ID A0A0G4KDL5_9PEZI Unreviewed; 3378 AA.
AC A0A0G4KDL5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE Flags: Fragment;
GN ORFNames=BN1708_001995 {ECO:0000313|EMBL:CRJ81851.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRJ81851.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRJ81851.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRJ81851.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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; CVQH01000002; CRJ81851.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4KDL5; -.
DR OrthoDB; 2582538at2759; -.
DR Proteomes; UP000044602; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00035; ChtBD1; 1.
DR CDD; cd00306; Peptidases_S8_S53; 2.
DR Gene3D; 3.10.50.10; -; 2.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 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; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF333; CHITINASE; 1.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR Pfam; PF00082; Peptidase_S8; 2.
DR SMART; SM00270; ChtBD1; 3.
DR SMART; SM00636; Glyco_18; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF54556; Chitinase insertion domain; 2.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 2.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 3.
DR PROSITE; PS51910; GH18_2; 2.
PE 3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 112..150
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 172..526
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 1719..1757
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 1758..1812
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 1827..2199
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 680..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2367..2396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2655..2685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3232..3259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1587
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3243..3259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 120..132
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 125..139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 144..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 1727..1739
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 1732..1746
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 1751..1755
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 1772..1784
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 1777..1791
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CRJ81851.1"
SQ SEQUENCE 3378 AA; 363399 MW; 43EC3018A6B72BE2 CRC64;
RFSAGVQAAM RSQSSTSLTV FAVVGIILLC LPALIFADVA YQPRAGRTIA QRDSDNTDLS
WRDQIVFSPA HQDPAKAPAV PIAALENSTT ASIPAVSVFN PRGLNTFQKR QALRCDDGPC
IDGSCCSKEK ICGYGPSYCG AGNCTSQCDA TAMCGEYSEN AEMPCGSGSS SKRKVGYYQS
WNVRDRRCNK VSPSQLDTTG YTHLFYSFAF IDPKTFRITP AHSDDDSMMR EFTKLSKDGK
LQTWIATGGF DFSNPEVATH TTWSDMVSTK ANRAAFIASV KEYMDTYGFQ GVDLDWEYPG
APERGGRKLA DVRNFPMLLR EMRAAYGSSY GISLTLAPDY WYLRWFDAKA MEPSVDFFGF
MAYDLHGSWD ADVLALGKKV RGQADIREIA NNTIPLWFDG LDPKKINFGL AMYGRGYTLA
DPKCNQLLCP FSGPSKPAPC TAFGGVMSLV EIKQLIKERG ITPQYLADSM MKQITWDDQW
