ID A0A1B8FGY7_9PEZI Unreviewed; 1324 AA.
AC A0A1B8FGY7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=VE02_08437 {ECO:0000313|EMBL:OBT82848.1};
OS Pseudogymnoascus sp. 03VT05.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT82848.1};
RN [1] {ECO:0000313|EMBL:OBT82848.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03VT05 {ECO:0000313|EMBL:OBT82848.1};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; KV459548; OBT82848.1; -; Genomic_DNA.
DR Proteomes; UP000091872; 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; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1324
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008607687"
FT DOMAIN 282..327
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 346..394
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 489..876
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 1324 AA; 143266 MW; 1D2F5490B9899E04 CRC64;
MVSLHATSRG AATLLALITL VEGTAFYSAV DRCPELCIAG ADSNSWTVYD GVKHLPWCNQ
TMLVDFAIYN PLNDTDSHSS IYACTTKDIP QALSKVAKTT AKSYQAKGEV QLITTDASDV
DIMKEDALGA IEHLQDYLSN NDSGKPVAFG YSRTAAVGVY LGTGIQTHDA ASTLLQKILD
QVQSQTVITK SLLQLCGSDR DSNSVFGVVI DSVSNLASIQ DAVRSWSDAE CATGYEGKET
RTNVNVLMKE PIHTAISNGI LSTIKEAHAN TQRGLEARGD CRAIQVQSGQ YCPTLATACG
ISGAEFTKYN PAKDFCAKLQ PGQWVCCSSG TVPDKSPKPK ADGSCFSYVV QADDNCSKLA
AANGITAAQI KDFNKNTWGF TGCDPLNKGV NMCLSKGDPP MPAPMSNAIC GPQKPDTKKP
TDGTKLADVN PCPLNACCNI WGQCGTTSDF CTILKSASGA PGTSAPGKNG CISHCGTDIV
NNGGAPASFI SLAYFEAWNR EGRSCLRMDV SQINSGGKET YSHIHFAFAT ITTDWKVDLT
KVQAQFDKFK KMTTKAKKIL SFGGWSFSTD ADSYPIFRNV VTKENRQAFA NNVVSFIKDN
NLDGVDFDWE YPGADIKGIP PGSKDDGKNY LEFLHMVRDA LPSGKTLSIA APASYWYLKG
FPIKEMAPVL DYIVYMTYDL HGQWDYGSKW SNPDCANGNC LRSHVNLTET LNSLSMITKA
GVPAAKIVTG VASYGRSFKM TKAGCTGIEC TFVGPESAAE KGPCTDTAGY ISHAEITSIV
AKGGSLNARD GGVKMWFDEE SHSNMLVYND VQWVAYMDPK TKADRTDKYK KLNLGGTTDW
AVDLQTYQSP EECPKTDADC YKNQYQNPSK DGVNWRKLTC ENEWVKNAMR NQTDRWFGLG
ADAAWKDATD SWKAAPHQGG FNFSQAISFF FNGDEGMNCA VMADSNKCHG AYHCDDFKDT
GAAAYFIMNS ITSIEGALLN FYNAIYHMEV TVNTAISDFI DDFAPMDSDP DWLKITIDLV
SMGFALAAAP TWNSWLKNTP YFLKQNGNTL GTMKDSVNGM VSNSMTLIKD GQVAGAALAT
QDTLLSTLSQ ATQAWASTVD ALNKKLFDGS DSSIKMLGDM MADGALLENP SVLSDQDILV
YLERALFSRL IPSAWQLSSQ KPFILDAGVP CGTVDPTIEY LEKDVADKTW ACAGNKLYYL
VVLKGNAATC TTGREGFCKH NYYSAPAGID KLDGKLWGGV KLEDFVVGGV NGYHSNGDKN
GWKSADPSDT KMASTLYDLG IRSPGVVGIP VCDTKTALQN WIDAERFGSH ENYPCVPLDV
VVPP
//
