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Database: UniProt
Entry: A0A0C9Y8E6_9AGAR
LinkDB: A0A0C9Y8E6_9AGAR
Original site: A0A0C9Y8E6_9AGAR 
ID   A0A0C9Y8E6_9AGAR        Unreviewed;       584 AA.
AC   A0A0C9Y8E6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=K443DRAFT_674431 {ECO:0000313|EMBL:KIK06452.1};
OS   Laccaria amethystina LaAM-08-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK06452.1, ECO:0000313|Proteomes:UP000054477};
RN   [1] {ECO:0000313|EMBL:KIK06452.1, ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK06452.1,
RC   ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR   EMBL; KN838553; KIK06452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9Y8E6; -.
DR   STRING; 1095629.A0A0C9Y8E6; -.
DR   HOGENOM; CLU_015598_0_0_1; -.
DR   OrthoDB; 383715at2759; -.
DR   Proteomes; UP000054477; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045194; MGRN1/RNF157-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22996; MAHOGUNIN; 1.
DR   PANTHER; PTHR22996:SF0; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054477}.
FT   DOMAIN          413..496
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|SMART:SM00184"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   584 AA;  61600 MW;  88C74FF57992F829 CRC64;
     MSHQPAAAGG APVVQLDHLL SPNTADPTNT PNNVKDKKSQ DPLFGPNIGS VSAGPAWTST
     MDKKIVTDEL TPDIVNGWIE KSKESSQPTT TLQALVNLKR PTLRLSPLAS VPEDPATPTP
     GDPYHQHHHG LEFEYDCDAP KCGIYVHVYL PKAHPDAPPA SPHHPFSKLL VFESVVEGGF
     ASHLTLDDGA LLELGRFEHM PAASTSSDPT GASTAPVDAL PGTKPTNGDP SPSDSSANPA
     ASSEVGPTGR QNARRRFTHF HFRRRSLNRS ISGPALAVVD AEPAAQGAKN KNGKDGENEG
     VKVTIRLAAL DKQATELASP NEQITYLHIV RLGAKPADAE EGTEDTRPWV VKVVKREATI
     GPHTFHLHEI FGLTSSPAAN HPATPVTPSS PTHTYPPAEN VQGADDDGPQ SECLLCLSSP
     REVVLLPCRH LVACKDCALN MVEFGAGGNI TQGVAEPAVP AVGGETGAAA TPGAPATPPA
     NQRRKRKAKG WFCPICRQPY SSLLRITTAP PPPLEDKDDS ETEDEAPPAE LETAETPATE
     VRSGGLLGGS LRPGFLRGLS LSRNPQQTVR ADIESTAGLG RVGV
//
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