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Database: UniProt
Entry: A0A409W474_9AGAR
LinkDB: A0A409W474_9AGAR
Original site: A0A409W474_9AGAR 
ID   A0A409W474_9AGAR        Unreviewed;       947 AA.
AC   A0A409W474;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
GN   ORFNames=CVT24_012299 {ECO:0000313|EMBL:PPQ73329.1};
OS   Panaeolus cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX   NCBI_TaxID=181874 {ECO:0000313|EMBL:PPQ73329.1, ECO:0000313|Proteomes:UP000284842};
RN   [1] {ECO:0000313|EMBL:PPQ73329.1, ECO:0000313|Proteomes:UP000284842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2629 {ECO:0000313|EMBL:PPQ73329.1,
RC   ECO:0000313|Proteomes:UP000284842};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
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:PPQ73329.1}.
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DR   EMBL; NHTK01005823; PPQ73329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A409W474; -.
DR   STRING; 181874.A0A409W474; -.
DR   InParanoid; A0A409W474; -.
DR   OrthoDB; 2900138at2759; -.
DR   Proteomes; UP000284842; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11065; CYP64-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR46300:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-RELATED; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   4: Predicted;
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284842};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..947
FT                   /note="CBM1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019354569"
FT   DOMAIN          20..56
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          62..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   947 AA;  103177 MW;  A15B4A0DA1780E8A CRC64;
     MPTAWKPSFV ALLFSLPAFA QQPLWGQCGG IGWTGGTTCV SGAVCNRNND YYSQCIPGQA
     TTPAPAPTTS TATTPPPSST SVPAAPGSCP VLPSNPSFTA NARLPNPFKF FNGNAVTTKA
     DWDCRREEIS QLLQRYELGT LPPKPSSVTG SYSGGRLTIN VSEAGKSISF QVSISTPSGA
     TAPYPAIIAY GGMSIPTPSG VSVITFNNDD IAAQTNTGSR GQGKFYTLYG SGHSAGAMTA
     WAWGVSRIID ALSTTTGHNI DLNRIAVTGC SRNGKGALVA GAFDTRIALT IPQESGSGGG
     GCWRISDKML SSGINTQTAS EIVGENVWFS KNFEPYVRSI NNLPFDHHLL AALVAPRALL
     VIDNTSIDWL GPRSVFGCMK TANKIWQALG VADHMGVSQV GNHNHCAFPS NEQGDLDAFV
     NKFLKNQSTN TNIVKTDGAN QVGFVDSEWV DWTTVAVILL CFTLYAYIRQ RVHRGSKLPL
     PPGPPGHIIF GNKLPESFAY RKYEEWTQEY GPVFTIRQGF NITIVVGRLQ AAIDIMEKEG
     ASLADRPRNI SAGEILSGGM RTLLTPAGER FKKMRRALHT HLQPKVVAGY SPTLMKNAKQ
     LLLDIIDAPE RHQDHAKRYS ASVVLALAYG KESQGYEDPA IVAVNRCITR VGENLRPGLW
     KVDIYPFLRY IPGYLNELKA GHAEELDLFK TQLREVKVKM ERGDEIPQSF GKYLLEKQQE
     LGLNEAETAY LAGSMFGAGS DTTASAISVA ILAAACYPEA QRRIQEEIDA VIGKERAPTT
     SDAESLPQTM AFVYESYRWR PVTAGGFPHK ATKDIIWQNY LIPKGATVVG NVWAVGRDPD
     YFPDPERFDP QRWLDSNGKL REDVKSYPFG FGRRVCPGLH MATASVFLNT ALINWAFSIH
     TDPESPIDDM AFTKSANAHP MPFKVIFKPR VTKTMEGVKE MMEDYGI
//
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