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Database: UniProt
Entry: A0A0C1Y4V2_9ACTN
LinkDB: A0A0C1Y4V2_9ACTN
Original site: A0A0C1Y4V2_9ACTN 
ID   A0A0C1Y4V2_9ACTN        Unreviewed;       441 AA.
AC   A0A0C1Y4V2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   28-MAR-2018, entry version 19.
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=QR77_20255 {ECO:0000313|EMBL:KIF75607.1};
OS   Streptomyces sp. 150FB.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF75607.1, ECO:0000313|Proteomes:UP000031584};
RN   [1] {ECO:0000313|EMBL:KIF75607.1, ECO:0000313|Proteomes:UP000031584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=150FB {ECO:0000313|EMBL:KIF75607.1,
RC   ECO:0000313|Proteomes:UP000031584};
RA   Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT   "Genome sequence of the mycoparasite antagonist Streptomyces sp.
RT   strain FB 150.";
RL   Submitted (NOV-2014) 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:KIF75607.1}.
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DR   EMBL; JTHL01000001; KIF75607.1; -; Genomic_DNA.
DR   RefSeq; WP_040023448.1; NZ_JTHL01000001.1.
DR   EnsemblBacteria; KIF75607; KIF75607; QR77_20255.
DR   Proteomes; UP000031584; 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   Gene3D; 2.30.250.10; -; 1.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KIF75607.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031584};
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:UP000031584};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        86     86       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       157    157       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       417    417       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   441 AA;  46923 MW;  17D53AAC25ED3FC7 CRC64;
     MSTSARFDRG HTDDLMSFLM ASPTAYHAVD NAAQRLRDAG FTHVREVDAW DGTTGGKYVL
     RGGAIIAWYV PEGAEPHTPF RIAGAHTDSP NLRVKPLPDT GAHGWRQIAV ELYGGTLRNT
     WLDRDLGLAG RLTLRDGSHR LVNIDRPLLR VPQLAPHLDR SVNTDGLLLD AQRHMQPIWG
     LGRAEEGDLI RFVAEEIGVE AGEVIGWDLM AHPLEPAAYL GRDRELVAGP RMDDLLSVHA
     STAALVAVAT ADAGRGAGEA AGQALPYIPV LAAFDHEEAG SQSDTGADGP LLGTVLERSV
     LSRGGTREDH ARALAGTICL SSDTGHAVNP NYAERHDPTH HPRPNGGPIL KVNVNMRYAT
     DGAGSAAFTV ACEKAGVPWQ NFVSNNAVPC GTTIGPITAA RHGIKTVDIG VPILSMHSAR
     ELCGADDPYL LANALVAFLE G
//
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