ID G2X445_VERDV Unreviewed; 1768 AA.
AC G2X445;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=VDAG_04782 {ECO:0000313|EMBL:EGY23344.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY23344.1};
RN [1] {ECO:0000313|EMBL:EGY23344.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY23344.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) 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}.
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DR EMBL; DS572702; EGY23344.1; -; Genomic_DNA.
DR RefSeq; XP_009652681.1; XM_009654386.1.
DR STRING; 498257.G2X445; -.
DR EnsemblFungi; EGY23344; EGY23344; VDAG_04782.
DR GeneID; 20706245; -.
DR KEGG; vda:VDAG_04782; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_001837_2_1_1; -.
DR InParanoid; G2X445; -.
DR OMA; YCCPEKE; -.
DR OrthoDB; 2582538at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_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:SF403; CHITINASE; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 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 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}.
FT DOMAIN 169..516
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 777..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1768 AA; 194861 MW; 25A4F81EE691214E CRC64;
MCGPVERQAD RQNTQNNDIF LPSSILFEVY VCCDLILGQE TAPRRHVGTI LACREDFAPV
DIGYDQYRGS YQSQSSCRRR TTSVRDLQKR HSVNLNAQGT ENTHPKLRLT APIGFWTFPP
KSVGTMSCRW GFCGMTEDFC EVKDNGATGG CQSNCKQPGP KRKGSNQLDR VIGYYEAWRY
NSECQGMPMK DIPINSLTHL YFSFAFITPN EYNIIGMDGL PSELFSEFTD LKKGNPSLKM
IIAIGGWTHN DPGPLQKVFS DMVSTKKNRS TFIENLMAFL RQYAFDGVDF DWEYPGADDR
GGVPDDGINF TQFLKELEAA NKKQPKRYIV SYTAPTSFWY LRHFDLKSIE YVDFINVMSY
EDNPIGSHIY GHTNLTEMSL AFDLFWRNDV SAGKLNMGLG FYGRAFQLAD PACNKPGCVF
KGGAKKGACS GESGILSYRE IMEVIKTKKL KPVHDKKAGV KYITWNTDQW VSYDDKETFK
QKKDLAKKLG LGGFLIWAID QDDDQLSALS AVLDPKPLGD FRSDKADDNW TGSNEKCYVS
KCGKGCSPGD IKITEQKCDK GKKSQLCCPL SGAPDPKDCT WRGGPNICNG RCHDDEVMTH
MSKWGGGADC WDGNAAHCCK SPLGEENSCY WGGVAKKCKA GHLPLTFSGT VLSILDDIAE
VILMVVGRAV PLAALTGRVL LEVLDQLDLD TNKLYCCPED DVDRWKNCAW YGKPGNCFDG
HCPDMKFVQL TDSYFGGGET CGGQLSRVRT FCCESAGDPL FLPVPLENLF EHPPDGDSVD
TDFSLKTDDS SAGGDDDPNE AAFQFVVLAS PDELQVSVDK RDGSHWDVFG CEDAVTEGEH
TVSMVCTDFS ERSNCHKIGL GHGVPGTILQ MPPGCGPGKY AVAKSMEPAD GEDHVKLLPR
RLAHLAPRKP TVYSLTFDYD FGRVPRDLGS TQMRIDFSNQ DDYWDTVVAG SVSKKKRDLT
KRTLADVGGN HVRWLEEEFR DDYHFGGLET RDLHERWFGT SILEWLSQLV KPEIKREFMH
RYDDTLTAKL IDETWSCSKG DISYEGHLLA QALLKIKVES SFGFTLIVND LSLPLDLSQS
YLTFYNKGAI TGVITLEAVA KVFYEKKSVI LNIPFPGASF KIPGIATIGP QLTVEGSIDA
SFAVAGTIET KLEIAKWEVR QVVPDNGDDA YKPKEIGKGD TSLDRTGDFG GIKKPEFYAG
VAVQGDVTAR LSAAAEFGVR FADRWDVDPA AAAVVGEASV MAKLTAGVST DAVCPFTYSL
DVGARLFARV QAPEVFGWPG GQYELTPKWN KGIIEAGTCP KLGAIPSKRD LDLVESAANL
STADNPSLQG DTKVGDHNKV ERRSGPLAKR GSVYGPVLSL PVGKFFCPPS SDDGENESSS
CQDVKAAWDR DKYLNEDYDG MRRRKREVPE DALLGVVDEQ DLDDVEGEIL AHLVGRSVSR
KPIKACSLKT TFSYPTDGSL DGDALVYGWE QPDVCGSYDW GGPLDARVAG TSYHSEHILE
AQMVVQFFAY MDEKMDSVAN PDPSASSNKK GISFCEYVNV MFDIDAVAAP GLDTARGFAA
TLTPINHIAA QFPTHQWKTE EYVSLGAVIN TPAKGKAWGA DDNIINTSSW LTDRLPTAAG
ARAMLKAMRS LVGSRVYHND GTVLGILRAQ KARVGAVLDL LDKTLLPANP PQGFTAWPQQ
GYGLRAEWDA FMKGEFLLMQ TKTMKVIYEF IGPLKEQWTG DAVRQANQDQ PGDSTTVLAT
KQGIRNLIDD IEAMDDYLAT MPPWQSAF
//
