ID W7N7U7_GIBM7 Unreviewed; 1262 AA.
AC W7N7U7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=FVEG_17600 {ECO:0000313|EMBL:EWG55819.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG55819.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG55819.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7600 {ECO:0000313|EMBL:EWG55819.1}, and M3125 / FGSC 7600
RC {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [2] {ECO:0000313|EMBL:EWG55819.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=7600 {ECO:0000313|EMBL:EWG55819.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2013) 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 -!- 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}.
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DR EMBL; DS022265; EWG55818.1; -; Genomic_DNA.
DR EMBL; DS022265; EWG55819.1; -; Genomic_DNA.
DR RefSeq; XP_018762009.1; XM_018906838.1.
DR RefSeq; XP_018762010.1; XM_018906839.1.
DR AlphaFoldDB; W7N7U7; -.
DR STRING; 334819.W7N7U7; -.
DR GeneID; 30074476; -.
DR KEGG; fvr:FVEG_17600; -.
DR VEuPathDB; FungiDB:FVEG_17600; -.
DR eggNOG; KOG2806; Eukaryota.
DR OrthoDB; 2582538at2759; -.
DR Proteomes; UP000009096; Chromosome 10.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; cd06922; ChtBD1_GH18_1; 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:SF333; 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:UP000009096};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1262
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010156259"
FT DOMAIN 62..110
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 115..471
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 79..91
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 84..98
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1262 AA; 141364 MW; 202881B31BAB6B48 CRC64;
MRMRTWLFGL LLLCLCLAVA AQDDTTCSAT KRCKNGCCNK SGNCGFGPDY CGTNCQSDCD
RKSECNPGFG SKWAENDKCP LNVCCSKHGY CGTTKDFCGS KKVKKPSCSK TGDVSRVIGY
FEGWAKARPC EAFSPEQIPI GLYTHINFAF ATIDPKTFEI KPDKESDIRM YKRLTDLKRR
DPELKVYIAV GGWTFNDPGP TASTFSDLAA SLPRQRAFMK SLVSFMSTYG FDGLDLDWEY
PVDTDRGGRA VDFANFPKFM ERLKSMMDAA DKGLSITLPA SYWYLRQFDI KKLEKTVDFF
NIMSYDLHGA WDQGKNYTQP FLNAHSNLTE IDLALDLLWR NNIQSDKVVL GMGFYGRAFS
VQTGTCTKPG CLFKAAGKAG DCSREKGILL NSEIVTTIKK YNIKPEFYKE EAVKVAKWGN
QWVSYDDEDT FKLKTDYAKS RCLGGVMVWA ISHDTKEARF NKALALSLNR KTTSGEFDEN
EKAYDIKKIP NEQCRWTNCK EGCRKGWVAV PRSDSGARKN EIMFDETGCG GDGGHTFCCP
AGDTKIPTCG WYGHNNGRCP TRSECPSDMT EIASNEIYCK KKGSKKQNFQ TACCKTDVVG
TKVYGTCEWG QYPKCDAQEG CPNPLGNKKM GSLLAYSASG SGGGNCDDAK NELGLNVPGV
QYRKFCCNDS DKNLRFTDCQ KFRNVGPEPE VMPRGFCRSG CPPDRIQVAI DTQVDTCAIA
GVGGMAHCCK TDYAEIFEVE NPKIDAFEND VKAWIKNPTC PKDDGGLFKR FDPTNDLAIN
SSISMNLSPR AKEMEDSYDV VILLARLIAG MISKEVAEAL TPKWNLVVEE EYPNLVVETL
QKAKKEVPEW EDEDAEVMSR VTICDPKRAN ARIAAILGKG SDGRTLAFNC TNTICQNGVC
EPGTPEAARR RRGLSMSRAS HSVAHLHYHL HARQAGAEHN EVPMRDRGGD QGLIEYEVPA
HDEPKKLVLR NPDAQVVDFA NEADCHETRL WYTTWSVSLE GLGFQTEHLI DKVILKRFFS
DAGFAVLRSG AQSQYHGIPV RFFEEALRLG RLRGRFPHIS GRDDAFDDQN LLTRVFECLG
SRDNFRNFVI VVGPINAIKG RVMKLNAPIQ LSELDTYDTD GLMSHIRTVI TVFEYMGSEE
RDENGKTVED KINNIVKNIV KQLVYAQDLW DEEHPGRPVP AARFFVEWLQ DYFEEAGTRA
RAWIQRAITI LRNRQRQASG ARAEEIRLAI ASFESQLSTV RIGTEWDIDW RDDDDEMDTS
SG
//
