NTA1_SCHPO
ID NTA1_SCHPO Reviewed; 286 AA.
AC O60178;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein N-terminal amidase;
DE Short=NT-amidase;
DE EC=3.5.1.-;
GN Name=nta1; ORFNames=SPBC23E6.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Deamidates N-terminal Asn and Gln. Component of a targeting
CC complex in the N-end rule pathway (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA18871.1; -; Genomic_DNA.
DR PIR; T39937; T39937.
DR RefSeq; NP_596603.1; NM_001022524.2.
DR AlphaFoldDB; O60178; -.
DR SMR; O60178; -.
DR BioGRID; 277186; 12.
DR STRING; 4896.SPBC23E6.03c.1; -.
DR MaxQB; O60178; -.
DR PaxDb; O60178; -.
DR EnsemblFungi; SPBC23E6.03c.1; SPBC23E6.03c.1:pep; SPBC23E6.03c.
DR GeneID; 2540661; -.
DR KEGG; spo:SPBC23E6.03c; -.
DR PomBase; SPBC23E6.03c; nta1.
DR VEuPathDB; FungiDB:SPBC23E6.03c; -.
DR eggNOG; KOG0806; Eukaryota.
DR HOGENOM; CLU_009854_1_1_1; -.
DR InParanoid; O60178; -.
DR OMA; VKILCWD; -.
DR PhylomeDB; O60178; -.
DR PRO; PR:O60178; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; ISO:PomBase.
DR GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..286
FT /note="Protein N-terminal amidase"
FT /id="PRO_0000314759"
FT DOMAIN 1..286
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 121
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 155
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 286 AA; 32427 MW; D069C63AAF898988 CRC64;
MKFGCVQFFP KLGKVNENIV HLRQLLDQHS EALQSVKLLV FPEMCLTGYN FKNSESIQPF
LENVTSNHCP SIQFAQEVSE QYRCYTIIGF PEFQNSNGIS TLYNSTALIS PKKELLNVYH
KHFLFETDKS WATEGKGFSF EPCIPELGPI SMAICMDINP YDFKAPFEKF EYANFILREL
EHQQMVSSNV SRPIICLSMA WLVSDDKVID ASLPDIKNLH YWTTRLSPLI NSNTDAIVLV
ANRWGKENDL NFSGTSCIME LSQGRAILHG VLKAAENGIV VGELEK
