKKDEGPSF ELAKSISEKF QCYTIIGYPE DDDEQKLYNS
ALVVNPQGEQ IFNYRKTFLY DTEMNWDCEE NPEGFQTFPM DFSKCAKLSN EDSYNRDVTL
KASIGICMDL SPYKFMAPFN HFEFSSFCVD NNVELILCPM AWLNSTSITD KQTLHNNSLL
EAAKNKIAFA LKEQGLPLAG SQGIYQLKIG DSQRTPRVPS DDSTSEYKDM DEPDMSNVNY
WILRFFPFLY FKSRINWFKN SSLIESILGK TRMPLDHEYY KDGKHKEDTI DLLDSEEVIK
DTVLEKTFLG TSLGQPWKFQ GKNAILVLAN RCGTEDGTTI FAGSSGIYKF NGKKPKGSQD
DDESSLDSLN ESVELLGNLG KGLEGAILRE VQFEVFR
