ID U6KLY6_EIMTE Unreviewed; 912 AA.
AC U6KLY6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Penicillin amidase domain-containing protein, putative {ECO:0000313|EMBL:CDJ38991.1};
GN ORFNames=ETH_00029250 {ECO:0000313|EMBL:CDJ38991.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ38991.1};
RN [1] {ECO:0000313|EMBL:CDJ38991.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ38991.1};
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:CDJ38991.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ38991.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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DR EMBL; HG674134; CDJ38991.1; -; Genomic_DNA.
DR RefSeq; XP_013229746.1; XM_013374292.1.
DR AlphaFoldDB; U6KLY6; -.
DR MEROPS; S45.003; -.
DR EnsemblProtists; CDJ38991; CDJ38991; ETH_00029250.
DR GeneID; 25254943; -.
DR VEuPathDB; ToxoDB:ETH2_1327500; -.
DR VEuPathDB; ToxoDB:ETH_00029250; -.
DR OMA; TINEAYW; -.
DR OrthoDB; 201899at2759; -.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1400.10; -; 1.
DR Gene3D; 2.30.120.10; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
DR InterPro; IPR043147; Penicillin_amidase_A-knob.
DR InterPro; IPR023343; Penicillin_amidase_dom1.
DR InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR InterPro; IPR002692; S45.
DR PANTHER; PTHR34218:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 1.
DR PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR PIRSF; PIRSF001227; Pen_acylase; 2.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT REGION 241..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 102615 MW; 08C7945F24F0ABC5 CRC64;
MPCDAVEVSG WSASRRVSLD PWDYYALTYT DFFSFVVGLI GRPVISRFFT PDEAFWNTPA
EVPGIQSTIK IGHDKYGLPY LTASSQRPAQ IELLRLVATG KSAAVLGASM TDTDMITRTV
ISEEALLWKL RKLPRHGVAC LIAYSRGKPR LSHKLQDPRL LLSGEHYFDF LTAPCRALMR
GLTRDFVRVH LKESLGDKWK LFDFGFPEGV PPLNPEGSGP SLYDLEGKPV AFPSVELKDT
EWSTRGPSAF PEITEGPHSL NPEFGGPMHD RDPSPKMTPE RMHQFKEDMQ RAEDFYDLKH
PKPWTTEQQP QHSNTFSLKV DGSNGWAVSG KLTKTGMPLL AGDPHVEVNA PGFWMPMWLK
SDGKLDGLPV RGVGATAVGT TGMFIGHNDY AAWTQTVAHT DIEDLFLVEL NEEGTHYYYG
GKQYPLKFIE HNIYVKGRPN PIRHISRYSH HGPLFSDAVP PLRKRIGKNQ ALVLASVALR
APLPVAWAEK MLFGKEWKDY IEMGQHAQMN EFVCIWATKD GAIGASVTGA VPVRPFSTIP
QFRDGSDPKQ DWKGVLPQEQ IPFVMNPKSG IIVAGNSVLA DDPKRLFGEV FVPGHRVRRA
HQLLADLKSK KEIEIQDLIK MQEDQYSEHG CEFKDFVLKE FLHRFDLKND QEEATALCAD
EGLTPYVARL LTAAMESWDC SMNATSHGAS IYEVWLQMVL QGVFAANNWS DEALFSLVES
GLLPAEYPLS RLLCKSATDT VKYLMGRLGP DVKDWHWGKL RSRYIDHLFV RDAPALRHLL
SVGPLKWGGN FGTLKAHHFE PHILKADDPL TGNFHRGIDT TSLRVVFDLS NWENSLWAYY
PGVSGWPGSK HYGDTAELLE DGKEKLMPIP WDEEKIEASL IATKILSPKQ ERQQAPQRSQ
QPPRQQQQKQ EF
//