ID A0A0V0X5Y8_9BILA Unreviewed; 1478 AA.
AC A0A0V0X5Y8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Putative chitinase 3 {ECO:0000313|EMBL:KRX83304.1};
GN Name=Cht3 {ECO:0000313|EMBL:KRX83304.1};
GN ORFNames=T06_4563 {ECO:0000313|EMBL:KRX83304.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX83304.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX83304.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX83304.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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:KRX83304.1}.
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DR EMBL; JYDK01000014; KRX83304.1; -; Genomic_DNA.
DR Proteomes; UP000054673; Unassembled WGS sequence.
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:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProt.
DR Gene3D; 3.10.50.10; -; 3.
DR Gene3D; 2.170.140.10; Chitin binding domain; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 3.
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; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF01607; CBM_14; 2.
DR Pfam; PF00704; Glyco_hydro_18; 3.
DR SMART; SM00494; ChtBD2; 3.
DR SMART; SM00636; Glyco_18; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 3.
DR SUPFAM; SSF54556; Chitinase insertion domain; 3.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 3.
DR PROSITE; PS50940; CHIT_BIND_II; 2.
DR PROSITE; PS01095; GH18_1; 3.
DR PROSITE; PS51910; GH18_2; 3.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673}.
FT DOMAIN 64..422
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 479..524
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 548..901
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 999..1339
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 1416..1476
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
SQ SEQUENCE 1478 AA; 169860 MW; ECE0BB4A7BFC037B CRC64;
MQQIKKSCMF KITKASRHEY TLGIINCIFK EDVLWENYSD TSHIKGWLLF LLCGCHLFIL
HDRANMLQVK QKSSFAVAIL QTGLNTDLEK ENILLTIINF EWNDIHHLYP SITKLKQSNS
QLKIILSVGG WNFGTAFFRP FKKLSSSADR RSRFANSSII FLRKHNFDGL DLDWEYPDDD
NDRKNLVLLS EDIMSAFKAE AESSKKPRLL LTAAVTADCV KAEAGYDISK LARLWDFMNL
MSYDFHGSWE SVTGINSPLF EKSTDSVQMK KWNIAYAAYC YHLRGMPKKK IIIGIPTYGR
GWTIQNKKNT EIGAPSIGPS LPTKYVRFPG VCAYYEICQM IKVGGQRYWD EESRTPYLVY
NNQWFTYDDE QSFKEKLNWL KEEEFGGAFV WALDFDDFNA QFCSHGERYP LISLLQKQLG
DVESMEKFTG EAQQNIHIQP AAEITNSDSH LNISEVQNND EKEKTNLPEK LINEASSPAF
KCPGNGIFPD LYDCSYFYSC ANGMHFRVAC AAGTLFDRYL KICNHAALIF LTVFLLSTVI
PRYQAKKYIR GCYFTNWAQY RPGEGKYFPE NFEPHLCDYI TYCFKAITFR NFEWNDVSRL
YPSLMNWWSY YGYTFRKFKL ISGSDENRKT FSESAIKFCR LYDFDGLDID WEYPDTSTDK
KNLVLLSRVL LQKFTEESIQ SGKPRLLLTS AVTANHVKAD IGYDVPELAK LWDFMNLMSY
DLRGAWDPIT GMNSPLFSRS TDQTHVKKWN IADAAYHYYK RGMPKEKIVI GLATYGRGWK
LKNRSDISVG AATIGASDST KYVREPGVCS YYEVCEMLQT GGKRYWDHQT RSPYLVKDDQ
WFSYDDPQSF REKLEWLKTE GYGGAFVWTL DFDDFNGVFC PENNGKRYPL ISLMSEILDV
DYVSSASTWP NINIPEISWN TENHRESSDS LLKQSTNSLQ PVYTNWNSLT IPQLFPSFGP
VHCQNNGIFV DHTSCAFFYN CVHGIAHRMA CPMAEAREYI RGCYFTNWAQ YRPEKGKYFP
EDFQEDLCNY VFYAFASINE NLEITNFEWN DVDRLYPDLM KFKELNSDLK IILSVGGATL
GTNSHKNRQN FANSAALFCR KHGFDGIDID WEYPDSAEDN QNLVLLSRVL LETFITEAEQ
SGNRRLFLTF AVTANQIKAD IGYNISELSK IWDFMNLMSY DFHGAWDSYT EYFTQADAAH
HYYKRGMPKE KIVIGLPTYG RGWTLQNASN IKIGAPAVGA SVATKYVREP GVCSYYEACE
MMQDGGIRYW DEETASPYLI KGNQWISFDD QEKWIKREGY GGAFVWTLDF DDFNGQFCPQ
NHGKTYPLTS LISEILSEMP INSSDKSIPN APEKAATLLN SKEQQLNESN DEIFSSSVAH
IPTTTAFAVW QELQESVKTD EITSNNETVV EEMPKHFQCP KPSGLFPNPD DCASFYNCAH
NIPYVINCPP ETLFDEKLLI CNHAYHVNGT RPGCSVSL
//
