ID S8AC19_DACHA Unreviewed; 395 AA.
AC S8AC19;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
GN ORFNames=H072_7634 {ECO:0000313|EMBL:EPS38651.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS38651.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS38651.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS38651.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:EPS38651.1}.
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DR EMBL; AQGS01000538; EPS38651.1; -; Genomic_DNA.
DR RefSeq; XP_011113383.1; XM_011115081.1.
DR AlphaFoldDB; S8AC19; -.
DR STRING; 1284197.S8AC19; -.
DR eggNOG; ENOG502RS04; Eukaryota.
DR HOGENOM; CLU_015101_4_2_1; -.
DR OMA; WIQQYSN; -.
DR OrthoDB; 1012174at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd01846; fatty_acyltransferase_like; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR45648; GDSL LIPASE/ACYLHYDROLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_4G14700); 1.
DR PANTHER; PTHR45648:SF22; GDSL LIPASE_ACYLHYDROLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_4G14700); 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..395
FT /note="CBM1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004560375"
FT DOMAIN 19..55
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 63..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 43140 MW; 0513AD14E69565E0 CRC64;
MSLTLVVLYL AFAFGTAIGQ QTAYGQCGGN GWTGPTTCVA GYTCTYQNDW YYQCVPGGAT
TTKTTTTTTR TTSPTTISTS STSRTSSSTT RTTSTTTTTT RTTSSSTRTT SSSASSTPSS
GSTIQHWFVF GDSYTYTGFN AWGAQPSTSN PLGNPTFPGD TTSGGANYVG LAITTYKKST
LFAYSLGISG ATVDPTLAFP TQGRALDVEM NTWIQQYSNR ATVGVQWTGD NTLFSMFFGV
NDITVTMSRT DMDTYTDKIL ASLMNQTNTL YNYGARKFMF INCPPVDRLP AVYGNAAIKT
NVARWNSRLL SFAADFKNSH AGGLNWEQSS YVVYDTWTDY NKVLDNPTAY NLNSNVQTPS
TDQSYFWRDS YHPNVKMHDV MAQSLSALWR SAGWW
//
