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CHI1_METRA
ID   CHI1_METRA              Reviewed;         424 AA.
AC   E9ERT9;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Endochitinase 1;
DE            EC=3.2.1.14;
DE   AltName: Full=Chitinase 1;
DE   Flags: Precursor;
GN   Name=chit1; ORFNames=MAA_02685;
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075;
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075;
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- FUNCTION: Secreted chitinase involved in the degradation of chitin, a
CC       component of the cell walls of fungi and exoskeletal elements of some
CC       animals (including worms and arthropods). Participates in the infection
CC       process and directly acts in the penetration process of the host
CC       cuticle (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class V subfamily. {ECO:0000305}.
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DR   EMBL; ADNJ02000004; EFZ01456.1; -; Genomic_DNA.
DR   RefSeq; XP_007818874.1; XM_007820683.1.
DR   AlphaFoldDB; E9ERT9; -.
DR   SMR; E9ERT9; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   EnsemblFungi; EFZ01456; EFZ01456; MAA_02685.
DR   GeneID; 19256971; -.
DR   KEGG; maj:MAA_02685; -.
DR   HOGENOM; CLU_002833_1_0_1; -.
DR   Proteomes; UP000002498; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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   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   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF54556; SSF54556; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..424
FT                   /note="Endochitinase 1"
FT                   /id="PRO_0000429865"
FT   DOMAIN          39..402
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          385..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         103..104
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         130..133
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         173
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         238..241
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         379
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   424 AA;  46113 MW;  9E460A593B3EE324 CRC64;
     MPSLFAQSLA IIATLQATLG LATPVSAPDT VTGKHAGGYV NAVYFTNWGI YGRNYQPADL
     PASQISHVLY SFLNLSNNGT VYSGDSWADI DKHYPNDSWN DVGNNVYGCV KQLYLLKKAN
     RNMKTMLSIG GWTWSTNFPA AASTAATRSN FAKSAVTIMK DWGFDGIDVD WEYPADDAQA
     ANMVLLLQAV RDELDAYAAK FAQGYHFQLS IAAPAGPANY NKLHLGDLGK VLDYINLMAY
     DFSGSWSNSS AHNANLYANP GNLNATPFNT DDAVNDYIKG GVPASKIVLG MPIYGKSFQK
     TNGIGKPFSG VGDGSWENGI WDYKVLPKAG ATVIYDDVAK GYYSYDNRTQ ELISYDTPDI
     TKEKVTYLKS KGLGGSMFWE ASADRQGPDS LIGTSSNKLG GPDTTENLLN YPDSKYDNMR
     KQMA
 
 
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