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Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Peptidase M)

 MAP2_CANDC              Reviewed;         452 AA.
B9WJA2;
03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 1.
28-FEB-2018, entry version 57.
RecName: Full=Methionine aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_03175};
Short=MAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
Short=MetAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03175};
AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_03175};
Name=MAP2 {ECO:0000255|HAMAP-Rule:MF_03175}; ORFNames=CD36_64570;
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF
3949 / NRRL Y-17841) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=573826;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
PubMed=19745113; DOI=10.1101/gr.097501.109;
Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D.,
Harris D., Aslett M., Barrell J.F., Butler G., Citiulo F.,
Coleman D.C., de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J.,
Munro C.A., Pain A., Poulter R.T., Rajandream M.A., Renauld H.,
Spiering M.J., Tivey A., Gow N.A.R., Barrell B., Sullivan D.J.,
Berriman M.;
"Comparative genomics of the fungal pathogens Candida dubliniensis and
Candida albicans.";
Genome Res. 19:2231-2244(2009).
-!- FUNCTION: Cotranslationally removes the N-terminal methionine from
nascent proteins. The N-terminal methionine is often cleaved when
the second residue in the primary sequence is small and uncharged
(Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). {ECO:0000255|HAMAP-
Rule:MF_03175}.
-!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
preferentially methionine, from peptides and arylamides.
{ECO:0000255|HAMAP-Rule:MF_03175}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Note=Binds 2 divalent metal cations per subunit. Has a high-
affinity and a low affinity metal-binding site. The true nature of
the physiological cofactor is under debate. The enzyme is active
with cobalt, zinc, manganese or divalent iron ions. Most likely,
methionine aminopeptidases function as mononuclear Fe(2+)-
metalloproteases under physiological conditions, and the
catalytically relevant metal-binding site has been assigned to the
histidine-containing high-affinity site. {ECO:0000255|HAMAP-
Rule:MF_03175};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175}.
-!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
aminopeptidase eukaryotic type 2 subfamily. {ECO:0000255|HAMAP-
Rule:MF_03175}.
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EMBL; FM992693; CAX41324.1; -; Genomic_DNA.
RefSeq; XP_002421164.1; XM_002421119.1.
ProteinModelPortal; B9WJA2; -.
SMR; B9WJA2; -.
STRING; 573826.XP_002421164.1; -.
MEROPS; M24.002; -.
EnsemblFungi; CAX41324; CAX41324; CD36_64570.
GeneID; 8048936; -.
KEGG; cdu:CD36_64570; -.
CGD; CAL0000171001; Cd36_64570.
eggNOG; KOG2775; Eukaryota.
eggNOG; COG0024; LUCA.
HOGENOM; HOG000226278; -.
KO; K01265; -.
OrthoDB; EOG092C3NQP; -.
Proteomes; UP000002605; Chromosome 6.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
GO; GO:0035551; P:protein initiator methionine removal involved in protein maturation; IEA:EnsemblFungi.
CDD; cd01088; MetAP2; 1.
Gene3D; 1.10.10.10; -; 1.
HAMAP; MF_03175; MetAP_2_euk; 1.
InterPro; IPR036005; Creatinase/aminopeptidase-like.
InterPro; IPR000994; Pept_M24.
InterPro; IPR001714; Pept_M24_MAP.
InterPro; IPR002468; Pept_M24A_MAP2.
InterPro; IPR018349; Pept_M24A_MAP2_BS.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00557; Peptidase_M24; 1.
PRINTS; PR00599; MAPEPTIDASE.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF55920; SSF55920; 2.
TIGRFAMs; TIGR00501; met_pdase_II; 1.
PROSITE; PS01202; MAP_2; 1.
3: Inferred from homology;
Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase;
Metal-binding; Protease.
CHAIN 1 452 Methionine aminopeptidase 2.
/FTId=PRO_0000407647.
COMPBIAS 74 90 Lys-rich.
METAL 223 223 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 234 234 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 234 234 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 305 305 Divalent metal cation 2; catalytic; via
tele nitrogen. {ECO:0000255|HAMAP-
Rule:MF_03175}.
METAL 338 338 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 433 433 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 433 433 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
BINDING 203 203 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03175}.
BINDING 313 313 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03175}.
SEQUENCE 452 AA; 51409 MW; E9BA5A87E7D7FAF9 CRC64;
MTGVTGTEDT KVIESKINEL NIDKSKPEKT NKVNKSDDVD NDDVDNDDND DEDNDDDDDE
ITESGNSASS SGDKKKKKNK NKNKKKKKKK IISIDSSYPE GIFPEGQWME YPLEDINSYR
ITSEEKRYLD RQQNNKWQDF RKGAEIHRRV RHKAQSSIKP GMTMIEIANL IEDSIRNYSN
NDHTLKSGIG FPTGLSLNHV AAHYTPNTGD KLILKKDDIM KVDIGIHVNG RICDSAFTMT
FNDEGKYDNI MKAVKEATYT GIKESGIDVR LNDIGAAIQE VMESYEMEEN GKIYPIKCIK
NLNGHNIDDF IIHSGKSVPI IANGDMTKME EGEIFAIETF GSTGNGYVLP EGECSHYAMN
KNIQHLKPPS ERSKQLLESI KQNFGTLPWC RRYLERTGEE KYLFALNQLV RHGIIEEYPP
IVDKRGSYTA QYEHTILLHP HKKEVVTKGD DY


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