ID A0A395HL36_ASPHC Unreviewed; 1148 AA.
AC A0A395HL36;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=BO97DRAFT_481591 {ECO:0000313|EMBL:RAL07004.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL07004.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL07004.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL07004.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GPI-anchored chitinase involved in the degradation of chitin,
CC a component of the cell walls of fungi and exoskeletal elements of some
CC animals (including worms and arthropods). Required to reshape the cell
CC wall at the sites where cell wall remodeling and/or cell wall
CC maturation actively take place such as sites of conidia formation.
CC {ECO:0000256|ARBA:ARBA00024658}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}. Secreted, cell wall
CC {ECO:0000256|ARBA:ARBA00004191}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000256|ARBA:ARBA00025727}.
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DR EMBL; KZ824343; RAL07004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HL36; -.
DR STRING; 1450537.A0A395HL36; -.
DR VEuPathDB; FungiDB:BO97DRAFT_481591; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000248961; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF47; ENDOCHITINASE A; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1148
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017379282"
FT DOMAIN 28..339
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 340..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 113548 MW; 58D713A6789E486C CRC64;
MVSQLVTVLA AVSAVTPFVS AFDPQSKSNV AVYYGQGYGQ KRLSHFCQES SLDIINLGFI
NVFPDQGIAG WPGSNFGNQC DGTTYQVDNL STELLKGCHQ LVEDIPICQA AGKKVFLSLG
GASPDTQQIL SEDSASGFAD FLWGAFGPKT DDWVSKNGPR PFGDVVVDGF DFDIEHNGDY
GYATMINRLR YHYSSQQGRT FYISGAPQCS IPDQHLDSAI ANAAFDFLWV QFYNTEGCSA
RDYIEGTVDG FNFDKWVDVI KAGGNPDAKL YVGLPAGPGA ANPGYYLSPN EAYSLAAEYM
ARFPDTFGGI MLWEATASDE NKIGDESFAD VMKQILVTLD PTPPQTSTAL PSSSTPAPAT
SYTSTSTPVV STSSAVSIPP VVSISSAVSS PPAVSSSSAV SSASAVSSSG TTGLSSISAV
VSSSSVVSSN SVLASTPVLT SSSVVASTAL STPVVVGSSA VSSFSAASSL PVVSGSTVVS
SSFVVSSASV VSSSPVVSGS SIISITPIIT TNRVVSSSAS ASSSLVVTSR PVIPSSSDVS
GSASSSPVVS GSSVSSSSPV VSSPVVATSS VTASPHGTSI SPVVSVSTQS GSSGVSISSV
VTSRPVIPKP SSSILAVPGD SRTPSSSVIP GTSGQAPSSV SQLSSPSIVS SSVGPSGPSI
TSVGSAPSSS AGASNNVAFS SGAETSSGQS LSSSSVVSTL TSTVAGVSSE TASSTSPSVG
SSTAVSTVSA AQSGGSAQSA SGTITVSASN THVASTASRT DATSKAELSS GSSPISTSVS
GSGAAPSANP ETSHEPGVTG STTALTILSP TDQRSTTSLS ATTHTIGDVS GQTGKPTAVT
SDATSTGSGA SAIITPGITS GLGGISVSPT ASVSEPVTTT TIIVTSYIDI CPEGFTTITT
TYTTTYCPAT AAAITTAPAT VTGAPGNPAS ATTVDIPEGW TTTVTVCTHC AATPTTVTLT
RPATSLPAGP ASPTTVPAPL SEWTTTVSVC TECGPTPTTV TVTVPVSTIV AVTGTQFGNP
YGVDAVREGS TGLGVSPTSV EVIPHPTFIA LVSASSGPAS ASHSASHSGP AGADSARPFS
GTGGANGARP SSTLLVQPSG SGFPGSVAPS HTQGGVSPVF TGAAPRMTAF KHGAGTLVTV
ALLLLTIL
//
