ID   A0A2G4SMM8_RHIZD        Unreviewed;       465 AA.
AC   A0A2G4SMM8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=GH18 domain-containing protein {ECO:0000259|PROSITE:PS51910};
GN   ORFNames=RHIMIDRAFT_205883 {ECO:0000313|EMBL:PHZ10037.1};
OS   Rhizopus microsporus ATCC 52813.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ10037.1, ECO:0000313|Proteomes:UP000242254};
RN   [1] {ECO:0000313|EMBL:PHZ10037.1, ECO:0000313|Proteomes:UP000242254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ10037.1,
RC   ECO:0000313|Proteomes:UP000242254};
RX   PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA   Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA   Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT   "Lipid metabolic changes in an early divergent fungus govern the
RT   establishment of a mutualistic symbiosis with endobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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}.
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DR   EMBL; KZ303856; PHZ10037.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4SMM8; -.
DR   STRING; 1340429.A0A2G4SMM8; -.
DR   OrthoDB; 3203764at2759; -.
DR   Proteomes; UP000242254; 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:UP000242254};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..465
FT                   /note="GH18 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013942142"
FT   DOMAIN          98..465
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          26..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   465 AA;  51615 MW;  662E8E4600642D76 CRC64;
     MRNLLFILIA LCVLFTYTAS AASHTKGHSK HKSVAHHHNK HSPKKHHTPA HHSTGKKKKT
     TKKVTKKTSK KGSKKGSKKS TTKKTPTTHA HQKAYPKHKI VAYVLDWDTP KNIVWNKLDH
     IVYAFAEPNV KGDLKNFDGN NLKKLVNEAH KHNVGVSISV AGWSGSIHMS SLVADANRET
     FASKIVALVD KYNLDGVNLD WEFPNSPDSI ACSERNPMDT ANYLALFQAL RKKLDAKYPK
     IHKALTVAAP VGPFNDENGR GIRRLDPAWA TTVDYFYLMS YEYNGSWNSV AAPNAAIRGS
     SHGWGVDTTV GFWANAGIPK NKMHIGITFY GKALKTAQPI TETSGMYVKL DGHIPIQGDK
     HDELAADPCP GAKPGYTGEF QYRSIVAQGI QQNKNGWKSY WDEQSQTPYA FHAADSKFLT
     FENPKSIQAK MEYAKSEGLA GCMIWSLEMD DPKHSLLNAV QSARH
//