ID A0A068RX00_9FUNG Unreviewed; 425 AA.
AC A0A068RX00;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glycoside hydrolase family 18 protein {ECO:0000313|EMBL:CDH54683.1};
GN ORFNames=LCOR_05904.1 {ECO:0000313|EMBL:CDH54683.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH54683.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH54683.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|RuleBase:RU004453}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDH54683.1}.
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DR EMBL; CBTN010000024; CDH54683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068RX00; -.
DR STRING; 1263082.A0A068RX00; -.
DR VEuPathDB; FungiDB:LCOR_05904.1; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; 3.20.20.80; Glycosidases; 1.
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:SF406; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 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 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:UP000027586};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..425
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001652816"
FT DOMAIN 34..415
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 425 AA; 46857 MW; 543FE2B541B8FD37 CRC64;
MRLFLSHLLC LAFTAIITTS AAASNSSSSK SSGKTLTGYF PNWLYARWPV SNIDFSKYTH
INYAFAIMIK GSTPEWTDPQ QVETQLPELV KAAHAKDAKV LISVGGWSGC LTFSSMVGDS
SKRSEFIKWS TDQIDKYDID GIDIDWEYPG RQGAGCNEVD KANDAKNLLT LLQELRSAMD
KKYKNKELTA AVHVRTFDTS SGNMKDVSAF GKVLDRVNIM AYDINGAFNS TSGPNAPFNF
EPGLGYDDSY VSSIETWIKA GVPASKISPG LAFYGRSTTS TVDMSKTNQY QPQVKGKPPK
GDSLDAYWQD PNCPKDPGGM SGIWRYGNLR SEGVLTAPDK AASPWIRQWD KVTQTPWLFN
PKDKTFISYD DPKSISIKVD YALCKDLGGV MVFSVDEDSS NNELLNEAYK IRTGSNSSSK
NCNSN
//
