ID G4T9R2_SERID Unreviewed; 391 AA.
AC G4T9R2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Related to deacetylase {ECO:0000313|EMBL:CCA68046.1};
GN ORFNames=PIIN_01913 {ECO:0000313|EMBL:CCA68046.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA68046.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA68046.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA68046.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCA68046.1}.
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DR EMBL; CAFZ01000024; CCA68046.1; -; Genomic_DNA.
DR AlphaFoldDB; G4T9R2; -.
DR STRING; 1109443.G4T9R2; -.
DR eggNOG; ENOG502S2CW; Eukaryota.
DR HOGENOM; CLU_706191_0_0_1; -.
DR InParanoid; G4T9R2; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000007148; 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.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..391
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003468601"
FT DOMAIN 31..138
FT /note="NodB homology"
FT /evidence="ECO:0000259|Pfam:PF01522"
FT REGION 316..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 43768 MW; 05969E87A115403E CRC64;
MLTLLTLLFF TIQGSQAAQD VYTLCKHGFG YTWDDGPWIY HQEILDSFNA VNGTTTFFMN
GDNYSCIYDE DNVRRLRATF ESGHQIGSHT WSYIDMEIQR LDEAFIRILG VKPRFIRPPF
GDLSEHVITY IRKKHHKYIV MWSDDSLDSV GGTAQDSYNF YKTFAIDRPD YTGLTLSHET
SDAGIQALRN GTVNVLANAD INLLSVAQCV DMEPYEYFGG YQERDASWTC EGSWTPSNFS
TLTRTSMPSR TTMVSWTRSI STETSRTSDV FTEPPLPEGT TPVQITSLTR WDVSSSIPIT
PYSSWMTFSS TPTAKWTPDA TATPTPTPTS DIATEAPLPE GTIPTPISSF TEEPDLPEGT
EPTILFSMTR VEVATPTDTS TATRCTPRYS S
//
