ID A0A165XB96_9AGAM Unreviewed; 821 AA.
AC A0A165XB96;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glycoside hydrolase family 18 protein {ECO:0000313|EMBL:KZV65859.1};
GN ORFNames=PENSPDRAFT_112379 {ECO:0000313|EMBL:KZV65859.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV65859.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV65859.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV65859.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV424612; KZV65859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165XB96; -.
DR STRING; 1314672.A0A165XB96; -.
DR InParanoid; A0A165XB96; -.
DR OrthoDB; 50378at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00035; ChtBD1; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF401; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 2.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 2.
DR PROSITE; PS51910; GH18_2; 1.
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}; Hydrolase {ECO:0000313|EMBL:KZV65859.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077086}.
FT DOMAIN 149..187
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 188..232
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 245..607
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 56..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 158..170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 163..177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 181..185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 202..214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 207..221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 821 AA; 88238 MW; 18C9663832A32A96 CRC64;
MAFGEHHTRR CIFAIVLLTF SILAFITESN AIKSVYLSPR AQQRRRERRQ ELAALAEQHR
SPLAHRAPPV SVPNLPRRPP ASLQAPSHPP AYVLASASSR SKITVPSTLR EKSSFGHAHG
HKGLANRLRA RQTNNESCNN ITITPPGFDG SCSVGNPCPN GACCGVSGFC GYGKTYCGDG
CTSNCDAVAA CGPDAAPGNQ ECPLNVCCSK FGFCGSTDDF CGANCVGDHC GIPSIPSGVN
SEVTTRIVGY YEGWASSRPC DAWYPMNIPS NGYTHLNYAF ALIDPDTYAV VPMAASDVAQ
YTQFTNLKQS NPNLKTYISV GGWSFNDPPT QTVFSDLAAS ETNRQAFSNS LVQFMVTYGF
DGADIDWEYP VACERGGVPA DRENMVAMFK TMRDTFDASG HTFGLTFTAP TSYWYLQHFD
LLGLLSYADW VNLMAYDLHG VWDAKDVFIG NIVQAHTNLT EIKESVNLFQ RVGVPLDGIV
LGLGYYGRSF QLSDPACSTP GCAFAGPAPG GPCTASDGTL SFSEIQNILV RTTSAGSAAT
SPPVYDQDAQ VKYVVYDTDN WVSYDDTQTL NAKVSWAKGA GFGGLMVWSV DQDDFSSTAL
SAILGQDATQ VIPSAIDVNS KDGKACMQPG CGQTCPSGYV QMADTTDGKL ASPSTGCNHI
GNPVCCPVDQ IPQNCQWRGT ASSCNGVCEV GEITLATDSW GTGAKCTSGH KAFCCQSGLT
QDEIEKATNC AWYGHQSKNC NDNVCPAGTF TKATDYYGDT GLLHACVMQE KQFCCYPPDG
KTTNNPFDVV RTLLPTSVRC YQAYAGAQRT IYSRIRPMMV I
//
