ID U6KLZ3_EIMTE Unreviewed; 767 AA.
AC U6KLZ3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=X-prolyl aminopeptidase, putative {ECO:0000313|EMBL:CDJ39001.1};
GN ORFNames=ETH_00029300 {ECO:0000313|EMBL:CDJ39001.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ39001.1};
RN [1] {ECO:0000313|EMBL:CDJ39001.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ39001.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ39001.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ39001.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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; HG674134; CDJ39001.1; -; Genomic_DNA.
DR RefSeq; XP_013229756.1; XM_013374302.1.
DR AlphaFoldDB; U6KLZ3; -.
DR EnsemblProtists; CDJ39001; CDJ39001; ETH_00029300.
DR GeneID; 25254953; -.
DR VEuPathDB; ToxoDB:ETH2_1328100; -.
DR VEuPathDB; ToxoDB:ETH_00029300; -.
DR OMA; LVDQAWG; -.
DR OrthoDB; 869at2759; -.
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:CDJ39001.1};
KW Hydrolase {ECO:0000313|EMBL:CDJ39001.1};
KW Protease {ECO:0000313|EMBL:CDJ39001.1}.
FT DOMAIN 13..136
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 408..668
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 679..758
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 767 AA; 84739 MW; C075026AAB8C217A CRC64;
MVSRGVDAAA AERLGALRLL LQAHQLDGLI VDDADAHGSE IPARAFARRT FLSNFSGSNG
LALVTRDSAF LWTDGRYFSQ AEQQLPVGLW QLMKSDFGNT PTLTQFLKQE TKIRRLGVDA
FTTSLGLLSQ IKEAGFNVQR EAQTHQGSQD ASVRHIIPLD QNLVDEIWGV QRPVLPSSSV
YAHPKEFRGL STREKVARTV QTMAKEGADL LLLSSLDEVA WLTNLRGSDS PNSTVFYSYA
LLAKGPNVAS TEDPHCAKPC PWRLLVYTDP TRVSSSAKAE LETEGAVLRP YESLASDLQL
LLTWNLRQQQ QLLQREHQQL PEDLQQQTHG GLLGAVDWLL AGGDETRHEP RSKLQITGAL
DERRAAWLDP KINLAIHRIL ADSKRLIVKD TPVSVAKAAK DEKELKGMAE AHEDDGVALA
TFFCWFEKQL LANARATMTP PQQQEHGGQE CSLTEWTLKE AVDASREAMS DLFRGTSFAS
ISCFGSNCAL AHYRPDPETS LQLKARMSEP QGLLCVTVRG PGGDPPAQNE SPVFLLDSGG
QYLTGTTDVT RTLHLGEPTD EQKEAYTLVL KGMIGLSAQK FPEGSKGPQI DALARQHLWN
RGLDYMHGTG HGVGHFLNVH EGPIGISPRL TGAASLHEMQ PGAVLSIEPG FYKDKAFGIR
IENLAAVKPS GLSHRGRRFL EFDSLTLVPI QARLIDASLL TRQEIAWLDA YHQRVFTRIS
SRLTTKGKDF PFRPPLPQAV SVTSEEVRLW LKKNTQPLHE LLQTEWP
//