ID A0A2R2MI59_LINUN Unreviewed; 2257 AA.
AC A0A2R2MI59;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Probable chitinase 10 {ECO:0000313|RefSeq:XP_023929899.1};
GN Name=LOC106153230 {ECO:0000313|RefSeq:XP_023929899.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_023929899.1};
RN [1] {ECO:0000313|RefSeq:XP_023929899.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_023929899.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR RefSeq; XP_023929899.1; XM_024074131.1.
DR STRING; 7574.A0A2R2MI59; -.
DR EnsemblMetazoa; XM_024074131.1; XP_023929899.1; LOC106153230.
DR KEGG; lak:106153230; -.
DR InParanoid; A0A2R2MI59; -.
DR OrthoDB; 1752999at2759; -.
DR Proteomes; UP000085678; 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:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProt.
DR CDD; cd02872; GH18_chitolectin_chitotriosidase; 1.
DR Gene3D; 3.10.50.10; -; 2.
DR Gene3D; 2.170.140.10; Chitin binding domain; 7.
DR Gene3D; 3.20.20.80; Glycosidases; 5.
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; 10.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR SMART; SM00494; ChtBD2; 10.
DR SMART; SM00636; Glyco_18; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF54556; Chitinase insertion domain; 2.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 10.
DR PROSITE; PS50940; CHIT_BIND_II; 10.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 2.
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:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2257
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015201116"
FT DOMAIN 25..397
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 465..844
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 893..952
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1002..1061
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1118..1177
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1235..1291
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1347..1403
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1461..1517
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1577..1633
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1690..1747
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1798..1855
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 2202..2257
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 398..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1754..1778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1949..1992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2009..2197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2257 AA; 247468 MW; 36E73A4DAAF46EA7 CRC64;
MKHLELVAVA LLNLILPSFP ETAEFRRVCY YANWSVYRTG DSKFLIELLD LSACTHAIYA
FATLVNGQLA PSEWNDDITY PQRHFFGGNY RRFNNQKVGT NLKTLLGVGG RNLGNTPFAQ
IVSTAESRRR FITHAVEFLT SRGFDGLSLE WNYPGSVAAD DKEKFATWVK EIKSEFERHA
LLLSIAILGD QQIISKAYNL PELSKYIDFA TVMAFDFASG SEKTIRHHSP LYGLKGPADT
TDTASQHWLV QHLIKDGLDR SRIVPVLPAF GVGYTLASPD NIAFGSAAYK PGTAGASGAG
DQVLLYHEIC NKVTSPGTSW KRAWSDLSKA PVVYNNESWQ WYSYDDEYSV AYKTKYAKDQ
RLGGIGVWSI DEDDFQSSCG PRSFPLIRHI QDVVSGTARA TTPSYPRLPA PQTATPAPTP
PDGGGQRPSP TPPQTPPAPV STEVPVPSSA PCDDKPAVRR NPSQYRRVCY YTNWSQYRSG
VGKFLPSHID PSLCSHVIFA FARLERGLLV PAEWNDLGTA WNRGLYDQMR DIKSKNKKLK
ILLAVGGWVL GVEPFTEMVA TSASRATFII HAINFIREHG FDGLDIDWEW PAQRDSPAID
RVRFTYLLQE LRAAIEKDAS STNRTKLLLS AAVAQNVKVI DTGYEACHIH KYVDFLSVIG
FDFYSSEGSV LGINSPLYHT CAEQYTEWGL ERNMYFIINY WLKQGIPRHK LVVGMGMFGH
TFRLASPTLT EPTDPSGGRG ISGTYTNEPG FIAYYEVCKK ILDENWVTKW SEEQAAPYAY
SVSSMGWVSY DNVTSIQLKA KYIIDQKLGG AMIWSLDLDD FTGQNCGQGK YPLLSAINQV
FRRPQRFPSF KLPKRCPATT TTTTTTAAPV EPFVTSSETG PVIPIPLPAP EDVAFCKGKS
FGSYPDPEDC KFFYACLGAV QQRIGCEGNQ YFNPDRGTCD DAGDNWDGTC PPSRPTQTTT
KRVRVTAPPV RTRGTTRRPK PTRIRTTAPR LQTTTNPPTA YPFTCSGKRA GSHPDPFDCS
GYYRCLGGGR LQHNKCRGVL HFNPKTKACD WPRNIKPPCT PAVMVTHPPT TPGSTVRTRA
PSTPWRRPTT RRRIVTTRRR TLTPPQPTTT QEPPTAYPFS CSGKQLGSHA DPYDCGKFYT
CLGGLRMQRQ QCLGGLHFNP KTGFCDWAFN IRPPCVTAIM VTYPPTTPGP TRATTPKPVR
IRPTPKSLGG RRTTARPVYG VQTTLTTPIR PTAYPFTCDG KATGRYADPF DCKSFYICVF
QTMKKYLCRG NLIFNPETRA CDWPQNTNCV PAIMVTLPPT EANKVTKKYV SSTPREKVTF
YKPIQQRTTT KVEQTTPVTT VQPTAYPFTC VGKTTGYYPD PFDCESFYFC IGSSQRHMKC
RTPLKFNKDN GACDWAFKVN CVEAKLVPRP TTDAPPSTRA ASSAAATTTR PYREGKITVT
KPTMPYPSVT ETTMTRPTAY PFTCQGKPSG RHADPFDCAS FYLCLFGSAR HLSCGRGLVF
SPKNQSCDWP DRVKCTPAVL VTRPPTTTHR PVESQGPVRQ TTNGPRTGAV IPTKDLTKTT
TPEQSTESTR PKVTAYPFTC EGKRNGRFAD PFDCSMYYLC IGGKGRHLQC MGNLKFNREI
GSCDWHFNAK CTEAEMVTHP YSSSSPVAGV TMSSQKPQRK TSTKRQQPAW TERQKTTTKP
TLGPRPTAYP FTCKGKSIGH YADPFNCRSY YLCLSGGQRR HITCIKPLIF NPNNKACDWE
FNYRCIPAIE VSPPTTEEPE TTKPVTTTSV KKEKETTLRL STTAQTEATF ASQPTAEAFT
CEGKDDLARY RDPFDCSAYY FCVRGVGRRI RCMKPLHYNE AKLACDWPRY VNCVPAVLAK
QISTTDGRRP KTTLGSTTQE PTITLKSTVV RTTLQSTVKA PTPTIVTTMS RTTTPVQPVL
STSESTTSAV TKIGSVTSAS TTAVMTASIA PEPTKEATAS ASVKSQPTIK KTSATTSESS
TSTVTTIESA PTTTVTTASI TPELTKAAST AASVKSQLKT TSTSTTTSES ATSAAPTTAS
PAFEGTSEAT TTVSKTTAAK TSPTTSAPTT TASTTTVSTT SASTTTAAVT SQSTREATST
TSELKTPEPT TTVSEPTTPM ATTASITTQT TTATSTTIKP TSSPATTSST TLEPTTVAVT
ATSNPTTAAD SSSASTKTIK QSVTPPVPQA TFPSTSKATD RPFQCGNNIG IFADPADCSM
FYLCTGKARR HVRCFGGLLF DPDTKACDRP SKVDCKN
//
