ID A0A0D9NTF2_METAN Unreviewed; 461 AA.
AC A0A0D9NTF2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=NodB homology domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=H634G_07038 {ECO:0000313|EMBL:KJK77299.1};
OS Metarhizium anisopliae BRIP 53293.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK77299.1, ECO:0000313|Proteomes:UP000054544};
RN [1] {ECO:0000313|Proteomes:UP000054544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA Ash G.J.;
RT "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT comparative genomics of Metarhizium species.";
RL BMC Genomics 15:660-660(2014).
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; KE384738; KJK77299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D9NTF2; -.
DR STRING; 1291518.A0A0D9NTF2; -.
DR Proteomes; UP000054544; 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; cd00035; ChtBD1; 1.
DR CDD; cd11618; ChtBD1_1; 2.
DR Gene3D; 3.30.60.10; Endochitinase-like; 3.
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:SF2; CHITIN DEACETYLASE-RELATED; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00270; ChtBD1; 3.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 3.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 3.
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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054544};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..461
FT /note="NodB homology domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002341355"
FT DOMAIN 30..74
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 107..303
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 360..406
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 416..461
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DISULFID 40..52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 45..59
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 379..393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 435..449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 461 AA; 50512 MW; 0D55F9C41F5A3D60 CRC64;
MTPKLGLLLA VYFQSLLAFR FNRELVANEK AMCGPGEGSC KMGSCCSEMG FCGTTAEYCS
GSQCQLDYSH TCDTLVPPDG SDTSEIPRPR VGKVPYGPMI TSCNNPGMVA LTFDDGPYIY
TTELLDLLAA HEVKATFFIT GDNRAKGHID DPATEWPSIL RRMYNAGHQV ASHTWTHRDL
TQVNETVRRA EIIHNEMALR NVLGRIPTYI RPPFLECSTG SGCEETLGDL AYHSISANLD
TKDYMYDDPV LIQRSKDRYS STLSTNSKEN SYIVLAHDVH EQTVHNLTEY MISLARERGY
KLVTVGECLG DPEENWYRSA ETSSNMARTV GKRNLCSGPA KPQVTSVSPP RNTTTRISPN
QRCGGSTGYI CPGSGFGDCC SHWGYCGSTP EFCGTGCDND FGDCDPSPQR VLDTTNGLCG
ARYSATCLHF AGKTCCSKYG YCGSQVEHCG EGCQDKYGHC D
//
