(data stored in ACNUC7421 zone)

SWISSPROT: Q750R4_ASHGO

ID   Q750R4_ASHGO            Unreviewed;       370 AA.
AC   Q750R4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 117.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
DE            EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
GN   ORFNames=AGOS_AGL122W {ECO:0000313|EMBL:AAS54369.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54369.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54369.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Cotranslationally removes the N-terminal methionine from
CC       nascent proteins. The N-terminal methionine is often cleaved when the
CC       second residue in the primary sequence is small and uncharged (Met-
CC       Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
CC       {ECO:0000256|RuleBase:RU003653}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal amino acids, preferentially methionine,
CC         from peptides and arylamides.; EC=3.4.11.18;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03174,
CC         ECO:0000256|RuleBase:RU003653};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03174,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03174,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03174,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03174,
CC         ECO:0000256|RuleBase:RU003653};
CC       Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC       and a low affinity metal-binding site. The true nature of the
CC       physiological cofactor is under debate. The enzyme is active with
CC       cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC       aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC       physiological conditions, and the catalytically relevant metal-binding
CC       site has been assigned to the histidine-containing high-affinity site.
CC       {ECO:0000256|HAMAP-Rule:MF_03174, ECO:0000256|RuleBase:RU003653};
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_03174}.
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DR   EMBL; AE016820; AAS54369.1; -; Genomic_DNA.
DR   RefSeq; NP_986545.1; NM_211607.1.
DR   STRING; 33169.AAS54369; -.
DR   MEROPS; M24.001; -.
DR   EnsemblFungi; AAS54369; AAS54369; AGOS_AGL122W.
DR   GeneID; 4622844; -.
DR   KEGG; ago:AGOS_AGL122W; -.
DR   HOGENOM; HOG000030427; -.
DR   InParanoid; Q750R4; -.
DR   KO; K01265; -.
DR   OMA; GDHAYTF; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0022626; C:cytosolic ribosome; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:EnsemblFungi.
DR   GO; GO:0035551; P:protein initiator methionine removal involved in protein maturation; IEA:EnsemblFungi.
DR   CDD; cd01086; MetAP1; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   HAMAP; MF_01974; MetAP_1; 1.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR002467; Pept_M24A_MAP1.
DR   InterPro; IPR031615; Zfn-C6H2.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF15801; zf-C6H2; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR   PROSITE; PS00680; MAP_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750R4.
DR   SWISS-2DPAGE; Q750R4.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_03174,
KW   ECO:0000256|RuleBase:RU003653};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03174};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03174,
KW   ECO:0000256|RuleBase:RU003653};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_03174, ECO:0000256|RuleBase:RU003653};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          6..51
FT                   /note="zf-C6H2"
FT                   /evidence="ECO:0000259|Pfam:PF15801"
FT   DOMAIN          120..348
FT                   /note="Peptidase_M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   METAL           202
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   METAL           213
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   METAL           213
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   METAL           277
FT                   /note="Divalent metal cation 2; catalytic; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   METAL           310
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   METAL           341
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   METAL           341
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   BINDING         185
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT   BINDING         284
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
SQ   SEQUENCE   370 AA;  41385 MW;  92C175DE6FC29072 CRC64;
     MTTVYCASLQ CGKATDSALK CPLCLKQGIQ SVFCNESCYR DCYKSHKALH IKDDSDKSYD
     PFQNFKYTGE LRAQYPLTPK RAVPDDIEKP DWAANGLPLS EQRNDRLNKI PVYNKEEIKR
     IRKACMLGRE VLDIAAAALR PGITTDELDE IVHAETIKRG AYPSPLNYYN FPKSVCTSVN
     EVICHGIPDK YVLKDGDIVN LDVSLFYQGM HADLNETYYV GDNISKEALN TVETARECLK
     IATKMCKPGV RFQDLGDAIE KHAKQNKCSV VKTYCGHGVG KFFHCSPSIP HYANNKTPGV
     MKPGMVFTIE PMINEGVWQD LTWPDDWTAA TKDGKLSAQF ENSLLITETG VEILTARTKK
     SPGGPRPRTK
//

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