ID A0A1I3W3U5_9RHOB Unreviewed; 593 AA.
AC A0A1I3W3U5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:SFK01091.1};
GN ORFNames=SAMN04488138_11942 {ECO:0000313|EMBL:SFK01091.1};
OS Celeribacter halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=576117 {ECO:0000313|EMBL:SFK01091.1, ECO:0000313|Proteomes:UP000183299};
RN [1] {ECO:0000313|EMBL:SFK01091.1, ECO:0000313|Proteomes:UP000183299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8891 {ECO:0000313|EMBL:SFK01091.1,
RC ECO:0000313|Proteomes:UP000183299};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766}.
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DR EMBL; FORY01000019; SFK01091.1; -; Genomic_DNA.
DR RefSeq; WP_066605170.1; NZ_QKZJ01000021.1.
DR AlphaFoldDB; A0A1I3W3U5; -.
DR STRING; 576117.SAMN04488138_11942; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000183299; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
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; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:SFK01091.1};
KW Hydrolase {ECO:0000313|EMBL:SFK01091.1};
KW Protease {ECO:0000313|EMBL:SFK01091.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183299}.
FT DOMAIN 17..151
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 311..519
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 534..592
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 593 AA; 65168 MW; B3CDBFE3B352AD60 CRC64;
MFQSFDVTTR PEQAAPRVTA LRKEMLDTGL DAFLVPRADA HQGEYVAPCD ERLAWLTGFT
GSAGFAVMLA SQAAIFTDGR YTVQVRAQCD PKLFDYIDWP ATSLGTWLLK TDAAKIGFDP
WLHSIREVES LRKTLLGTGK EMIATSNLVD RIWTDRPARP SAPVSKQPVE LTGKTSEEKF
AEIGEAVAAQ GAEAVVLTLP DSLSWLLNIR GSDIAHNPVV QAFGILTITG RLMLFDDAAK
YADLGPDPRI SILPRAAFGM ALEELTCRVL VDTNTAPFAV KTMLKNAEIV EGDDPCILPK
ACKTPEEIAG TREAHLRDGA AMVEFLSWLS EQPPENLTEI EVVKALESFR AATNQLKEIS
FDTICGSGPN GAIVHYRVTE DTNRALREGE LLLIDSGAQY QDGTTDITRT IALGDPGFEE
RAAFTAVLQG MIAISTAAFP RGVAGAHLDA LARAPLWRMG RDYDHGTGHG VGSYLSVHEG
PQRISRTSLL PLQEGMILSN EPGYYREGAF GIRIENLIAT QKAPDIEGAD GRDMLNFETL
TWVPIDRNLI LADELAPWER DWINDYHETV WEKLKDRVSE QAHVWLRQAV TPV
//