ID D1AU95_ANACI Unreviewed; 570 AA.
AC D1AU95;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Putative aminopeptidase {ECO:0000313|EMBL:ACZ49123.1};
GN OrderedLocusNames=ACIS_00504 {ECO:0000313|EMBL:ACZ49123.1};
OS Anaplasma centrale (strain Israel) (Anaplasma marginale subsp. centrale
OS (strain Israel)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=574556 {ECO:0000313|EMBL:ACZ49123.1, ECO:0000313|Proteomes:UP000000630};
RN [1] {ECO:0000313|EMBL:ACZ49123.1, ECO:0000313|Proteomes:UP000000630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Israel {ECO:0000313|EMBL:ACZ49123.1,
RC ECO:0000313|Proteomes:UP000000630};
RX PubMed=19854912; DOI=10.1128/JB.01330-09;
RA Herndon D.R., Palmer G.H., Shkap V., Knowles D.P. Jr., Brayton K.A.;
RT "Complete genome sequence of Anaplasma marginale subsp. centrale.";
RL J. Bacteriol. 192:379-380(2010).
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766}.
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DR EMBL; CP001759; ACZ49123.1; -; Genomic_DNA.
DR RefSeq; WP_012880594.1; NC_013532.1.
DR AlphaFoldDB; D1AU95; -.
DR STRING; 574556.ACIS_00504; -.
DR KEGG; acn:ACIS_00504; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_011781_2_1_5; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000000630; Chromosome.
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:ACZ49123.1};
KW Hydrolase {ECO:0000313|EMBL:ACZ49123.1};
KW Protease {ECO:0000313|EMBL:ACZ49123.1}.
FT DOMAIN 5..126
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 292..505
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 511..570
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 570 AA; 63735 MW; EF2FC4C68955D0F0 CRC64;
MDAKLRKLLP IMDEQGLDAL LLHHTDEYQS GWVHESRQRV KWLCGFSGSN AFLIICKKGK
SQFFTDSRYI VQSALEVDKD SYDVHDFRDL TPFAWLEEHI DEYPVVGYEG ELFTLSQVGR
YAKFLPKMVQ HIMLDKIWQR PMQIHQRIQE HPIKFAGLSS REKRAAVAHT LPTSGVMLMT
DVDAISWLLN IRNMAFTHTP SVLSRAILHS NGGVELFVDA AADQVHISDE DVRVFSIDKL
HGALMSAHSI VVDASTIPMS IFDAVRSKVV TIRDDDPCTF PRATKNETEI RGMIQAHVRD
GVAMTNFLYW LHTELANCRE VTELGAALKV REFREAQELF AGESFDAISG FGGNGAIVHY
RVNEKTSQVL REGGLYLLDS GGQYLDGTTD ITRTVAVGTP SREHIERFTD VLKGHIALAR
AVFPTGTSGG DLDVLARQCL WQKGLDYGHG TGHGVGSFLS VHEGPQAISR SNRVALLPGM
VLSNEPGYYK VGEYGIRIEN LMYVEACGEG FCRFQQLTRV PLDKNLIDTK MLSSEEIKYV
NDYHSFVYNE VAPHVAAAVK AWLQTACSPL
//