ID M2R476_CERS8 Unreviewed; 1037 AA.
AC M2R476;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Glycoside hydrolase family 18 protein {ECO:0000313|EMBL:EMD33736.1};
GN ORFNames=CERSUDRAFT_87079 {ECO:0000313|EMBL:EMD33736.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD33736.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD33736.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD33736.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(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};
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DR EMBL; KB445805; EMD33736.1; -; Genomic_DNA.
DR AlphaFoldDB; M2R476; -.
DR STRING; 914234.M2R476; -.
DR HOGENOM; CLU_293191_0_0_1; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000016930; 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 4: Predicted;
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:UP000016930};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1037
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004023740"
FT DOMAIN 42..428
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 428..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..457
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..693
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..743
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1037 AA; 101126 MW; 7DD0747644575E0B CRC64;
MLSFFTLALF AAPAVHAAGP SFFIRDATTA SPNTTTNATV DMVSASWYAG WHAQDFPLSN
VSWDKYTHLT YSFASTVPSV NNISLDASDA ELLPQFVSMA HQNGVKALVS TGGWGGSQYF
STDVNSPANR SAFVKTITSF AQQFQVDGID FDWEYPGSQG IGCNVVSPND TSNFLTFLQE
LRADPVGKNL IVTAATPLTP WKDDSGVSLT NVSAFAEVLD WIAIMNYDVW GSWSASVGPN
SPLNDTCAQP SDQQGSAVSA VKAWTAAGIP SHQIVLGVAS YGHSFHVDSD DALECDDDST
VLAAYPAFTA AEQPLGDKWD APTNTDQCGQ TSGPSGVFDF WGLIDAGFLF ANGSVAEGID
YRFDECSQTA YVYNETSEVM VSFDDAKAFA AKGDFIKSSN LRGFAMWEAG GDSDDILLDS
IRAAAGFEDD DDCEGNQESE IPGNDDGDDD CDDGDDETSS ASATFVAPTQ IAPSAAPAPA
PTQPSSGNSG NSGSSSSSSS SGSSNNSGNS RSSSSSSSSS SSDNGNSGAS NSNSGSSSSQ
SSSSSSGNDN SGASSGSSNS APANSEPAPA PSPSESSSEN SSSSNSGSSG SSNSNSNGGS
APEAPAPAPS SATGGSSVEQ TTAPAAEPTQ VTAAPTASAP AASPSSTGDG DDDDCDDEGD
EPTASASATL PTSTDDGDDD DDDCDDEGDE PEPTETPVPT SAPTTAPTSV PVPASASLTT
SAPEASSTDD GDDDCDDEGD EPEPSSVVVS ASVLSSASSA PSVSASVSSA SASSVSASAS
ASVAPSVSAS VSASAASVSA SASVASASGS VSASTVVPSA SVSVSASSAV ISASVSSVVI
PVSSASPVSA SSAAVSVSAS SVAVSGSASS VAVPASASSA AASASASSAA VSPSASSASA
PASVSSVAAV PSASSVAVAP SASSAVVSAA APSSSAPAPA SSAVASEAAP SVAPSAPASS
YVAPAPASSY VAPAPSSSYV APAPSSSPVV VAPASSAPAA APSSDAPAPI PSSAAAASAS
AAVPVSSAAA SPSADWY
//
