ID A0A1S8VNM7_9FUNG Unreviewed; 328 AA.
AC A0A1S8VNM7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Glycoside hydrolase/deacetylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BSLG_06025 {ECO:0000313|EMBL:OON03724.1};
OS Batrachochytrium salamandrivorans.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON03724.1, ECO:0000313|Proteomes:UP000189906};
RN [1] {ECO:0000313|EMBL:OON03724.1, ECO:0000313|Proteomes:UP000189906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS {ECO:0000313|EMBL:OON03724.1,
RC ECO:0000313|Proteomes:UP000189906};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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:OON03724.1}.
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DR EMBL; LYON01001256; OON03724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8VNM7; -.
DR STRING; 1357716.A0A1S8VNM7; -.
DR VEuPathDB; FungiDB:BSLG_06025; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000189906; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10951; CE4_ClCDA_like; 1.
DR CDD; cd11618; ChtBD1_1; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR036861; Endochitinase-like_sf.
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; PF00187; Chitin_bind_1; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189906};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..328
FT /note="Glycoside hydrolase/deacetylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013386343"
FT DOMAIN 31..74
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 122..313
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DISULFID 42..54
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 47..61
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 328 AA; 36044 MW; 2E8C47768784E669 CRC64;
MVALGHLLMS AAASGLQLNN SARVSLPETQ DGSCGKVAGF QCSVGDCCSQ YSFCGSTVDY
CGAGCQPEFG LCTNVPTHTS KIVATTTKTT ITTSSDIPSS TSYPAPDPKK RAKIITGCTK
PGVFAFTLDD GPTTNVTDIL DVLKKNKVKV TFFVNGRNFA DLTTEPYISI LSRAYNEGHQ
IASHTLTHPD MKTLTADQMW HEMKDNDDLI RAIIGKSPTY MRPPYGNTND LVLNAMGTWG
YKVITWNLDS ADWDHDGKPD MIALNEAAYQ EDLKGHPLPY TSFISLQHDF VVDEVTWIQI
VINKFKALKY KFVTVGECLG DRPANWYR
//
