(data stored in ACNUC7421 zone)

HOGENOM: ACIBL_1_PE1245

ID   ACIBL_1_PE1245                       STANDARD;      PRT;   250 AA.
AC   ACIBL_1_PE1245; Q1ISA0;
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; (ACIBL_1.PE1245).
GN   OrderedLocusNames=Acid345_1248;
OS   CANDIDATUS KORIBACTER VERSATILIS ELLIN345.
OC   Bacteria; Acidobacteria; Candidatus Koribacter.
OX   NCBI_TaxID=204669;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIBL_1.PE1245.
CC       Candidatus Koribacter versatilis Ellin345, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q1ISA0_ACIBL
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: HOG000030426 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q1ISA0; -.
DR   EMBL; CP000360; ABF40250.1; -; Genomic_DNA.
DR   RefSeq; YP_590324.1; NC_008009.1.
DR   ProteinModelPortal; Q1ISA0; -.
DR   STRING; Q1ISA0; -.
DR   MEROPS; M24.001; -.
DR   GeneID; 4069823; -.
DR   GenomeReviews; CP000360_GR; Acid345_1248.
DR   KEGG; aba:Acid345_1248; -.
DR   NMPDR; fig|204669.6.peg.1234; -.
DR   eggNOG; COG0024; -.
DR   OMA; TTDGTWS; -.
DR   PhylomeDB; Q1ISA0; -.
DR   ProtClustDB; CLSK774482; -.
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; ACIBL_1.PE1245; -.
KW   methionine aminopeptidase, type I;
KW   Aminopeptidase; Cobalt; Complete proteome; Hydrolase; Metal-binding;
KW   Protease; Reference proteome.
SQ   SEQUENCE   250 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAIICKSGAE IEKMRRSGRI VRQVLETVRA LVAPGVSTMD LERAAEKKIR ELGAKPAFKG
     YYDYPCVLCT SVNDEIVHGI PSEKRVLKTG DIVSIDTGVV LDGYYGDSAI TVPVGEAITS
     ELQKLLTITE QSLYKAIDAV KVGNTLGDIG SAVQQHVEAA GFSVVREFVG HGIGTRLHED
     PQVPNFGAAG AGSRLREGMV LAIEPMVNVG KPATRTLDDH WTAVTADGSF SAHFEHCVAV
     TRDGPVILTE
//

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