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Database: UniProt
Entry: U1PF01_9EURY
LinkDB: U1PF01_9EURY
Original site: U1PF01_9EURY 
ID   U1PF01_9EURY            Unreviewed;       357 AA.
AC   U1PF01;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Leucyl aminopeptidase (Aminopeptidase T) {ECO:0000313|EMBL:ERH08926.1};
GN   ORFNames=J07HX64_00678 {ECO:0000313|EMBL:ERH08926.1};
OS   halophilic archaeon J07HX64.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX   NCBI_TaxID=1085028 {ECO:0000313|EMBL:ERH08926.1};
RN   [1] {ECO:0000313|EMBL:ERH08926.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23637883;
RA   Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA   Allen E.E.;
RT   "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL   PLoS ONE 8:E61692-E61692(2013).
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M29 family.
CC       {ECO:0000256|ARBA:ARBA00008236}.
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DR   EMBL; KE356579; ERH08926.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1PF01; -.
DR   STRING; 1085028.J07HX64_00678; -.
DR   HOGENOM; CLU_057697_0_0_2; -.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR   InterPro; IPR035097; M29_N-terminal.
DR   InterPro; IPR000787; Peptidase_M29.
DR   PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR34448:SF1; BLL6088 PROTEIN; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:ERH08926.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
SQ   SEQUENCE   357 AA;  39614 MW;  6ACCAB99EB453FC7 CRC64;
     MDSRIQEHAE IIADHSVDLQ AGDNVIIRAP PAAEDLVVAL HEVLGERGAN PLTMSTNARF
     SRAYLRAADE FETPEHHLAL VEETDVYIAI RADANVTETS DVDPKTSAAQ AQAHQPILGE
     RLSKRWCLSQ FPAPANAQLA EMSTEAYAEF VYDAVIKDWD AVREHQAQMV EILDPAEEVR
     IVSGDTTDVR MRVGGNPTLN DYGEKNLPGG EVFTAPIVDS VEGEVLFDKP LYHQGREVTG
     VFLRFEDGAV VEHSAEKNED VLTEVLDTDA GARYLGELGI GMNRDIDRFT YNMLFDEKMG
     DTVHMAVGRA YEDTVGEANE RNESAVHVDM IVDMSEDSFI EVDGERVQED GRFIFEE
//
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