ID A0A428NKH1_9HYPO Unreviewed; 901 AA.
AC A0A428NKH1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=CEP53_012848 {ECO:0000313|EMBL:RSL41295.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL41295.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL41295.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL41295.1,
RC ECO:0000313|Proteomes:UP000287544};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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}.
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:RSL41295.1}.
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DR EMBL; NKCJ01000466; RSL41295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428NKH1; -.
DR STRING; 1325737.A0A428NKH1; -.
DR Proteomes; UP000287544; 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 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:UP000287544};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 57..110
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 112..470
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 75..87
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 80..94
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 901 AA; 98593 MW; CDB6001CD5CEE997 CRC64;
MQLSAARQDF VQLVVAVVQV TAVLPRIIVE KDVRHGHCGL GPDFCSKDNC VAGCEAKGEC
DPGGFGANFA NHTKCPLNVC CSKHGYCGTT KEFCGKNTVN RPSCSSKSSP MRRVVGYIEG
WASTRPCGSF KPSDIPDGIY THINFAFASI DPKTFQIVPA SRNDPALYRE LTLKKKIDPN
LKVFIAIGGW AFNDPGPTVT TFSDIARSEA NQRTFIKSLI SFMATYGFDG VDIDWEYPAA
DDREGREEDY DNLPKFLSNI KGALKQSGER NGLSIAIPAS YWYLQHFDLA KISKYVDYFN
VMTYDFHGSW GTPKSWLGNH LNSHTNLTEI KDAFDLLWRN KIDPDQVNMG LAFYARTFSV
SNPSCMSPGC LFDAGGPAES CTDAVGVMSN REIMRKSGGK IGQGELDKTA AVKILKLGRT
WLTYDDVDTW KLKLDFARSQ CLGGAMVWAI SQDTSEGKFS KQLQQATGYK SRAVTTFNSS
VALGGGVFKE TTENEANGDV GNAQCRWTNC AQTCPSGWSA VKRQDPYAKS IKELMLDDTG
CGGNGLRTFC CPPGKQPFCQ WLFHNNGKCS PGCPDSDMYE VASTSAACDN GKAQVACCKG
DTPGLDVYRQ YKWYSKEHDC AIDLGSKQCG WSSTFNMPLT SSWDGSGAQV CRDSKGKRGT
RPICGDESDS TKAHFTNCQW VDNFDLGLTN IADRSQCNGN CPSGKVKVAL EVNKYMCSKG
TLAYCCDVEA TFSTKDIDED DLEGLLKAWV KKPTCPKMDV SELSSRSTDT TPSSVSEQLA
PLVRRASSVT VPSAVAVQLT MQRIMEHAPN SPETREYREI FDRAFGTRWK DVTGAYLADR
WFPLKGAMSM ALPALNSMCH MNEEEKAAKD AGGGGALASR SFASGRTLRP LIPGSSKIQK
R
//
