ID A0A094HXS9_9PEZI Unreviewed; 1418 AA.
AC A0A094HXS9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=V500_05953 {ECO:0000313|EMBL:KFY89077.1};
OS Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY89077.1, ECO:0000313|Proteomes:UP000029284};
RN [1] {ECO:0000313|EMBL:KFY89077.1, ECO:0000313|Proteomes:UP000029284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY89077.1}.
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DR EMBL; JPKC01001955; KFY89077.1; -; Genomic_DNA.
DR STRING; 1420913.A0A094HXS9; -.
DR HOGENOM; CLU_001482_1_0_1; -.
DR Proteomes; UP000029284; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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 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; IPR001579; Glyco_hydro_18_chit_AS.
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; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
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:UP000029284};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1418
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001904003"
FT DOMAIN 291..336
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 355..403
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 476..845
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 1418 AA; 152481 MW; 754AE46ED440E65D CRC64;
MVSLRFAAKA APFLQLALAT PSDAGTFYSA ISNCPAPCAA GSQPSSWTTY DGPWHLGWCN
ETIMIDFSLH NPLNDPTTHH VIRACTTTTA PRAVSEIAAA GVETYPAKGE IQLISGGGGA
AIGTNASTSS DLVEKDDILA AIKHLQSYLG NDNTNATLAF AYSRTAAVGV YLGPGIEHRD
AAATLIQKLA DKAQSEAVGG KSLLQLCGTG RDADSVFGVV VDSVKNMASI QKIVKTWSEA
ECATGYEGTE TRTSVNVLMT APIIVAKNVS LPVQIARIGS RRALYARGDC RTTQVIAGSS
CASLATKCGI SGNDFTSYNS DPKLCSTLQV GQYVCCSAGT LPDRSPKPQP DGTCATYIVK
SGDYCSMIAA SNSISIANIE SFNKNTWGWT GCNNLLLGIS MCLSTGNAPM PAPMTNAICG
PQVPNTKKPA SGQKLADMNQ CLLNACCNIW GQCGTTKDFC TVSASESGAP GTSAPGKNGC
ISNCGTDIVN NGSPPSTFIN LAYFEAFNTD RWTLLIKVQA QFDKFTKMTT KSKKILSFGG
WSFSTNVDSY PIFRNTVTAA NRDTFATNVA KFVRDHGLDG VDFDWEYPGA PDIPGIPPGS
PYDGMNYVYF LNSMRDKLAD GKSLSIAAPA SYWYLKGFPI KAMSDLLDYI VFMTYDLHGQ
WDYSSKFANP ACDYGNCLRS HVNMTETYNA LAMITKAGVP ASKVVAGITS YGRSFQMTTA
GCTGPLCTFT GPESGASPGP CTNTAGYISM AEIKDILVRG DGGAKTWVDP VSQSNIMVYN
DLQWVSFMDD ENKASRIAFY KYINLGGTTD WAVDLQKYTD DTQCPKGSDD CFRLQFTSKS
RTGVDWRSLT CLDPWVIDAS QNQTDRWYGV GADVAWADAV NYWLQSPKPN PGGLTFSEMI
SNFLHQDEGM NCGSTADHNG CTGIFKCNEQ DPGPASYFVM GSITAVESGV LNLYDAIGRV
ESQITTQISD FVSDFAPVPS IDASLKIALD IVSLGFSLAV SPMWNSWLKT SAVFKANPNS
LGTIKDWVNP IVTNSITLIK DGMVAGAVLE RQNDIAKTLG KVVSAWYSTV DVFNQHLFDG
SQSSIDELTS MISDGKMVER PGTVSDLDIQ AYLERAIFSI LMPRAWELGG TVVFILDSGA
PCGAVNPSTN HFGTEHKGAN AWACADDKLY YIVGISEASR ACSGTPERPL QVCYPREFEV
DKLDGRVWGK ITREDIVVGA VNTYKANGNK NGGKPADPSN SQTLSDLYDY GVRAPGVMRL
AVCNADTAFH NWDNYLSDNI DIKPSSWPPY PWPCVSTEVS NPSPGYVGCY NVHKNPDWMK
FDVFTSGIEK VCGDLKGVSI NPGSDRSITV PGLKLEDGRD GVFVGAIKNT GQDPYEVDYD
YCIEKMGKIR DECHGKNSDT YGGEWHDVIW VVADTNGA
//
