ID G0R6S5_HYPJQ Unreviewed; 1377 AA.
AC G0R6S5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN Name=chi18-1 {ECO:0000313|EMBL:EGR52181.1};
GN ORFNames=TRIREDRAFT_71245 {ECO:0000313|EMBL:EGR52181.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR52181.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR52181.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
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DR EMBL; GL985056; EGR52181.1; -; Genomic_DNA.
DR RefSeq; XP_006961155.1; XM_006961093.1.
DR STRING; 431241.G0R6S5; -.
DR EnsemblFungi; EGR52181; EGR52181; TRIREDRAFT_71245.
DR GeneID; 18488083; -.
DR KEGG; tre:TRIREDRAFT_71245; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_71245; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002846_1_0_1; -.
DR OrthoDB; 11640at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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 CDD; cd02878; GH18_zymocin_alpha; 1.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
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 InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR47700:SF2; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Hydrolase {ECO:0000313|EMBL:EGR52181.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1377
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003408174"
FT DOMAIN 344..389
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 408..456
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 550..911
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 316..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1377 AA; 146511 MW; AAB6041C360733FA CRC64;
MRLTLGVAAV CLAAGAFWTP QGALAASSNA AADALIASLS QANSIKTASG PVSSRPTDRA
SARAAVLAGN FTSKLHHERR DRNRNSCPAA CNSADTGSWD VFHDINRLKE CNQTMLLDFA
LFNHVDDSKP VVKISACTAD LKVNENRLHS LSKTNDCAVE GVELSSKTTQ IQLGSSGASS
KTHVADVSAA LDQLLALSSI SSANCQETIK YATSGDVIIG VYAGSGIASQ GVLASVIDKL
SSEIQSNGQV TENLVAQVCG SKTPARYTLG IFATTKGHLG AVQRSVQSWK NGTCVATSST
GDVKIKSSSN SVTYLAPSAS HNNSTSKSSS GNSKKPLSAR ADCRTIQVEA GDSCASLATE
CGITPAQFTQ YNPSSTLCGA LTPGQHVCCS SGTLPDFTPK PDDKGYCYSY LVKDGDSCAS
IGAAYDLTNA QIESFNKKTW GWNGCAKLFA SYKICLSTGY PPMPAPVANA VCGPQVNGTT
PAPPGVDIST LNECPLNACC NIWGQCGTTG DFCTPSNSST GAPGTAAPNE NGCISNCGDE
ILTSDPPAET MNIAYFEAFD QKRTCLKMPV TAVDTSAYTH IHFSFITLNE DYSVNIDGVE
SQLRLLSGMA GVKRIVSVGG WDFSTSPSTY QIFRKAVSSE ENRQTLVNNI VDFLAEYDLD
GVDWDWEYPD EPDIPGIPEG TEDETTGYFL LLDELKLKLP SNRTVSITAP ASFWYLQYFP
ILALSFVVDY IVYMTYDLHG QWDYINKYAS PGCPSYDQGL GNCLRSHVNL TETLNALSMI
TKAGVPSNMI TVGVSSYGRS FQMSSAGCWT EQCTYTGPDS GALPGPCTNT SGYISNYEIN
RIVAGNPSAE VHWDQDSYSN IVVYNGTQWV AFMNDSNKAT RTALYPSINF LGIADWAVDL
LSEDGDSPDS SSSSEQTIYI DPGIWSSATP SVVAPPGASL IWPPKPLGST TTITFPLWTT
TVSYSSLTTE TSTLTDGSTT TYHAYVWVSW LTTLTIPAGI WGVSLNKSSS TGTIYLTSSV
QPPPFKVTIT PVVSGTTSII GPTKTSTIKG TVITYGSETW TEQDETQTQG RSTSIKGGTT
LPPTIITVTP NPHPTTVATK PDPEVNPKPP SWKSGSDPKP TAKPGCSGCG KPCILFCDSG
CPFCPPGIFH PGGGGGGDPN DPDDDDDDDD DDDPSQYTIY AESVLDDQFP DSPEDAGSLN
DLWNTEISRF ASEMGWLTTS STTTKPSSTA PPPPPPKPTP EATCEYFYGG VLYEFFIYYI
SGWDTDDLEG HLHDEENGCG ALTGWDWDYA HAKDPSVAFN LPLFIKDGCV ERAIVSAGGP
KISCSMYGGW GTPGPDDDDM DAAFAKAHQA NATQEHGPYR PMSWATLLAR ATGRRQK
//
