ID A0A1V6S3X9_9EURO Unreviewed; 1787 AA.
AC A0A1V6S3X9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=PENVUL_c008G06460 {ECO:0000313|EMBL:OQE08755.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE08755.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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 -!- 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:OQE08755.1}.
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DR EMBL; MDYP01000008; OQE08755.1; -; Genomic_DNA.
DR STRING; 29845.A0A1V6S3X9; -.
DR OrthoDB; 50378at2759; -.
DR Proteomes; UP000191518; 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: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; 3.30.60.10; 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:SF401; CHITINASE; 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 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:UP000191518}.
FT DOMAIN 19..64
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 80..432
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 1579..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1748..1772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 33..45
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 38..52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1787 AA; 200822 MW; 568EB5F307E91098 CRC64;
MHQGWLLQQR RCQGSCNATA ECGKYAAKDN FACPLDVCCS EFGYCGTTDE FCNDDCQNKG
GCPAVDRPQC SESTDAMSLD VRVGYYSMSG AERDCDTSLP ENIAAGALTH INLAFAGISE
DFEITDENGP IVARTSRLKK KHPGLRVSIA IGGWVFNDPP TQNRFSDMVS TRPNRERFIA
SLIRYIRRYS LNGVDIDWEY PVAADRGGTD LDKQNFVLLC SDIRDAFERE DSGLQLTVTL
PSSYWYLRGF DLKRLEKYID WFNVMTYDIH GIWDQKSVWT GPYLKGHTNL TEIEDGLDLL
WRADISPEKV VMGFGFYGRS FTMSDLKCYK PPSCKFDSAG FAGECTNEAG ILSYSEVMSR
KSQLGATVFY DEKSSVKYMT YGSNQWISFD DEESFEAKKK YLFSRCLRGL MVWSLDLDTQ
DHQAMTGLFG EKAMEGALTK SGLDSEEAEQ LSFDLSAWTG ERCYSTPTCT DGSKTERTAD
QVCKGGYTAL EMAHSPVQKN ADFTMNGDCD EGWWRYICCP TKALPQNCDW HGAPERSAFG
CDRGCGPSQF ELNIDMYLDA KGEGDCFSGA RSLCCDNTEI LDKCHWSDCD YRPDKSSCGD
DEESIAIRFD KNDGGSCGTT SFRPPGERTV RREFCCPKKD KFEKCSWSID DCKPGKCAKD
KLQVTTAQDP SWLYDISRYT SDECFGYHIP KMASSDFPLC CEPPSTYSEK WPVEPKYLWS
HYYDADDDDI SWQFSDNFGN NNKDTTPGDM DDDPGTDPYG FVMLDGPPGS INNAFGSQYT
VVTRDAPTNI KKRSIVTTNQ TSLDSVFEHA EETVLVYCNY PADSKECRQI FHNRAEDTII
RLPDHVGEGP WARVVSMEPV ESPSMHMPGW IIRKRSDTDN QNGVYALKFD YDFHAIKRDD
EQVNIRVDYT NLIPYWDEMT DSPATKRKRG TEESFTYEEW RNKVDRAKVL DTKRSSRNET
GKLTVRSNNT VQPRATLHRR WWGVFTEWVK KLTTVTKTDG GLLPMGLVRS LVLYSGRLRC
TNEEVTITAG LDITADFNME MNARYSYYFS GTVVPPTVTD MYAYVGVHPQ VYAGVGISGN
AQLYYPSERK KIIDTLTYPG LAIKGIAAVG PTMDLWGQID GRVTVSGDMQ VGLTYQFNPV
ELYFPNNDEA RNTLDVEDMQ SSQVDNSGLA PQISGNVRAD VDINIHATPE INMGIKIGGG
IGSLKGTLAD AHVSAFANTT LNFHAQAKAG TNNGDNSWSY GYSVSFLYRF GFGCVAEIYK
YGKWTSGIWY PFKQRVIPIY SKTFSASQSE KRSLEGPFFS EQPLSGAIFG LSSGLSAAYH
FDDTETDGYQ QYGNISLTRR ADGTMSDKET QFNLGSFKCT TGAGSVCDST LSENSLSQRG
LMPLSRDSAE IQKRAKKPTD CPSKIPRFYY NCVAFFHDMT FSDGGGRADM EGICSNIEKF
LTNNARGNSG ITLTWESQRQ AQRRKKSCPS KYCEPENEKI RQSLYGLGST DKTEFTNCDE
FPFASSEEGG VDFLGLAPDT PTGTVRTCVP KWQNDVQGQC NNLLNNIRTN VEYFNTVGKP
TEENPSWWRW NQHSSWGSKS GLGKRQRLVP YPDPQPKSYV GAMTKDDYDD PRNLNFYHKR
KFELFLSYPH AGQNPDGQYP DQDYDKGTMN IPSDKKKLQP VISDVPSPNV ICAVNTMGQH
RYGWAGANAL CTDGVSRDVK MWGGKYPSIH AFHCRVSFVG SPYTIKRDGT PQEPLGYFGD
DPYYSVERVD DTGYNYDEPE SDNDMSDDED RDFVNFYDID SDAEEFY
//