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Database: UniProt
Entry: A0A0N1FPH7_9ACTN
LinkDB: A0A0N1FPH7_9ACTN
Original site: A0A0N1FPH7_9ACTN 
ID   A0A0N1FPH7_9ACTN        Unreviewed;       430 AA.
AC   A0A0N1FPH7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, 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=OK006_7578 {ECO:0000313|EMBL:KPI02613.1};
OS   Actinobacteria bacterium OK006.
OC   Bacteria; Actinobacteria.
OX   NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI02613.1, ECO:0000313|Proteomes:UP000037912};
RN   [1] {ECO:0000313|EMBL:KPI02613.1, ECO:0000313|Proteomes:UP000037912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK006 {ECO:0000313|EMBL:KPI02613.1,
RC   ECO:0000313|Proteomes:UP000037912};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four Actinobacteria strains OK006 OK074
RT   OV450 and OV320.";
RL   Submitted (SEP-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:KPI02613.1}.
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DR   EMBL; LJCU01000250; KPI02613.1; -; Genomic_DNA.
DR   RefSeq; WP_054235549.1; NZ_LJCU01000250.1.
DR   EnsemblBacteria; KPI02613; KPI02613; OK006_7578.
DR   PATRIC; fig|1592326.3.peg.9471; -.
DR   Proteomes; UP000037912; 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:KPI02613.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037912};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KPI02613.1};
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:UP000037912};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        85     85       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       156    156       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       405    405       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   430 AA;  45461 MW;  D42595A91C131C75 CRC64;
     MSPTHDRSHS DDLLSFIRSS PSPYHVVANA AQRLEKAGFQ ELRETDDWTA GAEGGRYVVR
     AGALLAWYVP AGAPARTPFR IVGAHTDSPN LRIKPEPDTG SAGWRQIAVE IYGGVPHNTW
     LDRDLGISGR LTLRDGSSRL VCLDQPLLRV PQLAIHLDRG VNEGVVLDAQ LHMTPLWGLG
     PTRPGALLAR VAAEADTDVA EVLGWDLMLH DIQPPGYLGA DEEFLVSPRL DNQISVHAGV
     TALVSAATAA RPPAHIPVLA AFDHEEVGSG SQSGAQGPLL ERVLGRSVAA RGGSAEDFNR
     ALAGAFCVSA DMSHAVHPNY AERHDPDHHP LPNGGPVVKV NVNQRYATDG TGVAAFAAAC
     ERAEVPWQPF VSHNAMPCGT SIGPITAARL GVATVDVGVP GLSMHSAREL CGAQDPGLLA
     RVLTEFVTTG
//
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