ID E4V771_ARTGP Unreviewed; 783 AA.
AC E4V771;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=MGYG_08862 {ECO:0000313|EMBL:EFQ96937.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS989831; EFQ96937.1; -; Genomic_DNA.
DR RefSeq; XP_003169314.1; XM_003169266.1.
DR AlphaFoldDB; E4V771; -.
DR STRING; 535722.E4V771; -.
DR GeneID; 10024486; -.
DR VEuPathDB; FungiDB:MGYG_08862; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_2_2_1; -.
DR InParanoid; E4V771; -.
DR OMA; CASGTAM; -.
DR OrthoDB; 50378at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 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:UP000002669};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..783
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003188437"
FT DOMAIN 142..188
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 201..562
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 156..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 161..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 783 AA; 84149 MW; B5C9CFF650014F29 CRC64;
MCWYLSAIVA TGLLAGASVD ATTDSIPHTQ SLTTSTAKWE PHPPLPRNSS KALAALFQAY
SPDTPVFLNH ELANRLASNG THSSQMSLNG KDVVLDKKAL PLGTCAPGTP CTNGACCSKT
GVCSYAPSSC APKNCISNCD AKAPCGQYAA KGEGNCPLNV CCSEFGFCGT TTDFCGKGCQ
KDYGSCEEVK RPSCLGNSAN GRRIGYYEGW AGDPSARPCD RKLPTDLDLT GLTHLNFAFA
FFDPKSFSIT PMTDTTAKLY KSFTGLKDKH QWLETWISIG GWSFNNDGNN PDTRTAFSRM
VGSAANRRAF ISSLENFMQT YGFNGVDIDW EYPAAHDRGG VAADTGNLAE LVAEMRAAWG
KSYGITATLP LSYWYLQGFD VKTMQEYVDW FNVMSYDIHG VWDANTRFQG QYIRPHTNLT
EIKQGLDLLW MAGVAPEKVT LGVGWYGRSF TLADPSCSQP NGVCQFTEGG KPGRCTNSAG
TLSIAEIKAI IASGAATQYL DSEAAVRWMT WDNNQWVSYD DGATTLQKIQ AANSLCLGGI
MIWALDQDNS KGSAMNDLLG IGEANGVSEA AAREYKEQLN NATLQSAIAS SCYWTLCDEG
CNDGYFDVTE AKGQVTNVQK RPICSNGQLQ TLCCAPGTTV GKCEWEGFRG VGLPCTPVCS
DPEAAIVARN SNSYTNNEFD QLMDLTCTGG YQAFCCSGFV PSSKTNTKNK FLYGQGIFNK
LDLARIKSRD LAKGARDDTL TVAICAAAVG VLIAAAPFTS GLSLIGISEA LTLCHRWNSS
FGS
//
