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Database: UniProt
Entry: B0D3T0_LACBS
LinkDB: B0D3T0_LACBS
Original site: B0D3T0_LACBS 
ID   B0D3T0_LACBS            Unreviewed;       357 AA.
AC   B0D3T0;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   08-NOV-2023, entry version 42.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EDR11323.1};
GN   ORFNames=LACBIDRAFT_232887 {ECO:0000313|EMBL:EDR11323.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR11323.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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DR   EMBL; DS547096; EDR11323.1; -; Genomic_DNA.
DR   RefSeq; XP_001878624.1; XM_001878589.1.
DR   AlphaFoldDB; B0D3T0; -.
DR   STRING; 486041.B0D3T0; -.
DR   GeneID; 6073951; -.
DR   KEGG; lbc:LACBIDRAFT_232887; -.
DR   HOGENOM; CLU_026011_1_0_1; -.
DR   InParanoid; B0D3T0; -.
DR   OrthoDB; 325143at2759; -.
DR   Proteomes; UP000001194; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR032854; ALKBH3.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR   PANTHER; PTHR31212:SF4; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001194}.
FT   DOMAIN          151..273
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   357 AA;  41295 MW;  CC2B15B4B1D30594 CRC64;
     MSVLRAPPST VKNIIRLPPL MLTTPQLVAE HVPCTLHPSV LPSDLACELF YTMLDASRGW
     KRNKWWLFDR VVESPHRTSF YARKTDGLDG DETWQEAARY WYNGRMSEPP PVFPPVMEKA
     CKIVEDIVNE EMKKRKPFNL EWVEDDQPVW RANVAASNCY EGAKDSVGFH SDHLTYLGPY
     PTIASLSLGT RRNFSLREVI PTDERENRKA RTFNIPLSHN SLTIMHASCQ EKFKHSIPPQ
     NAIDIFRPAF PRSPGESTEP SPCRINITFR FYRPDFRPQS IPRCKCGVPT ILRPDMKNRT
     HGEADRYWWT CYAGAQNDGK GCDFWKLLDM LEEKRAPFTG FQKKNQHHQI INGQARF
//
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