ID A0A1Y2M8A4_EPING Unreviewed; 1794 AA.
AC A0A1Y2M8A4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=B5807_02580 {ECO:0000313|EMBL:OSS52335.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS52335.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS52335.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS52335.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(2017).
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}.
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DR EMBL; KZ107839; OSS52335.1; -; Genomic_DNA.
DR STRING; 105696.A0A1Y2M8A4; -.
DR InParanoid; A0A1Y2M8A4; -.
DR OMA; FDMNARW; -.
DR OrthoDB; 671410at2759; -.
DR Proteomes; UP000193240; 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 Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
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 PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF401; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW 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:UP000193240};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1794
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012417993"
FT DOMAIN 67..118
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 130..483
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 789..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1747..1794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1757..1794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 81..93
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 86..100
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 112..116
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1794 AA; 199213 MW; 2B3FF9C081EC2B79 CRC64;
MASHHSFTSF FVLLLCFSLI TFVTPQQGAT CDSETPCKSG CCSKLGNCGF GDEFCKPDVC
IGTCNATAEC GKWAETSGLE CPLNVCCSKW GFCGTTSEFC TPGDDSDDED GCQSNCDQPV
REHCTSNWEK RRIAYYESWA DNRTCDSFRP EDIPVHALTH INFAFGGIDD KHQVTVDAEG
VLVRVVKLKR RNPALQVMLA IGGWAFNDEG PTRSAFTNAA ATPDSRKAFA ESIVATLRKY
GLDGIDLDWE YPGADDRGGR PEDFDNYVYL LQTIKQHLEE ADPSYVLSIA IPASYWYLQH
FDLYNIQRYV DWFNIMTYDI YGKWDQYNEW TGPYVFGHSN TTSINAGLDL LRRNDVDLSK
VNLGMGFYGR SFTLDDPKCN EPGCVFSDAG EKGECSGEAG ILTFKEIMAR KNRFNGNTVK
YVKEHGVTYM VYDDNQWIGY DDKTSFEKKR EILSNDCLGG VMIWAIDQDT PDFQALSGLL
GDEFVQGALI EGGSMGEAER EALADELGGL TGDSCYVTMG CSGPGSNNKF ATCNKGDIAV
EKVHSPGGNP TNVYKTALLH EVETCPKGQW KTVCCPAKSP AINCKWVGAP ERSSIYCDGG
LEGKTCGTGR YELVTDRYLA STGGAICASG ARSLCCDSAP ELQECSWTDC QEEKKCPSGG
YLTFRGNKEG GQACPKGQTQ SFCCPIAGIY SDCSWAPVVE EITFDLENGV EMIKSSTMQQ
CMNTACSKDQ ITIAKATLPE RTSGYPAPCG YYNPGLQHRF CCNPPRDVDL PFDLKKIFPD
PKGADVAYQY KDNYGNNNKD PHGPDEDDVG DDPYGFIVLD GDQEALQSKF ASNFVFVHED
DGTGKPLKKR TTLTREDPDI LTWTFEHEES SHFVYCRPNR EDLCDKVFHG SAKDTIISIP
RHIGSGPFAR VISMEPVPDS LLTDHHLRKR ASEKHSSTVY ELKFDYDFAA IKREDSTVNI
RIDYTNLVPY WDEMTGEESS KGTSKRSLDK RWWGSYVDWL KKLNTVRASD EGKLPMSIHK
KMTLYRKRAS CARGNTRVKA GLDVILDSKI DMNARWAYYA QGTIVPLKVD EVYTYFEMEP
VVEAVLEVSG NAEIEYRMKE PIKIIDTLAY PGLAIKGIAA IGPTLDLFGE MRAKATIAGQ
IRAGAKITFP RYETYFPQVP EAKDYQKFPK PSTEQEQASK GTDFTPILDA SVQASVGVDI
LLTPMVNLGI KVNHPSVKGD IVSAQIQGFV NNTFRFEVST KADAGIGTNP AASYNIFIKY
IYNFGIGGAA TFKWLGDYAL SPLQLWPGEG RQKILYEHHG EVALGKRNPF ISDGEYSEKF
EPIYNSTYDF FDDVSEGVDL SGGVLRRFSK RAEGDEKTPL DEDSTSLFTC NDEGTCKEGG
CNGDACQWTP GKTSKKRQDS DDDDDDDPMD VDPVTPCPNS IPAFMYNCRY FPDHTSDGFE
FLGICHNILN YFRDHQGGGS GPFFGTFHHN RASEGGNRAN VCGDRSRTTY NDGDGNDVTT
TWSERCIAES DFYAISTSRR EGDPGNTNWL SCDEFPFNSL EEGGNPNRNA RACVPGYQQD
IQGNANQLLN IIRQQVTWID ASGNERTSTQ PKAWSADWRG SSATGRQTNP NKDTAWNWAL
NNNKEFTMHL FDSDSLLDAE GHSYSIFEHD IKDAPSQGDA PANLQTDITR VVSAVNFMGN
SKYSARYNAY CTTGQTRPHA LWGPFIRISQ CNVIFDNAAA QRKLKRGEQP TQEEMFNVQS
IEILEDGESV DIPTGSTSKG DKEENNKTER TFGSRDHQRH FKDHMAGLSK HHGS
//
