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Database: UniProt
Entry: A0A1M5QIH3_9EURY
LinkDB: A0A1M5QIH3_9EURY
Original site: A0A1M5QIH3_9EURY 
ID   A0A1M5QIH3_9EURY        Unreviewed;       362 AA.
AC   A0A1M5QIH3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:SHH13892.1};
GN   ORFNames=SAMN05443636_1921 {ECO:0000313|EMBL:SHH13892.1};
OS   Halobaculum gomorrense.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halobaculum.
OX   NCBI_TaxID=43928 {ECO:0000313|EMBL:SHH13892.1, ECO:0000313|Proteomes:UP000184357};
RN   [1] {ECO:0000313|EMBL:SHH13892.1, ECO:0000313|Proteomes:UP000184357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9297 {ECO:0000313|EMBL:SHH13892.1,
RC   ECO:0000313|Proteomes:UP000184357};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FQWV01000004; SHH13892.1; -; Genomic_DNA.
DR   RefSeq; WP_073308925.1; NZ_FQWV01000004.1.
DR   AlphaFoldDB; A0A1M5QIH3; -.
DR   STRING; 43928.SAMN05443636_1921; -.
DR   OrthoDB; 145069at2157; -.
DR   Proteomes; UP000184357; Unassembled WGS sequence.
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:SHH13892.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184357}.
SQ   SEQUENCE   362 AA;  40246 MW;  16C801E9FDBD05FB CRC64;
     MDPRIREHAE TIVDHSIELE AGDDLVIQLP AEAEDLAVAL HEYAGDIGAN PVYLNNSQRA
     ARAYLRARED DFELPEHELA LYEAADAFVI ARSGGNVSEK ADVDPETTAD YNRARRPVQT
     ERLSKTWCLT QFPTSGHAQL AGMSTEEYEN FVYDAVSIDW EAQAKFQQQM VELIDDAEEV
     RIKSGEETDL TMSVAGNTAL NDDGKANLPG GEVFTAPVKD SVNGEVYFDL PLYRQGREIE
     GVRLTFEDGR VEEFSAERNE EVLEGVFNTD ENARYLGELG IGMNRAIDRF TYNMLFDEKM
     GDTVHMAVGS AYPETVGEGN EVNESAEHVD MIVDMSEDSV IELDGEVVQR DGTFTFEDGE
     GE
//
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