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Database: UniProt
Entry: R9ADC7_WALI9
LinkDB: R9ADC7_WALI9
Original site: R9ADC7_WALI9 
ID   R9ADC7_WALI9            Unreviewed;       557 AA.
AC   R9ADC7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE            EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
GN   ORFNames=J056_001063 {ECO:0000313|EMBL:EOR00177.1};
OS   Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR00177.1, ECO:0000313|Proteomes:UP000014064};
RN   [1] {ECO:0000313|Proteomes:UP000014064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX   PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA   Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT   "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT   ichthyophaga: haloadaptations present and absent.";
RL   BMC Genomics 14:617-617(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate +
CC         chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-
CC         COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57704; EC=3.5.1.41;
CC         Evidence={ECO:0000256|ARBA:ARBA00023996};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC         Evidence={ECO:0000256|ARBA:ARBA00023996};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL27 family.
CC       {ECO:0000256|ARBA:ARBA00009124}.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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DR   EMBL; KE007236; EOR00177.1; -; Genomic_DNA.
DR   RefSeq; XP_009268966.1; XM_009270691.1.
DR   AlphaFoldDB; R9ADC7; -.
DR   STRING; 1299270.R9ADC7; -.
DR   GeneID; 20374015; -.
DR   KEGG; wic:J056_001063; -.
DR   eggNOG; KOG3418; Eukaryota.
DR   HOGENOM; CLU_489352_0_0_1; -.
DR   OrthoDB; 1343935at2759; -.
DR   Proteomes; UP000014064; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:UniProt.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd06090; KOW_RPL27; 1.
DR   Gene3D; 2.30.30.770; -; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   InterPro; IPR001141; Ribosomal_eL27.
DR   InterPro; IPR041991; Ribosomal_eL27_KOW.
DR   InterPro; IPR038655; Ribosomal_eL27_sf.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR10587:SF138; CHITIN DEACETYLASE; 1.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   Pfam; PF01777; Ribosomal_L27e; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000313|EMBL:EOR00177.1}.
FT   DOMAIN          302..501
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          140..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  61906 MW;  6C9EBD1C18FB42D0 CRC64;
     MPKIFKSGKV CVVLSGRYAG KKVVVIKQFD EGTKERPYGH CLVAGVERYP LKVHKQMGAK
     LIERRSKVKP FIKSINYNHL MPTRYALELE GLKGVVSPET FKEPTQREDA KKQIKKLFEE
     RYHSGKNRWF FHALRLHRKQ DETSSTSSSS PTATSTTATT TSIQSGTTGT GGTFTHIPNS
     SDIPLSSILP GMNLSGKTMS MPTTASPGQI PFSHAPPLPS STPVQAEYPE MDKIPPVDHP
     QVQEWISQID WDKVPDWSVN EGEASCSENP DSRDEAGPDQ RCWWTCGSCT ADDDITQCPN
     KHDWGLSYDD GPSPYTTTLL NYLAEQEITS TFFIVGSRAL SRPDMLRAEL VLGHQLSVHT
     WSHPHLTTLS NEELVAELGW TKKVIHEVTG LTPNTMRPPY GDIDNRVREV CRQMNLTPII
     WTTAQVDGQE LTFDTNDWKI ASGDVTTNKS YETFEKILDS SDEMDHGFIV LQHDLYQQAV
     ELAVAYVLPD ALQRQPELNL LSVIDCLQKP QTEAYIETSS NETAPSEVGA GGSSASKVFI
     SITKLSIAVA ITTLFLC
//
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