(data stored in ACNUC7421 zone)

HOGENOM: ACIAD_1_PE2074

ID   ACIAD_1_PE2074                       STANDARD;      PRT;   254 AA.
AC   ACIAD_1_PE2074; Q6FA52;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Methionine aminopeptidase; EC=3.4.11 18; (ACIAD_1.PE2074).
GN   Name=map; OrderedLocusNames=ACIAD2271;
OS   ACINETOBACTER SP. ADP1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAD_1.PE2074.
CC       Acinetobacter sp. ADP1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q6FA52_ACIAD
CC   -!- FUNCTION: Removes the N-terminal methionine from nascent proteins
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC       preferentially methionine, from peptides and arylamides.
CC   -!- COFACTOR: Binds 2 cobalt ions per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M24A family.
CC   -!- GENE_FAMILY: HOG000030427 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6FA52; -.
DR   EMBL; CR543861; CAG69061.1; -; Genomic_DNA.
DR   RefSeq; YP_046883.1; NC_005966.1.
DR   ProteinModelPortal; Q6FA52; -.
DR   STRING; Q6FA52; -.
DR   MEROPS; M24.001; -.
DR   GeneID; 2877828; -.
DR   GenomeReviews; CR543861_GR; ACIAD2271.
DR   KEGG; aci:ACIAD2271; -.
DR   NMPDR; fig|62977.3.peg.2170; -.
DR   eggNOG; COG0024; -.
DR   OMA; KKEVRLM; -.
DR   PhylomeDB; Q6FA52; -.
DR   ProtClustDB; CLSK707502; -.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0009987; P:cellular process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR000994; Pept_M24_structural-domain.
DR   InterPro; IPR002467; Pept_M24A_MAP1.
DR   Gene3D; G3DSA:3.90.230.10; Peptidase_M24_cat_core; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; Peptidase_M24_cat_core; 1.
DR   TIGRFAMs; TIGR00500; Met_pdase_I; 1.
DR   PROSITE; PS00680; MAP_1; 1.
DR   HOGENOMDNA; ACIAD_1.PE2074; -.
KW   Aminopeptidase; Cobalt; Complete proteome; Hydrolase; Metal-binding;
KW   Protease.
SQ   SEQUENCE   254 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRIAGRLAAE VLDMIKPHIQ LGVSTLELDR ICHDHIVNAQ QAIPACLGYG AAPGRPAFQH
     TICTSVNHVV CHGIPSSEKI LKKGDILNID VTVIKDGYHG DTNMMYVVGG ETSILANRLC
     NVAQEAMYRG METVRAGSFI GDIGYAIQKY VESERFSVVR EYCGHGIGTV FHDEPQVLHY
     GQKGTGMQLE AGMTFTIEPM VNAGVWQTKL LGDKWTVVTK DHKLSAQFEH TILVTETGLE
     VLTARPEEDL SRFM
//

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