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MAP22_LEPMJ
ID   MAP22_LEPMJ             Reviewed;         451 AA.
AC   E5R4J3;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Methionine aminopeptidase 2-2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE            Short=MAP 2-2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE            Short=MetAP 2-2 {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   ORFNames=Lema_P046670;
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Leptosphaeria; Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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; FP929083; CBX91961.1; -; Genomic_DNA.
DR   RefSeq; XP_003835326.1; XM_003835278.1.
DR   AlphaFoldDB; E5R4J3; -.
DR   SMR; E5R4J3; -.
DR   STRING; 985895.E5R4J3; -.
DR   EnsemblFungi; CBX91961; CBX91961; LEMA_P046670.1.
DR   GeneID; 13284777; -.
DR   eggNOG; KOG2775; Eukaryota.
DR   HOGENOM; CLU_015857_7_1_1; -.
DR   InParanoid; E5R4J3; -.
DR   OMA; NEIAAHY; -.
DR   OrthoDB; 601484at2759; -.
DR   Proteomes; UP000002668; Genome.
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..451
FT                   /note="Methionine aminopeptidase 2-2"
FT                   /id="PRO_0000407607"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..75
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT   BINDING         224
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         235
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         235
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         304
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         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT   BINDING         337
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         432
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         432
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   451 AA;  49158 MW;  08407BBF6A063CA3 CRC64;
     MAAQVEDDVA NLKLDDSTTK PTNGTSQPDS KLSAEAEDSD DDAEGDGNGT GEAGADGAAK
     KKKKRKPRKK KKAGTSATAG AKSQTSPPRV LISDLFPNDS YPEGEICEYR DENSYRTTNE
     EKRHLDRMNN DFLTDYRKGA EIHRQVRQWA ANWIKPGMTL TEIAEGIEDS VRALTGHQGL
     EEGDAQKAGM GFPTGLSINH CAAHYTPNAG NKVVVNYEDV MKVDFGVHIN GRIVDSAFTK
     TFDPVYDPLV EACKAATNAG IKEAGIDVRM SDIGAAIQEV MESYEVEIGG KMLPVKCIRN
     LNGHSIGHYT IHGGKTVPIV KGSDQTKMEE GETFAIETFG STGKGYVRDD METSHYALRP
     DAPKVALRIS SAKSLLASIT KNFGTLPFCR RYLDRLGHDK YLLGLNNLVS SGIVEAYPPL
     CDIKGSWTAQ SEHTFVLRPT CKEVLSRGDD Y
 
 
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