ID A0A182SJE2_9DIPT Unreviewed; 237 AA.
AC A0A182SJE2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Peptidoglycan-recognition protein {ECO:0008006|Google:ProtNLM};
OS Anopheles maculatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; Anopheles maculatus group.
OX NCBI_TaxID=74869 {ECO:0000313|EnsemblMetazoa:AMAM007932-PA, ECO:0000313|Proteomes:UP000075901};
RN [1] {ECO:0000313|Proteomes:UP000075901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=maculatus3 {ECO:0000313|Proteomes:UP000075901};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles maculatus species B.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMAM007932-PA}
RP IDENTIFICATION.
RC STRAIN=maculatus3 {ECO:0000313|EnsemblMetazoa:AMAM007932-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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DR AlphaFoldDB; A0A182SJE2; -.
DR EnsemblMetazoa; AMAM007932-RA; AMAM007932-PA; AMAM007932.
DR VEuPathDB; VectorBase:AMAM007932; -.
DR OrthoDB; 3432610at2759; -.
DR Proteomes; UP000075901; 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; 2.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 2.
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:SF66; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR Pfam; PF01510; Amidase_2; 2.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 2.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 2.
PE 3: Inferred from homology;
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 2..90
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 84..220
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT DOMAIN 91..214
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
SQ SEQUENCE 237 AA; 26794 MW; 405A00982A6BE4F9 CRC64;
MDGKNYDDIT FNFLIGGDGQ IYEGRNWYKI GAHTHGYNSK SQGIAFIGDY NYANKPTEKQ
MELLKYLLEY GARHKQLSES YKIYASEQLD PVSPTGKWLI EALRTLPQFT KCMYQVKLIQ
EFHADPNSRN FSDIAYQFLV GGDGNAYEGR GWTKQGAHTK GFNVDSICIA FIGTFIVAPP
PAAQLSAAQQ LIELGLQENY LASNYSLYGH RQLAPFESPG KALFDIIKTW PHWSNKL
//
