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Database: UniProt
Entry: A0A0N1H0H3_9ACTN
LinkDB: A0A0N1H0H3_9ACTN
Original site: A0A0N1H0H3_9ACTN 
ID   A0A0N1H0H3_9ACTN        Unreviewed;       441 AA.
AC   A0A0N1H0H3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 8.
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=OV450_1503 {ECO:0000313|EMBL:KPI32962.1};
OS   Actinobacteria bacterium OV450.
OC   Bacteria; Actinobacteria.
OX   NCBI_TaxID=1592328 {ECO:0000313|EMBL:KPI32962.1, ECO:0000313|Proteomes:UP000037826};
RN   [1] {ECO:0000313|EMBL:KPI32962.1, ECO:0000313|Proteomes:UP000037826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV450 {ECO:0000313|EMBL:KPI32962.1,
RC   ECO:0000313|Proteomes:UP000037826};
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:KPI32962.1}.
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DR   EMBL; LJCW01000043; KPI32962.1; -; Genomic_DNA.
DR   EnsemblBacteria; KPI32962; KPI32962; OV450_1503.
DR   PATRIC; fig|1592328.3.peg.1263; -.
DR   Proteomes; UP000037826; 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:KPI32962.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037826};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KPI32962.1};
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:UP000037826};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        97     97       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       168    168       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       417    417       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   441 AA;  47293 MW;  2BA97842FE1B31BC CRC64;
     MANTTVVKVN HMSSPARFDR GHTDDLMTFL TASPSPYHAV ANAAERLEKA GFRQLSETDA
     WDSGSGGRFV LRGGALIAWF VPEGASAHTP FRIVGAHTDS PNLRVKPLPD TGSQGWRQIA
     VEIYGGTLLN TWLDRDLGLA GRLSLRDGTE RLVNVDRALL RVPQLAVHLD RSVNSDGLKL
     DKQRHMQPIW GLGEVQEGDL IAFLEEEEGL PQGSVAGWDL MVHSIEPPSY LGRDRELVAG
     PRMDNLISVH AGVAALVAAS TADKLNNIPV LAAFDHEENG SQSDTGADGP LLGNVLERSV
     FSRGGTYEDR ARALAGSICV SSDTGHAVHP NYAERHDPTH HPRPNGGPIL KVNVNQRYAT
     DGSGRAVFAA ACERAGVPWQ TFVSNNSMPC GTTIGPITAA RHGIQTVDIG VAILSMHSAR
     ELCGAQDPYL LANALVAFLE D
//
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