(data stored in ACNUC7421 zone)

HOGENOM: ACIAC_1_PE3046

ID   ACIAC_1_PE3046                       STANDARD;      PRT;   271 AA.
AC   ACIAC_1_PE3046; A1TRS6;
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; (ACIAC_1.PE3046).
GN   OrderedLocusNames=Aave_3100;
OS   ACIDOVORAX CITRULLI AAC00-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAC_1.PE3046.
CC       Acidovorax avenae subsp. citrulli AAC00-1, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A1TRS6_ACIAC
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; A1TRS6; -.
DR   EMBL; CP000512; ABM33664.1; -; Genomic_DNA.
DR   RefSeq; YP_971438.1; NC_008752.1.
DR   ProteinModelPortal; A1TRS6; -.
DR   SMR; A1TRS6; 2-257.
DR   STRING; A1TRS6; -.
DR   MEROPS; M24.001; -.
DR   GeneID; 4667289; -.
DR   GenomeReviews; CP000512_GR; Aave_3100.
DR   KEGG; aav:Aave_3100; -.
DR   NMPDR; fig|397945.5.peg.2640; -.
DR   eggNOG; COG0024; -.
DR   OMA; TTNSLND; -.
DR   PhylomeDB; A1TRS6; -.
DR   ProtClustDB; CLSK963251; -.
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; ACIAC_1.PE3046; -.
KW   methionine aminopeptidase, type I;
KW   Aminopeptidase; Cobalt; Complete proteome; Hydrolase; Metal-binding;
KW   Protease.
SQ   SEQUENCE   271 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSITIKSAEE IAGMREACRL ASEVLDYITP HIRPGITTND VDRLAAECMA AQGTISATIG
     YQPPGYPPYP KSLCTSLNHV VCHGIPNDKP LKKGDIMNVD VTVITKDGWY GDNSRMYLIG
     DVSIAAKRLC QLTFEAMWLG ILQVKPGARL GDIGHAIQKF AEGHGLSVVR EFCGHGIGKK
     FHEEPQVLHY GRPGTLEELV PGMTFTIEPM LNAGRREVKE HGNDGWTIVT KDHSLSAQWE
     HTVLVTETGY EVLTLSAGSP PLPPFVTAVK T
//

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