ID L0ICZ3_HALRX Unreviewed; 388 AA.
AC L0ICZ3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:AGB15807.1};
GN OrderedLocusNames=Halru_1191 {ECO:0000313|EMBL:AGB15807.1};
OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB15807.1, ECO:0000313|Proteomes:UP000010846};
RN [1] {ECO:0000313|Proteomes:UP000010846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18193 / JCM 13892 / XH-70
RC {ECO:0000313|Proteomes:UP000010846};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Halovivax ruber XH-70.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003050; AGB15807.1; -; Genomic_DNA.
DR AlphaFoldDB; L0ICZ3; -.
DR STRING; 797302.Halru_1191; -.
DR KEGG; hru:Halru_1191; -.
DR eggNOG; arCOG01000; Archaea.
DR HOGENOM; CLU_017266_4_1_2; -.
DR OrthoDB; 1346at2157; -.
DR Proteomes; UP000010846; Chromosome.
DR GO; GO:0004177; F:aminopeptidase 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; IPR001714; Pept_M24_MAP.
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 PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:AGB15807.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:AGB15807.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010846}.
FT DOMAIN 13..145
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 154..372
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 388 AA; 42146 MW; A52104C352589E39 CRC64;
MTASQPTFDY EARTRACQEA LADRAIECVV LSPGPNMTYL SGFVDEPMER HLLLFVPQSG
EPIFLAPTMY DEQLQADSWV SRRRLWDDGD DPTDALAEIV ADLDLAGGRV LVDDRMWALF
TQDLRDAMPD ATFGLASEVL TELRLTKSEA ELEVMARAAT VADDVSVEIR ELGSSAVGMT
EAELAREIET RLADHGGDGP SFETIVGAGP NGAKPHHRHG DRAIRAGDPV VLDFGTRVDG
YPSDQTRTVV FGEDDSTATG DSTGPETVPD EFSRVFETVR EAQETAVAAV EPGIPAEAVD
RAARDVIEAA GYGEQFVHRT GHGVGLEVHE PPYIVAGNER TLEPGMVFSI EPGIYVQDSF
GVRIEDLVVV TEDGCRRLND SPHGYTVR
//