ID A0A1J1IP55_9DIPT Unreviewed; 438 AA.
AC A0A1J1IP55;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=CLUMA_CG013546, isoform A {ECO:0000313|EMBL:CRL00273.1};
GN ORFNames=CLUMA_CG013546 {ECO:0000313|EMBL:CRL00273.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRL00273.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRL00273.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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DR EMBL; CVRI01000054; CRL00273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1IP55; -.
DR STRING; 568069.A0A1J1IP55; -.
DR OrthoDB; 3475672at2759; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
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; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 3: Inferred from homology;
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..411
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 281..417
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 29..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 438 AA; 49466 MW; B6B8F6E3854D5C49 CRC64;
MFVMSSLNFK AEEKLKYLMD NSNDSKAIKD HSSLCDSSTH TNSSENYSQQ CKNNDDDFES
ESSTVYDSDT EQLEIDSVPK VCQVYDDEKN ISQFGNVIII DQKEENNKTS PKFESVSIHN
SSDIQIGNKT FYNGPVTIKQ FLVDDKNNKW VENQNFDNKS ELSLEGIINK GYVVSQNNVI
ESPLTKDKHN KCGNEILKLR ESGLYRKNVY LILLTAICSM IGIILLRFYV MKGEDLKHGI
VLGDGDDSRK NIAINSTIGS DLLLGNVLRM ISRDEWLAQP ANNELSNLIL PAKRVIIAHT
ATEPCDTQAS CTLRTRYIQT FHMESRSWDD IAYNFLIGGD GAVYEGRGWD KQGAHTKGYN
VGSIGVAYIG TFTKKLPNEK QIHAGFLLFK EGVRLKKLLP DYKIYAHRQL IPSESPGAAF
YEIIKKWDHW ASDAPEIL
//
