ID B0DFU5_LACBS Unreviewed; 462 AA.
AC B0DFU5;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDR06405.1};
GN ORFNames=LACBIDRAFT_294647 {ECO:0000313|EMBL:EDR06405.1};
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:EDR06405.1, 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; DS547108; EDR06405.1; -; Genomic_DNA.
DR RefSeq; XP_001882777.1; XM_001882742.1.
DR AlphaFoldDB; B0DFU5; -.
DR STRING; 486041.B0DFU5; -.
DR GeneID; 6078553; -.
DR KEGG; lbc:LACBIDRAFT_294647; -.
DR HOGENOM; CLU_037984_2_1_1; -.
DR InParanoid; B0DFU5; -.
DR OrthoDB; 140984at2759; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16494; RING-CH-C4HC3_ZSWM2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR007527; Znf_SWIM.
DR InterPro; IPR039903; Zswim2.
DR PANTHER; PTHR21540:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZSWIM2; 1.
DR PANTHER; PTHR21540; RING FINGER AND SWIM DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF04434; SWIM; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000001194};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 253..285
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 354..404
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 17..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 50225 MW; 2C9E32C20CA676B1 CRC64;
MVLSKRKANG EFVAWVSKSS SAAGSSPARA SSPLVSVQEP PAKRQRQAAG NKINDELTLP
SVAGSSTRTT YSTTSESSFT ARAAPLPSQR QRRPKFNDEL TLPSISAPPV QATRVLPTPS
TSSLSAHATA PPTKRQRKAV NKINDELTLP STLAQSRGLP SGSSQPRAAA SSSQPSSAGP
SSSQVPPKGR KKKDPNAPVP EKRGAKFKAK CPQNILDRVE RVREQRFFMI DRRRNEGELR
EEFSVLGSTG NVYTVTIDKT PRCNCPDALK GNHCKHILFI LIKVLQVSQV SGHWYQKALL
TTELESIFAE APLAPNDVTN PRIREAHDRA LGRSTAVTPA PQNKKRIPGK DDDCPICYDG
MHGVAETALV FCEECGNALH KECFGQWQTT SVNSGKELNC VWCRARWVVP GTAAGVGVQR
EGGYLNLGAV AGISPARDTS TYYHGPRRGQ RYYGAQEYYD DF
//