ID A0A0C3KX76_PISTI Unreviewed; 610 AA.
AC A0A0C3KX76;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=M404DRAFT_992399 {ECO:0000313|EMBL:KIO14147.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO14147.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIO14147.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIO14147.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., 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:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
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; KN831945; KIO14147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3KX76; -.
DR STRING; 870435.A0A0C3KX76; -.
DR HOGENOM; CLU_015598_0_0_1; -.
DR InParanoid; A0A0C3KX76; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000054217; 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:UP000054217}.
FT DOMAIN 416..512
FT /note="RING-type"
FT /evidence="ECO:0000259|SMART:SM00184"
FT REGION 215..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 65968 MW; 23E7724CF09A21F0 CRC64;
MSSLSAWYNN QYSTWNRTRR LQAPQFLART DTRTSRTATA MARTGTRDAV VINMGASDRE
SKQDTLFGPN IGVVNTTIPW AQSVTKRTSE DSLSPEVIKS WIAKSKQPSQ PTTTLQALVN
LKRPTLRLVP LAISPDDDDL GHADSRHHHG LEFEYDCDAP KCRIKVNVIL PADHPLSENV
DTRGFSSIPV YESVVDGGFG NILKLNEGAT LELGRFEQTS RNNRPSTSAQ PAASDSHRPA
ETTESSSSDS DRADRPKKRF SAFQFHKRAM NRRASGPALA VVDADHTQTS ENENGRGRHA
NEDMKDGVRV TIRLSALDAD GIDTAVANEQ VTYLHVVRLG APPPDGEDDT RPWVVRVVKR
EAIIAHYVFQ LHEIYGLSSR STVSHARASS PTSGAHTYPP TSATTASAHE ELSSECLLCL
SAAREVVLLP CRHLVACKEC AINMVEFGAG GTIVHNDDAT NNNSPTTNNS DGGGSPATSA
VATNSVPASA PSAVPQNPRR KRKAKGWFCP VCRQPYTSLL RISTIPPTKD ISDDDNHTMD
HDDGDGSDLE PEGEHGRAPT NSNPLSSSEN AAPLSTGGSG VLNTLRSNLR RNVCNDETLP
PDVERGVVAA
//
