ID A0A0V0ZVN6_9BILA Unreviewed; 1441 AA.
AC A0A0V0ZVN6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative chitinase 3 {ECO:0000313|EMBL:KRY16217.1};
GN Name=cht-1 {ECO:0000313|EMBL:KRY16217.1};
GN ORFNames=T12_7698 {ECO:0000313|EMBL:KRY16217.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY16217.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY16217.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY16217.1};
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:KRY16217.1}.
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DR EMBL; JYDQ01000082; KRY16217.1; -; Genomic_DNA.
DR Proteomes; UP000054783; 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; 2.
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:UP000054783}.
FT DOMAIN 147..374
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 436..481
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 505..858
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 956..1302
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 1379..1439
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
SQ SEQUENCE 1441 AA; 165262 MW; BBF40B84738EE5AC CRC64;
MKASRHEYTL GIINCIFKED VFWENYSDTS HLIKGWLLFL LCGCHLCILH DRANMLQVKQ
KSSFAVAILQ TGLNTDLEKE NILLTIILHN FYDASRNRLK IKLKLQLAAG ILAQRKSDNK
LLHLRNADSL DHLKNSLPPR TEEDIMSAFK AEAESSKKPR LLLTAAVTAD CVKAEAGYDI
SKLARLWDFM NLMSYDFHGS WESVTGINSP LFEKSTDSVQ MKKWNIAYAA YCYHLRGMPK
KKIIIGIPTY GRGWTIQNMT NTEIGAPSIG PSLPTKYVRF PGVCAYYEIC QMIKAGGQRY
WDEESRTPYL VYNNQWFTYD DEQSFKEKLN WLKEEEFGGA FVWALDFDDF NAHFCSHGER
YPLISLLQKQ LGDVSNASVE SMEKFTEEAQ QNIHIQPAAE ITSNDSHLNI SEVQNNDEKE
KTNLPEKLIN ETSSPAFKCP GNGIFPDLYD CSYFYSCANG MHFRVACAAG TLFDRYLKIC
NHAALIFLTV FLLSTVIPRY QAKKYIRGCY FTNWAQYRPG EGKYFPENFE PHLCDYINYS
FKAITFRNFE WNDVSRLYPS LMNWWSYYGY TFRKFKLISG SDENRKTFSE SAIKFCRLYD
FDGLDIDWEY PDTSTDKKNF VLLSRVLLQK FTEESIQSGK PRLLLTSAVT ANHVKADIGY
DVPELAKLWD FMNLMSYDLR GAWDPITGMN SPLFSRSTDQ THVKKWNIAD AAYHYYKRGM
PKEKIVIGLA TYGRGWKLKN RSDISVGAAT IGASDSTKYV REPGVCSYYE VCEMLQTGGK
RYWDHQTRSP YLVKDDQWFS YDDPQSFREK LEWLKTEGYG GAFVWTLDFD DFNGVFCPEN
NGKRYPLISL MSEILDVDYV SSASTWPNIN IPEISWNTEN HRESSDSLFK QSTNSLQPVY
SNWNSLTIPQ LFPSFGPVHC QNNGIFVDHT SCAFFYNCVH GIAHRMACPM AEAREYIRGC
YFTNWAQYRP EKGKYFPEDF QEDLCNYVFY AFASINENLE ITNFEWNDVD RLYPDLMKFK
ELNSDLKIIL SVGGATLGTN SHKNRQNFAN SAVLFCRKHG FDGIDVDWEY PDSAEDNQNL
VLLSRVLLET FITEAEQSGN RRLFLTFAVT ANQIKADIGY NVSELSKIWD FMNLMSYDFH
GAWDSYTEYF TQADAAHHYY KRGMPKEKIV IGLPTYGRGW TLQNASNIKI GAPAVGASVA
TKYVREPGVC SYYEACEMMQ DGGIRYWDEE TASPYLIKGN QWISFDDQES FRKKAKWIKQ
EGYGGAFVWT LDFDDFNGQF CPQNHGKTYP LTSLISEILS EMPINSSDKS IPNAPEKAAT
LLNSKEKQLN ESNDETFSSS VAHIPTTTAF AAWQELQESV KTDEITSNNE TVVDEMPKHF
QCPKPSGLFP NPDDCASFYN CAHNIPYVIN CPPETLFDEK LLICNHAYHV NGTRSGCSVS
L
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