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

 MAP2_DEBHA              Reviewed;         419 AA.
Q6BVB8;
03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 2.
10-OCT-2018, entry version 91.
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};
OrderedLocusNames=DEHA2C03894g;
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
NCBI_TaxID=284592;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- 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; CR382135; CAG85896.2; -; Genomic_DNA.
RefSeq; XP_457851.2; XM_457851.1.
ProteinModelPortal; Q6BVB8; -.
SMR; Q6BVB8; -.
MEROPS; M24.002; -.
PRIDE; Q6BVB8; -.
EnsemblFungi; CAG85896; CAG85896; DEHA2C03894g.
GeneID; 2900504; -.
KEGG; dha:DEHA2C03894g; -.
HOGENOM; HOG000226278; -.
InParanoid; Q6BVB8; -.
KO; K01265; -.
OMA; TINKHFG; -.
OrthoDB; EOG092C3NQP; -.
Proteomes; UP000000599; Chromosome C.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
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; Reference proteome.
CHAIN 1 419 Methionine aminopeptidase 2.
/FTId=PRO_0000407651.
COMPBIAS 48 60 Lys-rich.
METAL 192 192 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 203 203 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 203 203 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 272 272 Divalent metal cation 2; catalytic; via
tele nitrogen. {ECO:0000255|HAMAP-
Rule:MF_03175}.
METAL 305 305 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 400 400 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 400 400 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
BINDING 172 172 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03175}.
BINDING 280 280 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03175}.
SEQUENCE 419 AA; 46948 MW; FF3366D553F7D758 CRC64;
MSTNSSNPNE VMEKVQDLKI DDSKPKVDSE EQPEAESDGE SATDGAQKKK KKKKSKKKKK
ITAIDNSYPD GVFPEGEWQE YPLDVNSYRT TSEEKRYLDR QQNNHWQDFR KGAEIHRRVR
HKAQSSIRPG MNMTEIADLI ENSVRSYANN DHTLKAGIGF PTGLSLNHVA AHYTPNAGDK
TVLNYEDVMK VDIGVHVNGH IVDSAFTLTF DDKYDSLLKA VKEATNTGVK EAGIDVRLND
IGEAIQEVME SYEMELNGKT YPIKCIRNLN GHNIGDYLIH SGKTVPIVPN GDMTKMEEGE
TFAIETFGST GNGYVLPQGE CSHYAKNPGT DDIVVPGDKA KSLLNVINEN FGTLPWCRRY
LDRLGQDKYL LALNQLVRAG IVQDYPPIVD IKGSYTAQFE HTILLHPHKK EVVSRGDDY


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