IGYDDEETFA AKQAFADGMC FGGTMVWSID FQVPGSGGHD QNENTVYLDP KVYEGTPAQC
SAPCVFVLPP SALPSATTIQ IPPYSTSLSV APGITSNIVI RPPPIVTSSL QFSNVDVTQG
QTTGNVHPTV SLDLPPFVTT ITGPGGVQTR TLLLPPWPQI TNGPPESWTT SGNPWTNPGV
TGVPAPTDVI PLPPPEMITK TPYTGPGGSV DPTGTWPTSF DIQPVSTSVP DDGEDDDDDG
PKSKSTCNLW FFWTCIDIGG IKIGGWEWNL PQGIWGPGPP PIGRINPPPG FTFKGNLPNW
PKITVGPGGK VTAPPKPASC TPAEASLCAT TTSFGTTVQN GVTKTTTTQV KETCATITGC
NLRDVDSTET GRACSLAKRT INLTGVPLPE MTAAAEPPPD IAKRANSIWD CEETGEDGII
WPQDPKEGGQ TRIRALLQER KDALGGTHSW TEVRAGDLDY TAFYYVDNMG PVAQAYFDSD
EVKEINRAYN YRADIAPRLS RAQLRRSKAK RSAKASDSRT DAPVRVETLA SDGVEKLNEA
ADSLNNETPD IGKRATSPEI SDRWHLSHIS IPERVDWDVD DDPHIPSQNK FAYYFNNREG
SGQTVYIMEE RTGQSGEFTG QLKAPLSPHS YLSSMWYDDD PDDVTEMRRH GTVISAMVGG
VASAIARQAS LVVVPTKLEV EEDWPLEIFL ASLVAISQDI VKEKKPQDTT IVNMSFGIPM
KYAEPHFWTI MRQLMVLMEA KYGTVFVAAS GNAEPDPADG PLVDPGVFID ANSMPYEAMP
YVPGMMVVGA SNREGYRRKL SMVGKNVEFW APGEQLPYPL GVSNRRQING GSPAAGLVSG
LVASLRSDPT FSNFVKPAQL KQQMKSLARA ISYQGVTNAD KPVVVYNGQR SDQSCPPNSN
AGAVSERRLT IRQVESCPLP GQPGNPEGVP VPSLTYRPGP PGPLCTANCG RLCEGFFCVP
QPTGTPPEFT PPSNPGATGP GWVPPPPVTL PNLPTLPPSE PGVTPGPGTV CLSSATVTQC
NGRPGQAVCV TSTSCASFGT LGPFPTLPPS VTSPPGGICV STATWVITGG PKGEATVTTS
GCGKWTVPSA PEPTPNPPSP PPPPERNHGV VRSKGGWPVF IASAALPENI PHPDPPHHSP
VRCLPKLHSA PSSHLIWRSA LIFADVAYQP RAGHTIAQRD SGNTDLSWRD QIVFSPAHQD
PAKAPAVPIT ALENSTTASI PAVSVFNPRG LNTFQKRQAL RCDDGPCIDG SCCSKEKICG
YGPSYCGAGN CTSQCDATAM CGEYSENAEM PCGMKLCCSA MGWCGTRDIY CHNADPVQNT
LPCQAGYGSC SITPSPSCAQ GSGSSSKRKV GYYQSWNVRD RRCNKVSPSQ LDTTGYTHLF
YSFAFIDPKT FRITPAHSDD DSMMREFTKL SQDGKLQTWI AIGGFDFSNP EVATHTTWSD
MVSTKANRAA FIASVKEYMD TYGFQGVDLD WEYPGAPERG GRKLADVRNF PMLLREMRAA
YGSSYGISLT LAPDYWYLRW FDAKAMEPSV DFFGFMAYDL FMNDGVIRLS GVFRFADLHG
SWDADVLALG KKVRGQADIR EIANNTIPLW FDGLDPKKIN FGLAMYGRGY TLADPKCNQL
LCPFSGPSKP APCTAFGGVM SLVEIKQLIK ERGITPQYLA DSMMKQITWD DQWIGYDDEE
TFAAKQAFAD GMCFGGTMVW SIDFQVPGSG GHDQNENTVY LDPKVYEGTP AQCSAPCVFV
LPPSALPSAT TIQIPPYSTS LSVAPGITSN IVIRPPPIVT NSLQFSNVDV TQGQTNGNVH
PTISLDLPPF VTTITGPGGV QTRTLLLPPW PQITNGPPES WTTSGNPWTN PGFTGVPVPT
DVIPLPPPEI ITKTPYTGPG GSVDPTGTWP TSFDIQPVTT AVPDEGEDDD GDGPKSKSTC
NLWFFWTCID IGGIKIGGWE WNLPQGIWGP GPPPIGRINP PPGFTFKGNL PNWPKITVGP
GGKVTAPPKP ASCTPAEASL CATTTSFGTT VQNGVTRTTT TQVKETCATI TGCNLRDVDS
TETGKACSLA KRTINLTGVP LPEMTAAAEP PPDIAKRANS IWDCEETGED GIVWPQDPKE
GGQIRIRALL QERKDALGAT HGWTEVRAGD LDYTAFYYVD NMGPVAQAYF DSDEVKEIKR
AYNYRADIAP RLSKAQLRRS RAKRSAKASN GHPDTPVRDE TPASDGVEKL NEAAELLKNE
TSDIAKRATS PEISDRWHLS HISIPERVDW NVDDDPHIPS QNKFAYYFNN REGSGQTVYI
MEERTGQSGE FTGQLKAPLS PHGYLSSMWY DDDPNDVTEM RRHGTVVSAM VGGVASGIAR
QASLVVVPTK LEVEEDWPVE IFLASLVAIS QDIVKEKKPQ DTTIVNMSFG IPMRYAEPHL
WTIMRQLMVL MEAKYGTVFV AASGNAEPDP ADGPLVDPGV FIDANSMPYE AMPYVPGMMV
VGASNREGYR RKLSMVGTNV EFWAPGERLP YPLGVSNQRQ INGGSPAAGL VSGLVASLRS
DPTFSNFVKP AQLKQQMKSL ARAISYQGVT NADKPVVVYN GQRRDQSCLP NSNAAAVSER
RLSIRQVESC PLPGQPGNPE GVPVPSLTYK PGPPGPLCTA NCGRLCEGFF CVPQPTGTPP
EFTPPSNPGA TGPGWVPPPP VTLPNLPTLP PSEPGVTPGP GTVCLSSATV TQCNGRPGQA
VCVTSTSCAS FGTLGPFPTL PPSVTSPPGG ICVSTATWVI TGGPKGEATV TTSGCGKWTV
PSAPEPTPNP PSPPPPPERN HGVVVISYYE FGQFTVGGTF WTREHRAFSV PFGGQIKQCS
ASAIASQSAP GVLASAKLPT KMGPFQAEGR TCEYSGSPDS PGQLSCNGLP TVSCEGASQT
DICGSGTPIM KALAFCRF
//
