ID A0A068RSZ7_9FUNG Unreviewed; 406 AA.
AC A0A068RSZ7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glycoside hydrolase family 18 protein {ECO:0000313|EMBL:CDH53129.1};
GN ORFNames=LCOR_04518.1 {ECO:0000313|EMBL:CDH53129.1};
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:CDH53129.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH53129.1, 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:CDH53129.1}.
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DR EMBL; CBTN010000016; CDH53129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068RSZ7; -.
DR STRING; 1263082.A0A068RSZ7; -.
DR VEuPathDB; FungiDB:LCOR_04518.1; -.
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 CDD; cd06548; GH18_chitinase; 1.
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:SF317; CHITINASE 11; 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}.
FT DOMAIN 11..382
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 406 AA; 45695 MW; 18540201F26B8772 CRC64;
MQPPPPATNG PVIAGYFVNW GIYARNHNVI DLAPDAHKLT HLLYAFANLE PSGNVILGDV
WADKDKHFPA EQTIDGQADS WNDQGNNLYG NFKQLYLLKQ RHRHLKVTLS VGGYSWSANF
GAVAADPQKR ATFVQSAIKH VADLGLDGLD IDWEYPKDPQ EAFNFVHLLY ELRIALDRYQ
QSLGQTNEPR LLLTLAVACG PDNYRLLRLR EMEPYVDIFY LMAYDFAGSW DSQTGNQSAL
HGGSINGHRA VTDYMQAGVP PHKLVLGLPA YGRAFSNTSG LHSSFRGLPK GTWGEDGMYD
YKELPRPGAT EHNDLQNMAS YSYDPAKREF VSYDTPEVVR AKCEYIKQMR LGGAMFWELS
ADHKDNHPRS LLNTVYNSFG GHLDTIPNHL RFPQSQYDNI RAMGNM
//
