ID F8D579_HALXS Unreviewed; 365 AA.
AC F8D579;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Peptidase M29 aminopeptidase II {ECO:0000313|EMBL:AEH36436.1};
GN OrderedLocusNames=Halxa_1808 {ECO:0000313|EMBL:AEH36436.1};
OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halopiger.
OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH36436.1, ECO:0000313|Proteomes:UP000006794};
RN [1] {ECO:0000313|EMBL:AEH36436.1, ECO:0000313|Proteomes:UP000006794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18323 / JCM 14033 / SH-6
RC {ECO:0000313|Proteomes:UP000006794};
RX PubMed=22675596; DOI=10.4056/sigs.2505605;
RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL Stand. Genomic Sci. 6:31-42(2012).
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; CP002839; AEH36436.1; -; Genomic_DNA.
DR RefSeq; WP_013879329.1; NC_015666.1.
DR AlphaFoldDB; F8D579; -.
DR STRING; 797210.Halxa_1808; -.
DR GeneID; 10796773; -.
DR KEGG; hxa:Halxa_1808; -.
DR eggNOG; arCOG01889; Archaea.
DR HOGENOM; CLU_057697_0_0_2; -.
DR OrthoDB; 145069at2157; -.
DR Proteomes; UP000006794; Chromosome.
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:AEH36436.1}; 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:UP000006794}.
SQ SEQUENCE 365 AA; 40177 MW; 630E76CE24868C6E CRC64;
MDERVREHAD VLVDWSARVE AGDDVVLSVG PDAHELAVAV AEKLGERGAN LLATYGSGEI
TRAYLRAHDG DFDENPAHER ALFENADVYL SLGGGRNTSA TADVPGDTRR AYSNARTEIR
EARFDARWVS TVHPTRSLAQ QANMAYEEYQ DFAYDAILRD WESLADEMAN MKDLLDAGSE
VRLVSDGTDL TMAIDDRTAV NSAASVAYDS HNLPSGEVFT APYATEGEVT FDVPMTLRGE
AVRNVRLEFD DGEVVDYGAE QGEEVISEIL ETDDGARRLG ELGIGMNRGI DQYTDNILFD
EKMGETVHLA LGRAYDACLP EGESGNESAV HVDMITDMSE DSRIEIDGDV VQRNGQFRWE
DGFEE
//
