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Database: UniProt
Entry: A0A177HW50_9ACTN
LinkDB: A0A177HW50_9ACTN
Original site: A0A177HW50_9ACTN 
ID   A0A177HW50_9ACTN        Unreviewed;       434 AA.
AC   A0A177HW50;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   25-OCT-2017, entry version 9.
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   ECO:0000313|EMBL:OAH14910.1};
GN   ORFNames=STSP_17470 {ECO:0000313|EMBL:OAH14910.1};
OS   Streptomyces jeddahensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH14910.1, ECO:0000313|Proteomes:UP000077381};
RN   [1] {ECO:0000313|EMBL:OAH14910.1, ECO:0000313|Proteomes:UP000077381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA   Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J.,
RA   Madkour M.H., Al-Ansari A.M., Almakishah N.H., Steinbuechel A.,
RA   Daniel R.;
RT   "Genome sequence of Streptomyces sp. G25.";
RL   Submitted (DEC-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:OAH14910.1}.
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DR   EMBL; LOHS01000053; OAH14910.1; -; Genomic_DNA.
DR   RefSeq; WP_067274229.1; NZ_LOHS01000053.1.
DR   EnsemblBacteria; OAH14910; OAH14910; STSP_17470.
DR   PATRIC; fig|1716141.3.peg.1831; -.
DR   Proteomes; UP000077381; 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   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:OAH14910.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077381};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:OAH14910.1};
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:UP000077381};
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       410    410       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   434 AA;  46189 MW;  AE89FD4A78A994E0 CRC64;
     MTSPARFDRG HTDDLMSFLA ASPSPYHAVA SAAERLEKAG FRQVAEMDAW EGSTGGKYVL
     RGGAIVAWYV PEEAAPHTPF RIIGAHTDSP NLRVKPLPDT GAHGWRQIAV EIYGGPLLNS
     WLDRDLGIAG RLSLRDGSSM LVNVDRPLLR IPQLAIHLDR SVHTDGLKLD KQKHLQPIWG
     LGEPGEGGLI RFLEDENGIE PGEVTGWDLM VHSIERPSYL GRDRELMAGP RLDNLLSVHA
     GTAALAAVAG SAVSGADLPY IPVLAAFDHE ENGSQSDTGA DGPLLGSVLE RSVFARGGSY
     EDRARAFAGT VCLSSDTGHA VHPNYAERHD PTHHPRANGG PILKVNVNNR YATDGSGRAV
     FAAACERAGV PLQSFVSNNS MPCGTTIGPI TAARHGIKTV DIGVAILSMH SARELCGADD
     PFLLANALVA FLEG
//
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