ID A0A2J6SLJ7_9HELO Unreviewed; 696 AA.
AC A0A2J6SLJ7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 02-APR-2025, entry version 27.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=K444DRAFT_235619 {ECO:0000313|EMBL:PMD51636.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD51636.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD51636.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD51636.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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DR EMBL; KZ613912; PMD51636.1; -; Genomic_DNA.
DR RefSeq; XP_024728540.1; XM_024871270.1.
DR AlphaFoldDB; A0A2J6SLJ7; -.
DR STRING; 1095630.A0A2J6SLJ7; -.
DR GeneID; 36579352; -.
DR InParanoid; A0A2J6SLJ7; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd22584; Rcat_RBR_unk; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 509..696
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 154..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..251
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 78129 MW; 55A9DBF5A7AE0DD4 CRC64;
MDATEEEVKS VLTEALNGYL KIILLEQTLH ETSQPRQGKG IETEIDIARV QYFQSRTHVT
ETCLQFSGRI ASNVRAWAAG EPEKVERKVA MESLLDAISP SVHHFLLPAK EDDESFLNPF
TGQWIQPTNS SRSAGPSNWH GSAAQNDFDY LKVETNTPLP SKGKEKEGTK KAPPDEVENL
IDFSTLDVAE SFNPPQFPDF FGLVHGTSTA TPYIATWRDN TQPTSNPFSD QYQSYESSGP
DTPRTLTPPT LHSQCNSRPH TPTTNTISFE EDVAAVQKRQ SEWAQDDYNQ ELLPVDTTLT
RQFDLDFPPV DSSLISQFEI DYPPIDTSFS LDFLTAQNLQ AEYDTELQVQ ESYARQVQHL
EKQQSPNFDQ DLAEARRLQS EWEAQDASTQ QDWKYWQAKA QQEDQQMAAQ VEFARGVARL
DEEMAEDIER DKAAALAAQA QWEAAAMELE AQVKRAVEEA ERREAEDRRR EAEEEAARRA
EEERREAEDR RREAEEEAAR RAEEERRARV AECVSCTEEG EKSDMCMLNC EHGYCRGCVA
EAIKSALKSR APFKCCNATP PMPLLSRFLP APLLASYNNL LLELSTPNPK YCSNAHCSLF
LPPSSIIGPL ATCSSCRTRT CALCSGAEHA GVCQQDVAGQ KVLALAGRKG WKICPNCKSV
LERTEGCLHM TCRCGAQWCY SCLANWGSCQ STCPRR
//
