ID A0A0D7B8A1_9AGAR Unreviewed; 910 AA.
AC A0A0D7B8A1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 02-APR-2025, entry version 55.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CYLTODRAFT_398670 {ECO:0000313|EMBL:KIY66480.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY66480.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY66480.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY66480.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KN880553; KIY66480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7B8A1; -.
DR STRING; 1314674.A0A0D7B8A1; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043130; F:ubiquitin binding; IEA:TreeGrafter.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR GO; GO:0097039; P:protein linear polyubiquitination; IEA:TreeGrafter.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd22585; Rcat_RBR_DEAH12-like; 1.
DR CDD; cd00590; RRM_SF; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR051628; LUBAC_E3_Ligases.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_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; PTHR22770:SF13; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF14608; zf-CCCH_2; 4.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; CCCH zinc finger; 3.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50103; ZF_C3H1; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
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 2..29
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 38..65
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 85..112
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 114..140
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 239..314
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 693..905
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 697..748
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 2..29
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 38..65
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 85..112
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 114..140
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 138..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 910 AA; 100281 MW; 45E33C087A8BECAB CRC64;
MSVSQLICPY FLQGKCMYGD DCRQRHSLPS TITKPPPARK IMACAFYSKG TCTKGDKCPF
FHPTSQAQDS WRRAPTSQET PKTSTGAFKP CAFYLKGRCT KGDTCPFPHT GGVISQPPCA
YYLAGRCRYG AQCSASHDAP SSPVSSSSPT PPSPLFRTYA PSKSRAIPIR SQPAQETTTK
SRNPNTTKGN AQDGIDESLA AASPTETPLV EHEMTLSHCG VVFTAGARVK EVVTPFESCT
LIVANLVEEE TQASLIRVFD PFGSLQTIVL LRDRDTAMAR VTYRTAAEAT SAIHGLRGSQ
YQPKMDLKVV KSGDAVLRST KVKLSWYAPK RIGWAHYKTI ARARENAARL DGTKFNSTTI
KATFQTPSFR QHTSFSVELR GLPSNTTETH LARFCRSETV ALKPMGYDRD TSLLDVQSQL
QEVGPLETFD ALPVDSTKSK IVVFAQFAHS EHAEAAVARL HNSKQSYLNH SPMWLERIHA
VKYTVSIGLL SAIRDPLEVL AATCEDCKLR FYEPQADAPQ ESAGIATIRL FSANAKALGV
AKRQLEKLLD GERLVDHSGM QVWDEFLVEV TGERFLHFIE RIHGVYVKCD KRNRVVHLFG
GVNGGLEEAR EAILERLAEL KTSSTEIPVE RSVLAWLMRG GMDVLSERFG HEFGTVNIVR
RILVVKPDIE VKEVQAAIDN RGRAVAVSNA QSDSACCPVC CSDVDAPYTL QCGHAYCKDC
LTLMLSTTSS AAPSVACIFE DSECRSCHSN IDLSVVRELL TPEQERTLFE TSFRSYVHSH
PNDFKYCPTP DCGVIYRPGD EGTVLSCPSC LDKICAACNT QFHEGLSCSE YRDHREGGER
SFRQWKAANQ VKDCPSCGAS IEKVAGCNHM TCLSCQTHMC WVCLKTFAAS EVDSEDGVYA
HMRRVHGGIQ
//
