(data stored in ACNUC7421 zone)

HOGENOM: SACEN_1_PE1006

ID   SACEN_1_PE1006                       STANDARD;      PRT;   503 AA.
AC   SACEN_1_PE1006; A4F8I7;
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   SubName: Full=Leucine aminopeptidase; EC=3.4.11 1; (SACEN_1.PE1006).
GN   Name=pepA; OrderedLocusNames=SACE_1030;
OS   SACCHAROPOLYSPORA ERYTHRAEA NRRL 2338.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Pseudonocardineae; Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SACEN_1.PE1006.
CC       Saccharopolyspora erythraea NRRL 2338 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:A4F8I7_SACEN
CC   -!- FUNCTION: Presumably involved in the processing and regular
CC       turnover of intracellular proteins. Catalyzes the removal of
CC       unsubstituted N-terminal amino acids from various peptides (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-
CC       Yaa-, in which Xaa is preferably Leu, but may be other amino acids
CC       including Pro although not Arg or Lys, and Yaa may be Pro. Amino
CC       acid amides and methyl esters are also readily hydrolyzed, but
CC       rates on arylamides are exceedingly low.
CC   -!- GENE_FAMILY: HOG000243129 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A4F8I7; -.
DR   EMBL; AM420293; CAM00362.1; -; Genomic_DNA.
DR   RefSeq; YP_001103287.1; NC_009142.1.
DR   ProteinModelPortal; A4F8I7; -.
DR   STRING; A4F8I7; -.
DR   GeneID; 4940886; -.
DR   GenomeReviews; AM420293_GR; SACE_1030.
DR   KEGG; sen:SACE_1030; -.
DR   eggNOG; COG0260; -.
DR   OMA; VVRHYGG; -.
DR   ProtClustDB; CLSK2535996; -.
DR   BioCyc; SERY405948:SACE_1030-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR011356; Peptidase_M17.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR008283; Peptidase_M17_N.
DR   PANTHER; PTHR11963:SF3; Peptidase_M17; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF02789; Peptidase_M17_N; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
DR   HOGENOMDNA; SACEN_1.PE1006; -.
KW   leucine aminopeptidase;
KW   Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Manganese;
KW   Metal-binding; Protease.
SQ   SEQUENCE   503 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MIPTSLVEVD VVRRPRDGVP TAVPLPDGES GPELAPVAEA FEVDIALLEA IGVKSAAGDV
     RTVPLPEGRF GWVVGIGSGE AAQWRTAGAA LARATREKLG ETGEAEGDTV DFGEPSEAEY
     LQIRLPAGIG QDAVSALALG LALGDYRFRV TGQPAPPRLR KALLVTDDEE LREPVARARE
     WAAATALARD LANSPSNVKD PDWFTGLAAR LAGEVDGLTA TVRDEKWLAD HGFGGILAVG
     GGSASPPRLL ELAWRPADAT GPHLVLVGKG ITFDTGGISL KPAEGMHLMR TDMSGGAAVI
     GAMLAVARLG LRVRVTALVP SAENHLSGSS YRPGDVVRHY GGKTTEVGNT DAEGRMVMAD
     ALVYGVRHHE ADLLVDVATL TGAMKVALGL RTGGVFATDP DLSRRLRDAG DRVGEAWWPM
     PLIEDHTEAV RGELADVNQT PPGPGGVTAA LFLREFTEGL PWAHLDIAGP ARADKNYAEV
     VAGGTGFAAR SLVEFVASLA EQG
//

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