(data stored in ACNUC7421 zone)

SWISSPROT: Q751I9_ASHGO

ID   Q751I9_ASHGO            Unreviewed;       349 AA.
AC   Q751I9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 2.
DT   11-DEC-2019, entry version 116.
DE   RecName: Full=Methionine aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_03175};
DE            Short=MAP 2 {ECO:0000256|HAMAP-Rule:MF_03175};
DE            Short=MetAP 2 {ECO:0000256|HAMAP-Rule:MF_03175};
DE            EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_03175};
DE   AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_03175};
GN   Name=MAP2 {ECO:0000256|HAMAP-Rule:MF_03175};
GN   ORFNames=AGOS_AGL283W {ECO:0000313|EMBL:AAS54208.2};
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:AAS54208.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54208.2, 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). {ECO:0000256|HAMAP-
CC       Rule:MF_03175, ECO:0000256|RuleBase:RU003653,
CC       ECO:0000256|SAAS:SAAS00103118}.
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_03175,
CC         ECO:0000256|RuleBase:RU003653, ECO:0000256|SAAS:SAAS01125695};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03175,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03175,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03175,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03175,
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_03175, ECO:0000256|RuleBase:RU003653};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|SAAS:SAAS01092738};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS01092737};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|SAAS:SAAS01092736};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03175,
CC       ECO:0000256|SAAS:SAAS00103115}.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase eukaryotic type 2 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_03175, ECO:0000256|SAAS:SAAS00888053}.
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DR   EMBL; AE016820; AAS54208.2; -; Genomic_DNA.
DR   RefSeq; NP_986384.2; NM_211446.2.
DR   STRING; 33169.AAS54208; -.
DR   EnsemblFungi; AAS54208; AAS54208; AGOS_AGL283W.
DR   GeneID; 4622677; -.
DR   KEGG; ago:AGOS_AGL283W; -.
DR   HOGENOM; HOG000226278; -.
DR   InParanoid; Q751I9; -.
DR   KO; K01265; -.
DR   OMA; NEIAAHY; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035551; P:protein initiator methionine removal involved in protein maturation; IEA:EnsemblFungi.
DR   CDD; cd01088; MetAP2; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   HAMAP; MF_03175; MetAP_2_euk; 1.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR002468; Pept_M24A_MAP2.
DR   InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   TIGRFAMs; TIGR00501; met_pdase_II; 1.
DR   PROSITE; PS01202; MAP_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q751I9.
DR   SWISS-2DPAGE; Q751I9.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_03175,
KW   ECO:0000256|RuleBase:RU003653, ECO:0000256|SAAS:SAAS00103116};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03175, ECO:0000256|SAAS:SAAS00103101};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03175, ECO:0000256|SAAS:SAAS00103119};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03175,
KW   ECO:0000256|RuleBase:RU003653, ECO:0000256|SAAS:SAAS00103103};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_03175, ECO:0000256|RuleBase:RU003653,
KW   ECO:0000256|SAAS:SAAS00103105};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          32..336
FT                   /note="Peptidase_M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   METAL           123
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   METAL           134
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   METAL           134
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   METAL           203
FT                   /note="Divalent metal cation 2; catalytic; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   METAL           236
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   METAL           330
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   METAL           330
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   BINDING         103
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
FT   BINDING         211
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03175"
SQ   SEQUENCE   349 AA;  39310 MW;  38EE016664ECF925 CRC64;
     MDYGQDFNVA RVTDAERRYE ERDRARAEEW NDMRKGAEIH RRVRRHLQNR LRPGQTLTEV
     VELVENATRK FTGTDEHGRF AATPKAQGIG FPTGVSLNHC AAHFTPNAGD TTVLRHEDVM
     KVDFGVQVNG HIIDSAWTVT FDPRYDPLLE AVREATYTGI REAGIDVRLT DIGEAIQEVM
     ESYEVTLGGQ TYQVRPCRNL CGHNIVPYQI HGGKSVPIVK NGDETKMEEG EHFAIETFGT
     TGRGYVVQSG ECSHYAKNPG ALPAPTLSRA KALLRTIDAN FGTLPWCRRY LDRLGEDKYM
     FALNHLVKQG IVQDYPPLVD VEGSYTAQFE HTILLHPHKK EVVSKGDDY
//

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