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MAP2_KOMPG
ID   MAP2_KOMPG              Reviewed;         448 AA.
AC   C4R2P3;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Methionine aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE            Short=MAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE            Short=MetAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE            EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03175};
DE   AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_03175};
GN   Name=MAP2 {ECO:0000255|HAMAP-Rule:MF_03175};
GN   OrderedLocusNames=PAS_chr2-2_0159;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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:0000255|HAMAP-
CC       Rule:MF_03175}.
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:0000255|HAMAP-Rule:MF_03175};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
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:0000255|HAMAP-Rule:MF_03175};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175}.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase eukaryotic type 2 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03175}.
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DR   EMBL; FN392320; CAY69767.1; -; Genomic_DNA.
DR   RefSeq; XP_002492047.1; XM_002492002.1.
DR   AlphaFoldDB; C4R2P3; -.
DR   SMR; C4R2P3; -.
DR   STRING; 644223.C4R2P3; -.
DR   EnsemblFungi; CAY69767; CAY69767; PAS_chr2-2_0159.
DR   GeneID; 8198269; -.
DR   KEGG; ppa:PAS_chr2-2_0159; -.
DR   eggNOG; KOG2775; Eukaryota.
DR   HOGENOM; CLU_015857_7_1_1; -.
DR   InParanoid; C4R2P3; -.
DR   OMA; NEIAAHY; -.
DR   Proteomes; UP000000314; Chromosome 2.
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:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Protease;
KW   Reference proteome.
FT   CHAIN           1..448
FT                   /note="Methionine aminopeptidase 2"
FT                   /id="PRO_0000407664"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT   BINDING         218
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT   BINDING         229
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT   BINDING         229
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT   BINDING         298
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT   BINDING         331
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT   BINDING         429
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT   BINDING         429
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
SQ   SEQUENCE   448 AA;  50204 MW;  6BCE8381B94A08F1 CRC64;
     MTSSVDKVSQ KVADVKLGSS KSTKNNKSKG KGKSNKNQVV EDDDEDDFEK ALELAMQLDA
     QKLAQKKADD VPLVEEEEKK VEEKIEQQYD PISTFYPDGN YPQGEVVDYK DDNLYRTTDE
     EKRALDREKN NKWNEFRKGA EIHRRVRKLA KDEIKPGMSM IEIAELIENA VRGYSGEDGL
     KGGMGFPCGL SLNHCAAHYS PNANDKLVLN YEDVMKVDFG VHVNGHIIDS AFTLTFDDKY
     DDLLKAVKDA TNTGIREAGI DVRLTDIGEA IQEVMESYEV TLDGETYQVK PIKNLCGHNI
     GQYRIHGGKS VPIVKNFDNT KMEEGETFAI ETFGSTGRGH VIGQGECSHY AKNPDAPANA
     ISSIRVNRAK QLLKTIDENF GTLPFCRRYI DRLGEEKYLL ALNQLVKSGV VSDYPPLVDV
     KGSYTAQYEH TILLRPNVKE VVSRGEDY
 
 
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