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Database: UniProt
Entry: A0A0L0C1T7_LUCCU
LinkDB: A0A0L0C1T7_LUCCU
Original site: A0A0L0C1T7_LUCCU 
ID   A0A0L0C1T7_LUCCU        Unreviewed;       897 AA.
AC   A0A0L0C1T7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Peptidoglycan-recognition protein LE {ECO:0000313|EMBL:KNC26217.1};
GN   ORFNames=FF38_05391 {ECO:0000313|EMBL:KNC26217.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC26217.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC26217.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC26217.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC26217.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNC26217.1}.
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DR   EMBL; JRES01001003; KNC26217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0C1T7; -.
DR   STRING; 7375.A0A0L0C1T7; -.
DR   EnsemblMetazoa; KNC26217; KNC26217; FF38_05391.
DR   OMA; IACAKEQ; -.
DR   Proteomes; UP000037069; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 3.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 3.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR015510; PGRP.
DR   InterPro; IPR006619; PGRP_domain_met/bac.
DR   PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR   PANTHER; PTHR11022:SF78; PEPTIDOGLYCAN-RECOGNITION PROTEIN LE; 1.
DR   Pfam; PF01510; Amidase_2; 3.
DR   SMART; SM00644; Ami_2; 3.
DR   SMART; SM00701; PGRP; 3.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 3.
PE   3: Inferred from homology;
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037069}.
FT   DOMAIN          127..270
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   DOMAIN          139..276
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
FT   DOMAIN          418..561
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   DOMAIN          430..567
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
FT   DOMAIN          731..874
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   DOMAIN          743..881
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
FT   REGION          22..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   897 AA;  100412 MW;  68EEC260174BFB66 CRC64;
     MKEIVKKMLS LKVSNTSNVE TSDKEKQISK RISTTTGNTS PATKGQLVPD MNAIQDTLLE
     LSTSVVKSNI TITDSSNVHL GNKINYDGNL YLNLLKQNNE TGISLIQHDN NNGVLIKTTS
     NVHISDYPII PRSFWSIRKP REEYDKIKEP VGLVVISHTA TTSSTNQSKN IQLIRDIQAF
     HVDTHNWNDI GYNFLIGCDG TIYEGRGWGI EGAHTFGYNN RSMGITFIGC FINKKPTEDA
     LYACKNLLER GISEGHLDKN YKLLGHRQCS ETESPACETL DDAESLASSI VESSIVDSAS
     EADGENSQDD DDDSRSYTNI SELPIYNQLL NTNSLRKQLE QIAPLATYNN VNVANSSNVV
     FGNVIKVKGV LNINVYNKDK NNKNYNENQE ENIDPLHKRR ESSPQANKES LNDNSSLCRI
     IPRNYWSTLE PSEEFEYVDG PVDIVIISHT ATDSSLSSQE NTQLLRNIQT FHVDVQGWDD
     IGYNFLIGCD GNIYEGRGWN VVGVHTYGYN RRSLGIGFIG SFSRSLPSEK AIEACKNLLK
     RGIEEGHLKK DYKLLGHRQC IATVSPGRLL YEEITKWENF YPKDIHDDLK QVLCKNMSKL
     PANKCDEIRS WLNSIDINED AELSDVEESC SVSVVESSII ESSSSSSDSG DEVALGQSSH
     NHIKEYNNNL LPQIPALSFN NVNICNSSNV YLGNIYSVNG TLNINVINGE EKPQEDQEPT
     AKKSPVIRPA CLIFPRYRWL AMDPLSESNK LPEPVEFISI GYTATTSSTV QARNIGIIRD
     YQTLNVEAQG FNDIIYNFLI GCDGTIYEGR GWGVEGEHTA GYNHKSIGIA IVGNFKQELP
     PERTFKACQK LITRGIEEGH LSKDYKIFAP PTANYNLLNE ELKKWDHFWD IKNCNES
//
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