ID A0A1Y3NU33_PIRSE Unreviewed; 232 AA.
AC A0A1Y3NU33;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Carbohydrate-binding module family 18 protein {ECO:0000313|EMBL:OUM68743.1};
GN ORFNames=PIROE2DRAFT_3428 {ECO:0000313|EMBL:OUM68743.1};
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:OUM68743.1, ECO:0000313|Proteomes:UP000195826};
RN [1] {ECO:0000313|EMBL:OUM68743.1, ECO:0000313|Proteomes:UP000195826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2 {ECO:0000313|EMBL:OUM68743.1,
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; KZ150767; OUM68743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3NU33; -.
DR STRING; 73868.A0A1Y3NU33; -.
DR Proteomes; UP000195826; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR CDD; cd00035; ChtBD1; 2.
DR Gene3D; 3.30.60.10; Endochitinase-like; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR47849; CHITIN-BINDING LECTIN 1; 1.
DR PANTHER; PTHR47849:SF8; LECTIN; 1.
DR Pfam; PF00187; Chitin_bind_1; 2.
DR SMART; SM00270; ChtBD1; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 2.
DR PROSITE; PS00026; CHIT_BIND_I_1; 2.
DR PROSITE; PS50941; CHIT_BIND_I_2; 2.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Reference proteome {ECO:0000313|Proteomes:UP000195826}.
FT DOMAIN 13..60
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 172..219
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DISULFID 26..38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 31..45
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 185..197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 190..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 232 AA; 26238 MW; 5788EC8493397189 CRC64;
MYQRRGNRNK NVFQKCGKID GEKVKCPEGQ CCSKDGVCGT TPDFCSIEKE CQSEFGECFV
TCDELLKKIP IQKVDDEDDT YCENNENGYV NSLKITSTEI ETLPSFENLT SLEEILIHDN
KLKSLPEGLE NLPNLNTLDI SRNCFECPVK PNIESLEQYT CIRDEASERK CLPKCGEIDG
EKVKCPKGQC CSKDGVCGTT PDFCSIEKEC QSEFGECFIT CDELLKKFQY KK
//
