ID A0A1Y3MSH7_PIRSE Unreviewed; 260 AA.
AC A0A1Y3MSH7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Carbohydrate-binding module family 18 protein {ECO:0000313|EMBL:OUM58177.1};
GN ORFNames=PIROE2DRAFT_16620 {ECO:0000313|EMBL:OUM58177.1};
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:OUM58177.1, ECO:0000313|Proteomes:UP000195826};
RN [1] {ECO:0000313|EMBL:OUM58177.1, ECO:0000313|Proteomes:UP000195826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2 {ECO:0000313|EMBL:OUM58177.1,
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; KZ151229; OUM58177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3MSH7; -.
DR STRING; 73868.A0A1Y3MSH7; -.
DR Proteomes; UP000195826; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR CDD; cd00035; ChtBD1; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR041219; Phage_lysozyme2.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF18013; Phage_lysozyme2; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW Reference proteome {ECO:0000313|Proteomes:UP000195826};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..260
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012215178"
FT DOMAIN 26..68
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DISULFID 36..48
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 41..55
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 260 AA; 30025 MW; E91918C49B0311B2 CRC64;
MRYLNIILIA IAVISSTSAA PAAFLKDRCG PGEGECDPGH CCSQYGWCVT FKDHCGKGCQ
SEFGVCENNS TSKTTKTKTT KIKTTKTKTT KTTKTSKLTV LNQQLIHHQL NRKINMVRTV
DNGLVQWTSK KRKTKLFNYA REHSKSIGDL QMQLDFLWLE LQDKKYDNER AKYGKISKNE
IFIPNNEMRE IFEIFIQSKN YQNLNKKIKN SKNICVTRPR PFGKTVTVNM IKAYYSFSES
KITVFDDKRI SEIKNWDKYL
//
