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
//