ID X0M926_FUSOX Unreviewed; 1334 AA.
AC X0M926;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=FOTG_05063 {ECO:0000313|EMBL:EXM30032.1};
OS Fusarium oxysporum f. sp. vasinfectum 25433.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089449 {ECO:0000313|EMBL:EXM30032.1};
RN [1] {ECO:0000313|EMBL:EXM30032.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25433 {ECO:0000313|EMBL:EXM30032.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum Cotton.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXM30032.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=25433 {ECO:0000313|EMBL:EXM30032.1};
RG The Broad Institute Genomics 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.;
RT "The Genome Annotation of Fusarium oxysporum Cotton.";
RL Submitted (MAY-2012) 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; JH657925; EXM30032.1; -; Genomic_DNA.
DR HOGENOM; CLU_001482_1_0_1; -.
DR Proteomes; UP000030701; Unassembled WGS sequence.
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; 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; 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; 2.
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; 2.
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; 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}; 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 Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1334
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004944689"
FT DOMAIN 282..328
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 347..395
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 408..476
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 488..853
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 433..445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 438..452
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 470..474
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1334 AA; 145833 MW; 38A3F35B6E408952 CRC64;
MRLAIVRAAV LLPTLFSLTH VAAIGSSNPQ LYVCPPLITE AGVDSSNWTL LSSLDEVFAC
NHKPRLLDFT VHYPLRPSGP GNVLRACTSY QGELLNLTST GNSSSLAKGG KTASKFELLW
DDADAAVITP QAITALKELQ SFFLTEDTGD KRSAFAQYGD TSVGLYIGGR IVSVSLAKVV
IEAVVNRLWT SSMPRRLVVQ LCGDSHNADS TAGIILDTTP GPASLINVQA VVSGWSNATC
VEGLQQSKSF GYFPIEMIPE SPKPSNKSNS TASNLAKRAD CRTIQVKSGD TCGALAERCG
IKAADFTKYN SQTKNLCSTL IDGQHVCCSS GDLPDFRPQP KPDGGCATYT VESGDFCSKI
AAANSIKVED IENFNKNTWG WSGCKLLFDK AVICLSKGDP PMPNPIANAE CGPQKPGTKK
PEKGKDLSDL NPCPLNACCN IWGQCGVTAD FCKNTTLGPP GTAKPGTNGC ISNCGTDIVN
NKSPPSSFMS VGYFEAWNQD RPCLWMDVSE LEKRTELTHV HFSFARLTES FEVDVSHVSY
QFNKFKKLKG PKRILAFGGW VDSTHPTKYH ILRNAVKMEN RLQVAKNIAA FIKKHDLDGV
DIDWEYPGAP DIPDIPKADE EDGKNYLGLL TLLKGQLGGL SLSIAAPASF WYLKPYPINN
IAKVVDYIIY MTYDLHGQWD YDNKWASPGC PKGNCLRSHV NLTETMGALA MITKAGVPST
KVIVGITSYG RSFKMAKKGC AGPMCTFLGS STESLARKGV CTGESGYISN AEIDNIANKQ
ASWWIDESDS DILVYNDTEW VAYMSDSTKK RRISKYQGLN FGGVTDWAVD LQKFGKLEDS
TLIEIIDKDG KCKWKTKDGF TCLDKAVTDS LQPAVNRWNG IRTPCAWREV ALGWIDERTS
KALNTSDREN ANDFSRYVSD VLDAKESFHC ASFTAGANGC EPLEKCEATR DAGPAAYFIV
NSFANIHSNL KSLWETVDRV ENGMQSRLDE LVETFAPDVD ESSNFNLIAD LLGIVVGMFT
APFFNKVLRA NNNPTSDPTP DIKDLVANSA SWGATLAKDI QNSKRETPKS KVAGKLSQIA
DMWDSAITIF TEQIFRGDDS SVEYIGDLIA EGKFNNKKPL LMEDLRKQLR KVFFAILIPE
AWKVGAGFAP AFVMDSGYDC NAVGPLNYDY IAPSTAEEMG YCYDGRRYYL LAPNGPATKD
GFPNPPGGSS ERPNNYFTAP QGIEKLEKNE EGENDWGGIT AQDFVAGSVA VEGWKANKKE
NGGGFLDLTK ASNYDFLLDE DAEEVNIRAP GFIQIPVCKP EAARAMWRWF DSLSASQKPT
VFETLKYYPC LNEN
//
