ID L9WJR0_9EURY Unreviewed; 399 AA.
AC L9WJR0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Peptidase M24 {ECO:0000313|EMBL:ELY49612.1};
GN ORFNames=C495_00245 {ECO:0000313|EMBL:ELY49612.1};
OS Natronorubrum sulfidifaciens JCM 14089.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1230460 {ECO:0000313|EMBL:ELY49612.1, ECO:0000313|Proteomes:UP000011661};
RN [1] {ECO:0000313|EMBL:ELY49612.1, ECO:0000313|Proteomes:UP000011661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14089 {ECO:0000313|EMBL:ELY49612.1,
RC ECO:0000313|Proteomes:UP000011661};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELY49612.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOHX01000001; ELY49612.1; -; Genomic_DNA.
DR RefSeq; WP_008158854.1; NZ_AOHX01000001.1.
DR AlphaFoldDB; L9WJR0; -.
DR STRING; 1230460.C495_00245; -.
DR PATRIC; fig|1230460.4.peg.52; -.
DR eggNOG; arCOG01000; Archaea.
DR OrthoDB; 1346at2157; -.
DR Proteomes; UP000011661; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01092; APP-like; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF3; AMINOPEPTIDASE YPDF; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Reference proteome {ECO:0000313|Proteomes:UP000011661}.
FT DOMAIN 8..156
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 166..378
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 399 AA; 43352 MW; F35A17A8B9145F92 CRC64;
MDAPFATRIR DCKRRLEDVD AALLICFPSP NLTYLTGFEE TPSERHLLLF VPRTGDPVFV
APAMYDQQLA SLPLDCRFWN DGDDPVELVD DVLEEILDQP RGERQTTARD SADRSTADDT
TLLVDDRLWA TFSQDLRACV PNATFGLAST VLEEVRIRKD ARELDALRRA GAVADRVSLE
VRSRGEDLIG MSERELAGEI ERLLASAGGG EPAFSTIVAS GPNGARPHHH SSDRPIEVGD
PIVLDFGAFV AADLEGGTGR YPGDQTRTMV VGEPPAKYRQ VHETVLHAQQ AAIDAVEPGV
TAGSIDRAAR SVIEDAGYGD AFVHRTGHGV GLEVHEPPYI VDGNDRELEP GMVFSVEPGI
YLEGEFGVRI EDLVVVTDDG AERLNDSPRG WATGSVGEQ
//