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Database: UniProt
Entry: A0A022QM75_ERYGU
LinkDB: A0A022QM75_ERYGU
Original site: A0A022QM75_ERYGU 
ID   A0A022QM75_ERYGU        Unreviewed;       425 AA.
AC   A0A022QM75;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Transglycosylase SLT domain-containing protein {ECO:0000259|Pfam:PF01464};
GN   ORFNames=MIMGU_mgv1a006936mg {ECO:0000313|EMBL:EYU27575.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU27575.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU27575.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC   -!- FUNCTION: Defense against chitin-containing fungal pathogens.
CC       {ECO:0000256|ARBA:ARBA00003102}.
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DR   EMBL; KI631456; EYU27575.1; -; Genomic_DNA.
DR   RefSeq; XP_012849375.1; XM_012993921.1.
DR   AlphaFoldDB; A0A022QM75; -.
DR   STRING; 4155.A0A022QM75; -.
DR   GeneID; 105969176; -.
DR   KEGG; egt:105969176; -.
DR   eggNOG; ENOG502QQ89; Eukaryota.
DR   OMA; DCGHRAY; -.
DR   OrthoDB; 334560at2759; -.
DR   PhylomeDB; A0A022QM75; -.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00254; LT-like; 1.
DR   Gene3D; 1.10.530.10; -; 2.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   PANTHER; PTHR37179; TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR37179:SF1; TRANSGLYCOSYLASE; 1.
DR   Pfam; PF01464; SLT; 2.
DR   SUPFAM; SSF53955; Lysozyme-like; 2.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT   DOMAIN          74..173
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
FT   DOMAIN          317..395
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
FT   REGION          204..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   425 AA;  48432 MW;  CBE8C954FEB48071 CRC64;
     MASVSFKYWN DCVDPEDLDA MWMEPDVRAE WIDVGETMGS KVHLSRDPDG QPYLTQTEMR
     AVAGIIVRRH FVSQIDSDML CAIAELESDR QPLATSYNKK SEDVKMGIMQ ISPRTSEWLT
     RELGYSAYQV AEDPKFLYKP FLNVYLAAAY LKWISNYDQK ERSEEFMVRA YKGSIKKATH
     KSTLPYWRKY LSVKESLPSR KAFGVGSAPN VPSSSATAVS QSKEASPVNA TWDSRTSGED
     MEDMWNHPDV NKEWTKSGER RGNVRLSHDA EKHPYLSRVE LRAVAEIILA KHSNIKGVKP
     TVLCAVSEMV SMRFVNGVGQ RTGLMGIDYP TARWLYKDGG YKGYMVQSTE DLTKPFVSMY
     FGAAYMAWLS QYEGRERSLQ FVVQAYLSGP QNVNLQETGP LWMKFEEALS RYEETRRENG
     SCVIM
//
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