ID   A0A0D1YP83_9EURO        Unreviewed;       448 AA.
AC   A0A0D1YP83;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=NodB homology domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV11_08703 {ECO:0000313|EMBL:KIV76848.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV76848.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV76848.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV76848.1,
RC   ECO:0000313|Proteomes:UP000053599};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR   EMBL; KN846954; KIV76848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D1YP83; -.
DR   STRING; 1016849.A0A0D1YP83; -.
DR   HOGENOM; CLU_021264_11_3_1; -.
DR   OrthoDB; 1343935at2759; -.
DR   Proteomes; UP000053599; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10951; CE4_ClCDA_like; 1.
DR   CDD; cd00035; ChtBD1; 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; IPR018371; Chitin-binding_1_CS.
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:SF4; CHITIN DEACETYLASE; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 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};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00261}; Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..448
FT                   /note="NodB homology domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002237105"
FT   DOMAIN          66..112
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   DOMAIN          145..338
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   DISULFID        69..84
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        78..90
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        83..97
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   448 AA;  48831 MW;  212253A15CB3A2B3 CRC64;
     MRSLFALLSV LSLLPFLHAI SLPASWRQPS WCPGSRNASN DTQLQSALLV SGNGFAYSII
     KRQAEEPRCG PSQGNQSCGF GQCCSGTGFC GTGSNFCSVP QNCQRNYGFC DSDITPDGPD
     TEGEQRNAQG PVPYGQVIFN CTTPQTLALT YDDGPSNHTQ ELLDILQSVG ANATFFVSGI
     TNGKGAIDRT PEWINAIKRM DAEGHQIASH TWSHPNLTNS SSEDRAVDMR KNERAIANIL
     NKYPTYMRPP YLSCTTESGC LSDMNNLGYH VVENSLDSQD WAHPNNLSAM VDTFDSGLGQ
     ALPNGSMLLM QHERIPISAL NLTKYILMDI TQRGWKVSTV GDCLGDDPQN WYRTPTRTEP
     ATMAIDSCVV SSNGFCGTLN VFTNKQECDD SNGNCYTQVD DCNNANKGAA CDKMKNICDF
     QALYCASCGT MTPNISCETK DFGFTNQQ
//