ID A0A395S2Y8_9HYPO Unreviewed; 1326 AA.
AC A0A395S2Y8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=FLONG3_8813 {ECO:0000313|EMBL:RGP66617.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP66617.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP66617.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP66617.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:RGP66617.1}.
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DR EMBL; PXOG01000219; RGP66617.1; -; Genomic_DNA.
DR STRING; 694270.A0A395S2Y8; -.
DR Proteomes; UP000266234; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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; 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 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; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 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; 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.
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, 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 Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000266234};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1326
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017303244"
FT TRANSMEM 1208..1227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 338..387
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 406..454
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 467..540
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 552..929
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 123..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 495..507
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 500..514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 534..538
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1326 AA; 144124 MW; 0B399C7465204E53 CRC64;
MMLHTLIPFV GFLAGFSSAA TSGLNSTRLG PIDLTKVDNS TEHELDLGTT PLAPYGEKQT
SEEWATPLIN GCPRLCATTG PSGANWTHIH SVMDLQGCDA PLLFDMNVHS ETVETIRVCA
LGSSSSSNPP KAAAHLRQHK RHGAERREAK VAETDGKSSS SKCSPAPLSP VPIIVTSGMP
GVLNDTGDVT TALQGLKQHI NKKTSCGQTV LFSKAGSAIV GLYISADLGT VAGSAIFERF
ETVASQGVQI MQACDVNPMN PYTFGVFAVD KISDLELVRK NVATWIRGYC AAMPLTRPKD
AHIKVNVPGG DLFMASSNAT SVANSGLVTD LEARAECKTI KVDPDDNCTT LSVRCGIRGT
DFIKYNVGKM TNAAYCNGLK AGQLVCCSSG TLPDNKPKPD SEGTCATVEI DVGDTCWDLG
APYGLDEDDI AGFNKNSWGW AGCGNLQQGQ IICLSKGNTP MPAQIKDVAC GPQKLGTQKP
SGSFDGWDLT KLNQCPLKTC CSGWGYCGTT TEFCTESPAD TKAPGAFKKG TNGCISNCGT
SIVNNKSPPK EFKRIGYFQA YNPGRPCMNM DASEIEKNFK DLTHVHFAFA GITADYDVNI
PEDVKKQFEI FDKMDAPFKK VLSFGGWAES TDADTFQRYR DIVKPEFRSK FSANIVKFLE
KHKSFDGVDI DWEYPGAIDQ GIEPGDRNDG VYYTRFLSVL RNLLPPSKSL SIALPASFWY
LKPFPVDDMA KVLDYFVYMT YDLHGQWDYG NKYANPGCEN GNCLRSHVNR TETRDSLVMI
TKAGVPAEKV IVGIASYGRS FRMADKSCTG PHCLFTGSYT ESEAEPGQCT GTGGYISNAE
LDVIWQAASE GAEGYSAKRW HDTKTHSDIM TYGTQGNGMT DWVAYMSDET KKERVSWIKA
LNFGGTTDWA IDLAGVFEGP STKEGWSNGG WSDFKSDDIT CESADWPTSL KGLADNIDSV
HANCRAIALM KILIDDLIAA VAEYKEVSKG YDDKFGWYAD WVKDSIDDRI EEFLAPARGK
GLKYLDCEWQ SNRGSDKGRC DETWPPVAPG PGAGPRNVWY TLRDKDGFYK ALLDETGIEE
DWVEWVKMDA QPDPCSCIRP NICTPPGCQH GNNYEMRNNW LKRIKDKGKI HVSNPKKILD
EAIPSTDDLI TIAVATFMNM RLGRLDADPA DVVTSFSMPI FMMQDASESI KEIKKIGEDM
KDTKTKQLIM DILTIIFTVI PFAGAATSAL GGAAMIARAA LIVGEAGNIA LSIVEIVDNP
ASAPFAVLGI LIGASGLRGG MSPRKAFKEA ADARGALTPE KMKAFSQAFR DKDALVQNVI
KSCKFR
//
