ID A0A074YIH2_AURPU Unreviewed; 1122 AA.
AC A0A074YIH2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=M438DRAFT_404228 {ECO:0000313|EMBL:KEQ86651.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ86651.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ86651.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ86651.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; KL584978; KEQ86651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074YIH2; -.
DR STRING; 1043002.A0A074YIH2; -.
DR HOGENOM; CLU_010456_0_0_1; -.
DR OrthoDB; 671410at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
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; cd11618; ChtBD1_1; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_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:SF333; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 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 Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT DOMAIN 45..91
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 105..467
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 681..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 59..71
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 64..78
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1122 AA; 121399 MW; F453E71A435116B0 CRC64;
MQILPALTVR VVVQMGFVVI RQPSVEVAIV HRKLTIRPQS NCNAKAECGQ YGVIGKQTCP
LGVCCSKFGF CGSTDEFCST GCQTGFGGCG PVTRPSCKGG NSAAKRSVGY YESWSNTRKC
QSVAPEDLNL NGFTHINFAF AFFDPTTFAI APMDGKTGYL YSRFTALKSQ GVQTWISVGG
WSFTDPGPTR TAFSTMSSTS ANRKAFISGL IDFMDTYGFD GVDIDWEYPQ ADDRGGASAD
TANYVALVKD MRTAFGTKYG ITVTLPTSYW YLQHFDLANM QASVDWFNVM SYDLHGVWDA
ESKNIGPYIA PHTNLTEIDL GLDLLWRAGI KPDKVVLGQG WYGRSFTLTN PTCKTPNGKC
QFSGGADAGK CSNAAGILDL QEIKDIISDN NLTPTWDKTA GVKWINWASD QWVSYDDDDT
FKQKADFANS RCLGGLMVWA MDQVDQTAGN QNSVTLDVTE DQQADAKQKA ADLTAGISCY
TTDCDAKCKS GTNQVEQMNG QPGSLSTNDR CSKGKYRSLC CDDGTTMGTC QWRGYRGVGL
SCISGCDDGE TEVVQDTNHK EKKKDQTCSG GLQSYCCKGF QPAPNGPDLA KDAKELASNA
AEAIAAEVAL DIAAKAFCRI AVPALLLPLE LIEDAIPIVG EILDLIEIAA TPAIIQACVK
GIEKEGKAEF KVFGKKHTLS MDKPTKPVTS RPPTSTHSPA KTSSNCPRIP KRDLEKRALD
KRAPACVNEK YVTVTTKISD EAGPKDKFVC TYAGGNKPGG QACLHYSSVI AAQGQAYDTF
TCKYSATKAT KRPGVAEYNV DRPTVRTIQK VPVTLGWFQD IGGNACERDE WPPAAFLIAN
DGYIGLEGAQ ARTGVDVQQF IRYLDKQENN FAGKGWVGIC AKSPPVRLIN TKEVKDKPDA
KGTTTITRSV EAVFKRQTYS YSFEAMPNPM LPDWGLADNR CQPSKPNRDD RGFALLDRDP
WFGGGVVANA VPQQADYKLQ FSLVKRDVLD GLDALGINGT SEASSCEAYD EEETQLSRDD
MLEAFGIKQC KEKSCKEEAE ALGLESLRIA YADTATLPAG IPAIATATGT VVGSETAATS
ADGTRETNGA LSRSQATSSM PRVTHHPRHQ AGHHHQGHRD GV
//
