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Database: UniProt
Entry: A0A124IFE8_9ACTN
LinkDB: A0A124IFE8_9ACTN
Original site: A0A124IFE8_9ACTN 
ID   A0A124IFE8_9ACTN        Unreviewed;       431 AA.
AC   A0A124IFE8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   22-NOV-2017, entry version 10.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   ORFNames=AQJ91_09650 {ECO:0000313|EMBL:KUO21232.1};
OS   Streptomyces sp. RV15.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO21232.1, ECO:0000313|Proteomes:UP000053260};
RN   [1] {ECO:0000313|EMBL:KUO21232.1, ECO:0000313|Proteomes:UP000053260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RV15 {ECO:0000313|EMBL:KUO21232.1,
RC   ECO:0000313|Proteomes:UP000053260};
RA   Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA   Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. RV15, isolated from a
RT   marine sponge.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KUO21232.1}.
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DR   EMBL; LMXB01000025; KUO21232.1; -; Genomic_DNA.
DR   RefSeq; WP_067018465.1; NZ_KQ949078.1.
DR   EnsemblBacteria; KUO21232; KUO21232; AQJ91_09650.
DR   Proteomes; UP000053260; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KUO21232.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053260};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053260};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        87     87       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       158    158       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       407    407       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   431 AA;  45867 MW;  F7E2914D4468055C CRC64;
     MSEPTRFGGR GHTDDLMSFL SASPTPYHAV ANTAERLEKA GFRQVAETDA WDGSTGGKYV
     LRGGAIVAWY VPEGAEPHTP FRIVGAHTDS PNLRVKPRPD SGAHGWRQVA VEIYGGPLLN
     SWLDRDLGLA GRLSLRDGSS RLVNIDRPLL RVPQLAIHLD RSVSAEGLKL DKQRHLQPIW
     GLGDNIRDGD LIAFLEESAG IAAGQVTGWD LMVHSVEPPA YLGRDEELVA GPRMDNLLSV
     HAGMAALVAV SGGDLPFIPV LAAFDHEENG SQSDTGADGP LLGSVLERSV FARGGSYEDR
     ARAFAGTVCL SSDTGHAVHP NYAERHDPTH HPRVNGGPIL KVNVNNRYAT DGSGRAVFAA
     ACEKAGVPFQ SFVSNNSMPC GTTIGPITAA RHGIRTVDIG VAILSMHSAR ELCGADDPQL
     LARSLAAFLE G
//
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