ID A0A166Q7X8_9AGAM Unreviewed; 1102 AA.
AC A0A166Q7X8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 02-APR-2025, entry version 47.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=FIBSPDRAFT_781676 {ECO:0000313|EMBL:KZP26858.1};
OS Athelia psychrophila.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Athelia.
OX NCBI_TaxID=1759441 {ECO:0000313|EMBL:KZP26858.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP26858.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP26858.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV417512; KZP26858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166Q7X8; -.
DR STRING; 436010.A0A166Q7X8; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 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; IPR027370; Znf-RING_euk.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
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 Pfam; PF22191; IBR_1; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076532};
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, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 41..63
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 135..163
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 776..987
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 780..822
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 41..63
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 135..163
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1002..1029
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..221
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 123104 MW; 431032A305824F3A CRC64;
MASEAPTGKP QVALPNNRTR PGRNNQMQHV QATDDLKLEG KCRFFMQGHC KFGNLCKRSH
GDPPGEFITS PTVRMPTDVS QTQVPHHASG TSATSSNAPG QSTTSSASTL LRPNATTTTT
TTVHSSASPG TIPPKQAKKA CFSWAKSGTC QLGSKCRYDH NANAAQRAQE DGARRAAQAE
VRRAREAQQE EARQKEARRV RQVEQEQEAA EAALKAQQAQ EKAARQAEAR RVREARQEEA
RRARQAEQER EAAEAALKAQ QAQEKAARQA EARRAEQEAR MVELAKEEAA MTMQHIVLDF
TVVTFSAGLA IQDVLLGFES CRITIKNLPI DATIKEVSEL FTQQGIEASR FHVLGLARTP
AGKQEAFLIG HEDLKMVAIA LEEVDFRQDR LSFEIMGHSG GDGMRATALD ANTLTLTWRA
PSVAYVVTCV DGAQAQAKVR ELDRKICRGR RVKTQINQRS AGRQVLILGF PPEVTDQEVM
MMVGSAQVER RKPITFDTTQ AAELIRRYID SIPGVQITRF ERVIFDSMGG TYSARVHFGS
WTQTRDAFHR CDQQRLVFIG NSTFCWLRLP DPIQYTISIS GPQYRAQRKS WDDLLVTVRD
KEGLTLSIAP RDRMHLIRVG GEDKKVVGSL KVRVESIAAG EKLEGWHPSL SQKFMDRVLQ
DTGALLRIDR RLRAVKVYGE RGSIEAARAL VNRELALLES QEQTILLRRQ SVRFFVTRGL
AILKEELGDE NATLVVSSIP AKIIIKGGDA ARHTLSRLIE ESLDASNIVP RTGETGEAIC
PICYDAVTLP IKLGCGHTYC SACIRHFLTS ASTFPLVCMG DEDKCHAPIP IPVVQRFLPI
QQFTHLLETA FIAHIDRHPQ DFKYCTTPDC RQVYRCTISD TASIVHCPSC LSSVCSVCHE
EAHEGMTCAE RKLNNDPEEQ ERLNDELATQ SGFKKCPQCA VWIEKTEGCN HMTCKCGAHI
CWVCMGIFNA GSVYAHMDTA HGGMYEANGN RAEPLFQPGA FAEQQEALRQ IALRRAQLAQ
QQRHEAEDAQ HRVAQQHLYA RQLRERDAAR IQDEARRAEL FRRMEEYRRA EEVVLRREAT
TRRQAQEQQR KEEGGGWGCV VM
//
