(data stored in ACNUC1829 zone)

HOGENOM: TETNG19_PE64

ID   TETNG19_PE64                         STANDARD;      PRT;   239 AA.
AC   TETNG19_PE64; Q4S5B0;
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;Flags: Fragment;
DE   (TETNG19.PE64).
GN   ORFNames=GSTENG00023810001;
OS   TETRAODON NIGROVIRIDIS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Actinopterygii; Actinopteri; Neopterygii; Teleostei; Elopocephala;
OC   Clupeocephala; Euteleostei; Neognathi; Neoteleostei; Eurypterygii;
OC   Ctenosquamata; Acanthomorpha; Euacanthomorpha; Holacanthopterygii;
OC   Acanthopterygii; Euacanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetraodontoidei; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS TETNG19.PE64.
CC       Tetraodon nigroviridis chromosome 19 TETRAODON8  sequence 1..7272499
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:Q4S5B0_TETNG
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: HOG000230651 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Tetraodon_nigroviridis;ENSTNIG00000012670;ENSTNIT00000015851;ENSTNIP00000015644.
DR   EMBL_PREDICTED; CAAE01014731; - ;
DR   UniProtKB/Swiss-Prot; Q4S5B0; -.
DR   EMBL; CAAE01014731; CAG04172.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q4S5B0; -.
DR   NMPDR; fig|99883.3.peg.17905; -.
DR   eggNOG; fiNOG09110; -.
DR   PhylomeDB; Q4S5B0; -.
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; IPR002468; Pept_M24A_MAP2.
DR   InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:3.90.230.10; Peptidase_M24_cat_core; 2.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR10804:SF9; Pept_M24A_MAP2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; Peptidase_M24_cat_core; 1.
DR   TIGRFAMs; TIGR00501; Met_pdase_II; 1.
DR   PROSITE; PS01202; MAP_2; 1.
DR   HOGENOMDNA; TETNG19.PE64; -.
KW   ENSTNIG00000012670820036002503210000011;
KW   ENSTNIP00000015644A2003600250321000001-PAA;
KW   Aminopeptidase; Cobalt; Complete proteome; Hydrolase; Metal-binding;
KW   Protease; Reference proteome.
SQ   SEQUENCE   239 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MARGCICCIK YMLFLFNLFF WLGGCGLLGV GLWLSVSQGS FATLSPSFPS LSAANLIITL
     GSIVMVTGFL GCLGAIKENK CLLLSFFIVL LIILLAELIL LILFFVYTDK VSENARRDLK
     EGLALYTTDN NAGLKDAWNT IQAEWRCCGV TGHRDWYAAL HDNLVPDSCC QLPFQGCGRN
     SSNTFWTRGC YEKVEAWLDE NKHLLGTIAM CVLVIQLLGM AFSMTLYQQI HRTGKKYEA
//

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