ID B8MPH4_TALSN Unreviewed; 703 AA.
AC B8MPH4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 22-FEB-2023, entry version 63.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=TSTA_106220 {ECO:0000313|EMBL:EED14413.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED14413.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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: 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; EQ962658; EED14413.1; -; Genomic_DNA.
DR RefSeq; XP_002486651.1; XM_002486606.1.
DR AlphaFoldDB; B8MPH4; -.
DR STRING; 441959.B8MPH4; -.
DR GeneID; 8098775; -.
DR VEuPathDB; FungiDB:TSTA_106220; -.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_392409_0_0_1; -.
DR InParanoid; B8MPH4; -.
DR OrthoDB; 360175at2759; -.
DR PhylomeDB; B8MPH4; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
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 InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF03221; HTH_Tnp_Tc5; 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 wall {ECO:0000256|ARBA:ARBA00022512};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
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 Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..703
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002877882"
FT DOMAIN 30..326
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 662..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 78036 MW; 9FA242DAD5FED086 CRC64;
MHSLSKIFIA GALASTALAF PTVHQRDSQY KLTVYWGAED DSTTLSDVCS DDSYQIVNLA
FVSYFNGDGG YPTLSLSTLD GPSQAQQDAG ATSLQDGSSL VDAIQACQSS GKLVLMSLGG
GAGDSNVILS GDDQAKDVAD MLWNLFGGGT DENITPLRPF GDVKLDGFDI DNESGDPTGY
SALVSRLRSN FAQDTSKKYY LTAAPQCPYP DQSVPLDVCK ELDYVWVQFY NNGDCDVAKS
DFINSVKTWS KGIGNAKLFI GAVASDADGD EGYVDSETMA SSLKKVEKLG LSNFGGAMLW
EAQLAVKNDN YQWDVAAAFK LSREYGVSRK KLSRRWNGLP SRSTRSPTNR LLSLDQEKAL
ILWIEYLDNI GAPPTNEQIE ESANYLLAKD FTDPGEPPRA GKIIVQKPQE RDWTTAEHYG
EIERWFIDLK IAIQELKIVP QKFWNFDETG FIVGKGKDEA VVARLGGFDF NKNDFFEELC
NIQIKIFTTR TIRHGWKERG IWPYDPKLIL DKMPQPDEAF EKLAADGDTL KIYGEPDDTI
PSSPTTKSIS PPSSVAKLRR YINKIEKSVD GIKDILDSAI PGLSHRIKAI NQGSLTLAEL
GRLYRESFIK VRDTEKRKQQ KTTKRQVKAM GALYVKDTNR LIKRRHEGDL LRIHKSHILG
VEELEQQEAP TEPGPTPNRR VEGGDATGRT LKYSHATSYM DFK
//
