ID R9P481_PSEHS Unreviewed; 302 AA.
AC R9P481;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Chitin deacetylase {ECO:0000313|EMBL:GAC96166.1};
GN ORFNames=PHSY_003746 {ECO:0000313|EMBL:GAC96166.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC96166.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
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}.
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DR EMBL; DF238801; GAC96166.1; -; Genomic_DNA.
DR RefSeq; XP_012189753.1; XM_012334363.1.
DR AlphaFoldDB; R9P481; -.
DR STRING; 1305764.R9P481; -.
DR GeneID; 24109032; -.
DR eggNOG; ENOG502S2CW; Eukaryota.
DR HOGENOM; CLU_021264_11_2_1; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000014071; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR PANTHER; PTHR46471:SF2; CHITIN DEACETYLASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000014071};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..302
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004487456"
FT DOMAIN 82..267
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 302 AA; 33449 MW; C12D3940A82017F1 CRC64;
MRFSSVLAAA AVISAAMLTP ATASPTSMST LPDTISENVR RELAALPSDD YTLFERNAGP
SHKLSKRAAQ LNGIQTGCTR QNCLSITFDD GPYQWENKLV DMFANAGNQK ATFFVNGFNW
RCIYDDASVK QLRNTYEKGH QICSHTWSHP DISKMNNQQL DQQVQLVEDA LWKILGVVPA
CIRAPYGSIR SDQVKYLNDR WGLVVVGWNY DTKDADGAGT QAGLKLYKNL RQPAQAIVLN
HETVQGTIDT VMPQAVNIVR QNGYTSHTVQ RNLGFNPYKV VGKYQNRDSS WTCDGTPAPG
AN
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