ID A0A0A2KU70_PENIT Unreviewed; 1444 AA.
AC A0A0A2KU70;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=PITC_014660 {ECO:0000313|EMBL:KGO70456.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO70456.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO70456.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO70456.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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:KGO70456.1}.
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DR EMBL; JQGA01001043; KGO70456.1; -; Genomic_DNA.
DR STRING; 40296.A0A0A2KU70; -.
DR HOGENOM; CLU_001482_1_0_1; -.
DR OMA; RERNCDP; -.
DR OrthoDB; 11640at2759; -.
DR PhylomeDB; A0A0A2KU70; -.
DR Proteomes; UP000030104; 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: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; IPR001002; Chitin-bd_1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR029226; Ecp2.
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:SF1; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF14856; Hce2; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00270; ChtBD1; 1.
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; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 1.
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, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
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:UP000030104}.
FT DOMAIN 224..269
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 349..417
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 428..830
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 1199..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 374..386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 379..393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 411..415
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1444 AA; 158569 MW; 5D94B7163F3B7367 CRC64;
MKQLDRCNLP LFYGFNMYDD VDDTDTYHRI LACTAYGNDW RENPEARLQP SHPVKEHKVN
YEIGWSSYSE GTESKYRSLI RQMRDYIARG HLTPSKTAML YSRFGATSAG IYIGNSLQSK
DIADVALDSV DHTMTLNTSG FLALRNGTFR AIQSAFESWS NAECLDFEKS TNFTASTHFT
SPMLSSIKAG NTTTSSMEAS GLPLPAKSST QQERNLLFSR AECKTEKVQK GDSCAAIAKR
CGISGADFTK YNSAKSFCSK LKPGQHVCCS PGTLPDFSPK PNKDGSCATT IVGDGESCST
IGAANGLTEK DIDGFNQKTW GWTGCKNIFK DSVICISKGS PPMPAEVSDA ECGPQVPGTT
PPKDMSKLAD INPCPLNACC NTFGHCGTTA DFCTDTNTGA PGTAKAGTNG CISHCGMDIV
KGNAPSEFRS IGYYESYQFK RDCLYQDVTQ VDHSKYTHLH FGFGDISSDY KISIDDKLAN
YQFNNFKHIS GPKRIISFGG WDFSTQESTY QILRQGTSAA NRKKLATNIA KFVNDNNLDG
VDIDWEYPSA PDIPGTPPGD KSEGANYLAF LVLLKNLLKD KSVSIAAPGS YWYLKGFPIA
GISKVVDYIV FMTYDLHGQW DAGNPDAQPG CDDGSCLRSH VNLTETLQSL SLITKAGVDS
GKVIVGVSSY GRSFKMADAD CDGPLCKFTG DRLGSNADKA DCTGTAGYIS NAEINQLLKS
NSSLVNREYV DAHSNSNISN AEIDQLLKRD SSRVNKHFVD DHSNSNIMVY DDTNWVAYMS
PEIRAQRAKM YESLSMGGTV NWATDLEQFN DPPEGFDDWR DLILHAESGI TTPRGAGNRR
GNWTKFDCDN EYYRENPYWS PTTRWEKLGA ADAWRDVIAD WKDYRGKSGK DISDQFSSQI
LYFLGNSDGA KCHRIEDDSN CVQTRSCSEF EVEKNYKTGA AAVLIWNSLV AIHQMYAEFR
SALVANAALV IDNTLPDLEK TFAPVPPKKS DAWLNALLGL ISLGVPLVGG KFFDDVLAGI
PAMAAKTSTS RDHIKSVMNA ILTSPVTLAV NLKGSPAVDD WTPEKQAEFS KYMGQSLKAW
EYIFKKDLEN LFDGSDKSIE RLTTMIADGR LLDGIAEDIP YPNKTKRKEK GTEATDAQKK
LVEDGFLTTF WAYSIPAVWQ ASGHHPFIID AGRSCDDKHG DKDFKSACYE NRLYKLADPD
GKSHDCPDNG GSPAGSECPD TPFSSPKGVQ ELDGKAWNGL KAEDIIIGSV KTYKQNGNEN
GGGKANPKDS GTFEALKRMD ITTPGFMRLP VCSETLARKS WENADKTEII RDREGFPCNN
DNGKAYCTTS KTTYIEETTS DSPLIDDCLV IVKNIQGTSG SWDKPIERQF GILNFGTCTF
GIEGKGRKGN IDVYIGAQDA VDIIRYTSKH WGHGTGKMQG KGVMQCDGNI KKQEVHWAIY
KKQG
//
