ID A0A061H0X4_9BASI Unreviewed; 659 AA.
AC A0A061H0X4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=GH18 domain-containing protein {ECO:0000259|PROSITE:PS51910};
GN ORFNames=PFL1_06766 {ECO:0000313|EMBL:EPQ25694.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ25694.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ25694.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ25694.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000822};
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DR EMBL; KE361652; EPQ25694.1; -; Genomic_DNA.
DR RefSeq; XP_007882503.1; XM_007884312.1.
DR AlphaFoldDB; A0A061H0X4; -.
DR GeneID; 19320837; -.
DR KEGG; pfp:PFL1_06766; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_6_2_1; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF406; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..659
FT /note="GH18 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001599562"
FT DOMAIN 227..659
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 38..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 68436 MW; 610552B26DB78DD8 CRC64;
MKLLPLALTA LATMATTATA IPGYDDVPFH LSRSANAVPG PSSLAPTPSS SGSYARSSQG
PGTARASSAP GRRSGAGAGA ALEPQPPAVG RTTASVWDIL GGRRRRAVRS GQPRAEQRSP
SFSTMIEMVD PGTRSKGKGK ARATESDVVG GGRRTKRAKT CKRQDGAGGK GSATGGASSG
AGSATASGIV AAPTATASAK PGATNTNTTT TTNTTTTDGD KTVDTGKVMA GYWPDWSSSS
LPPEKIDFSK FDFINYAFAL PTQDFNLNFP TDNTKGLLKR LVTAAHGAQS KVVLSIGGWG
GSTYFSPAVK TSASRSKFIA NIKGVYDQYQ LDGIDLDWEY PGQGNEGNQY DPQDTMNFQT
FLQELRAALP QGAILSAAVS HQPWIASTGQ PVTSVERAAS ALDYVLIMNY DVWGSSGNPG
ANAPLADLCG NSSQPSANAA AGVKQWASAG MPREKILLGI PSYGYINSSS RRKLKARSDN
SLRAKTLAIR DASPSKGATT PPGYVAAPER DEGSLLELRS DVPSGRVGRY DARRLPSSGS
SSTAPALSRR GTLTSSDGST SSGQINFNQL VKQGALTKDK STGLFVAAGG YQKYWDDCSD
TPYLANGQTV VTYDDTSSLW DKGAFAVQAG IGGLNIWSID GDTDGWDLVN SAIAGMSQA
//
