ID A0A1Y3N4C1_PIRSE Unreviewed; 454 AA.
AC A0A1Y3N4C1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE SubName: Full=Carbohydrate-binding module family 18 protein {ECO:0000313|EMBL:OUM62355.1};
DE Flags: Fragment;
GN ORFNames=PIROE2DRAFT_11358 {ECO:0000313|EMBL:OUM62355.1};
OS Piromyces sp. (strain E2).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM62355.1, ECO:0000313|Proteomes:UP000195826};
RN [1] {ECO:0000313|EMBL:OUM62355.1, ECO:0000313|Proteomes:UP000195826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2 {ECO:0000313|EMBL:OUM62355.1,
RC ECO:0000313|Proteomes:UP000195826};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; KZ150937; OUM62355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3N4C1; -.
DR Proteomes; UP000195826; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd00035; ChtBD1; 1.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW Reference proteome {ECO:0000313|Proteomes:UP000195826}.
FT DOMAIN 12..56
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 72..114
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT COILED 259..289
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 82..94
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 87..101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OUM62355.1"
SQ SEQUENCE 454 AA; 51196 MW; B5682AC5F3FCFA32 CRC64;
PLTIASNIKC EQFYTVQADD YCYGISAGNG ISLTKLKILN PEIDCENLIP GSSVCTKGNL
HYSDYVDYVS VDGRCGEGYG NCPAGQCCGS NGYCGTGDEY CGIGCQTGFG HCYIPGTTMV
KRDYTYETVE NNIVDQSTNI KEKVNDAMEQ LFPDAKEAEE FKSFSEFALA GFENAMNFTE
IHDGVDLQSI NTDECKAKCG AALAQFEYVI NDPNNNFNLE SYNDVLQLSD QGSIDKDYFF
NVCINQCYLI DEFKEVYANA NISESVESMK EEIQHMEELS NSTDNLRKRE EFDCSKKETY
ITVHHYVNDD KDLPVYNAND GSIFNRNTGG RVDGCSAQYK ILQDFIYFFT PACNGHDSCY
HCSEKEECDK AFQNNMFSLC DKGYSIVPKP KLLFACKTVA TTVRLIVQYA EFAFDGYKWD
HEFVAKHKGK NTNEFASYCV CDDYDMKHFV KNNE
//
