ID A0A0N1INA4_PAPMA Unreviewed; 2481 AA.
AC A0A0N1INA4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Acidic mammalian chitinase {ECO:0000313|EMBL:KPJ07038.1};
GN ORFNames=RR48_04058 {ECO:0000313|EMBL:KPJ07038.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ07038.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ07038.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ07038.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ07038.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR EMBL; KQ461192; KPJ07038.1; -; Genomic_DNA.
DR STRING; 76193.A0A0N1INA4; -.
DR InParanoid; A0A0N1INA4; -.
DR Proteomes; UP000053240; 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 CDD; cd02872; GH18_chitolectin_chitotriosidase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 2.170.140.10; Chitin binding domain; 1.
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; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF400; CHITINASE 6, ISOFORM C; 1.
DR Pfam; PF01607; CBM_14; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00494; ChtBD2; 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; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000053240};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2481
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005874177"
FT DOMAIN 23..402
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 528..589
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 306..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..1799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2325..2366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..654
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2481 AA; 277137 MW; F31AC8238E5766CB CRC64;
MTTWLPLVLA VVTFATPVLS VEPRVVCYYT NWSVYRPGTA RFNPQNINPY LCTHLVYAFG
GFTKDNTLKP FDKYQDIEKG GYAKFTGLKT YNKNLKTMLA IGGWNEGSSR FSPMVASRDR
RKEFVRNAIK FLRQNHFDGL DLDWEYPAFR DGGKPKDREN YAKLVKELRE EFERESEKTG
KPRLLLTMAV PAGIEYIEKG FDIETLNKQI YTGIGLVRTG ACNAALKSAR ENDYTIKFYL
ENGADPKKLV LGIPTYGRSY TLFNPDAVEI GSPADGPGEQ GDATREKGYL AYYEICEALK
PKQKKRSISS DSEEYSDEEE EEDEEWTVMH PNPTAMGPVA FKGNQWVGYD DINIVKKKAE
YVAENGLGGI MFWSIDNDDF RGNCHGKPYP LIEAAKESYI QKLGSTDNTI VSERPKSRKS
GSKSGRRNKR PRTTSTTTTT TTTTEEPSTR STDNTIVSER PKSRKSGSKS GRRNKRPRTT
STTTTTTTTT EEPSTRSNKR KSGSATSTTP AWNVITPEPP TTPDPGSDFK CTDEGFFPHP
RDCKKYFWCL DSGPSDLGIV AHQFTCPSGL YFNKAADSCD FARNVLCKVS AATTKAPTKA
PTTRTTVTTT TTTTTRKPLR ISTRNSLLFR TSTTPAPQEE EYEDEDDEDN TADDAEDPKV
IKELIDLIRK VGGVEQLEKQ LGLSETSIST SSDVATSTPS SFNKKLYQKV LERARGRGKF
NTNGVTGSQS QNSRSGPQNE GLQPTADQDR LLKKDRPQYV TINRSRPPTS VTTANSLESE
EIEDEQESEE QLTRGRSAGV QSKVATTSKP LQYVNIRRSK PTTTVPDTDD DQDPEAVNSL
DIASARRENI PEYVTIRRSR PTTESTTAQY QNSETEVESQ ESALEREITS SSLQPQYTSV
LRIRSTTLPP LEEPSSPEPT TVLAVQISSL LNSPTAAEVP SSEPLSSISI TTQEIEVPTT
TATSPTTTTL PTTPSASTTT ETPSTTTSRR GLRRRGSTTA STATPSSPTS TTQVSARNYN
FIRRRKPLTT PNEITSESEE NVLSRKIRST TPNSREVEGI KQNSEYARNR RYRTRYQPSV
DDSLPAAASP VSANNFGEKF NGDEGLSLIS VDVDAPLFVR RDTNSEGIDE ETSSTEIDEV
PEDSEVSATT VEDKRPTNIF RGRGRYTTIT TTEAISQSTT TESAFTQRRP SFARFTPRPF
ARPTLRPSNN RERSEGVISP RIPLRASFGR ARLSTPTPNN AIGIQPRRLP FPSRSRTTTT
TTTTEQTFTT EIDDEDLENK RDDIYLSESA IEEKEHKDEN EGYSTTNFED TEKLTNNRFS
TTESYDVGET VTSDTGTRKF KVIRRRPTKT TVATETTSTA DFTDTTISTV PRLRKVIRKK
IKQLDSDVET TTKKYTTPDT FKEITKLAFN YGEKTKSTTM TPTTTESQDV EDLPIEPKFE
SNKQQPKLKG NDSSQETQPK PANEDETILK TDEDDNSQND QLTRIEGSET TLGDETASDS
EVNSKDNQKN PDTDTKEDKV LTEDDESDNM AKFNENNNAT VSDQNDNLSD NVEITTFENK
TDIVPDFENM DNLKETDDTI SNNNENIDNT KSENQESDNR SESETNAEDE ASNGTITTTL
ADNAEVVIDS DRGIDLSEKS EYSEGSLTQA NDTSEIEPIT TTSTTTSPSS SVRTRLPYRP
PKRLFTSTTE SSLPSSSRTF SRKYNPGAYT SPATVEREPF RPSVTRRPLF SRTFTRKPFT
ARTTKRVEED EYSDEELLEE EGLDEEAENP FVFVPPSQLF TRKPDSEEEY EDEGNDEFED
GLEEEEIYDE EQVTTPQTTT IGRFTTTSRR PLFRPRVVNS NTFRTSTTTT ELPNTRANAT
QLPKRTFTSG QNKTAVYNRF SSNKPVNDTK KRVQNVPIGY NAPKATSDIK NTTSPVKVEE
KVTTVSPDAS DSELTTIQNE IYTSSNNTTS ILIEAPNDEP ATTMIESQPT TDPIEVNTDE
YLVNSDSYVT KANSEDTQVQ IESIPMTTEP PTTFAITTLE PDKEIITTSQ VPDTTTNATP
APPIVKTQFN KLFSVSRVVE VSSKQDKHHI NKNNETTSIE EGPIVIEKKP TVDKIGEVSR
FTLIKIVEDE IPIYLTKLGH VYPVDNPPNN PIRIDEGRNA RSLGNYYNYP KESLVASESM
NEAYRHIKEF SEQHKEPLLK REVEHISDDD FLSYVNEDKK VEMVKENHNY QFIPAANPST
LSLEGLFKTA SPVTPNKNSD TIESQPFFVY SVADPTESTK KVELIKSEIS SASADNIKKP
KVEQYTTLSP KHIVKPTVNM PTQTSDKNIT ASPVIDILSR IQPTSATESK NVTTTPEPLT
TSEIKTTESS TPKTLSRNNK NTNFPFIRRP NLKISNLTRT VETPRTAKKI STTVKTNSIQ
KSNKTSTFTP SKSRFTANRA QNIPVDTRKK STASKFVPKI TTETPKLTTV KKTFVRPTRQ
TFRPAFIPRR SKSTTNKDLI L
//
