ID A0A3B4YIZ9_SERLL Unreviewed; 471 AA.
AC A0A3B4YIZ9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000030555.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000030555.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR AlphaFoldDB; A0A3B4YIZ9; -.
DR Ensembl; ENSSLDT00000031437.1; ENSSLDP00000030555.1; ENSSLDG00000021637.1.
DR GeneTree; ENSGT00940000162989; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF379; CHITINASE-RELATED; 1.
DR Pfam; PF01607; CBM_14; 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 SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669}.
FT DOMAIN 1..357
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 422..471
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 375..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 51507 MW; 848428CE2F6CF5E2 CRC64;
MLSVSDLSTE DGKFRISNIN PNQCTHLIFA FSDISSVNDL VPSRDTDVQL YQSFNGLKTR
NPLLKTLLAV GGITFNRQKF STMVSTQTTR AMFIQSAITL LRKYGFDGLN LDWRFPAAAG
SQSDNKQKFT LLCQELNAAF VAEGTQNNSD RLILTASVSA EKAVIDASYE VAQIAGNLDF
INVLTFDFRG PWENVTGHHS PLFRGSQDTG DKINSNTDGM QYWRDQGAPA QLLNLGLATY
GRAFTLSSPS TDVGAPANGT GEEGCYTGED GFWAYYEVLL YYYALITDQK VPYALTENQW
VGFDNKESFE TKVSYLKTNN FGGAFVWSLD LDDFTGKFCN DSKYPLISHV HDLLVPGDKN
AISVCCILPT TTPTTTTPTT TTPTITTPTT TTPTTTTTSS TTTTPTTTPT TTSPTTITTT
PTSLCAGKNS GLISNPKDPQ SFFNCGDKAV HLQYCQARLI FKESCQCCDY P
//