ID A0A0D7BVB3_9AGAR Unreviewed; 870 AA.
AC A0A0D7BVB3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 02-APR-2025, entry version 53.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CYLTODRAFT_416388 {ECO:0000313|EMBL:KIY74129.1};
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:KIY74129.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY74129.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY74129.1,
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; KN880432; KIY74129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7BVB3; -.
DR STRING; 1314674.A0A0D7BVB3; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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; -; 1.
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; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; PF13923; zf-C3HC4_2; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000054007};
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 31..58
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 107..134
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 658..870
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 662..703
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 31..58
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 107..134
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 97552 MW; 01BECBD96775DB92 CRC64;
MSRITPGQPS DAVPIPQAVS TQAHAEKHPH PWSSQLCWGW EHDWCPEGWQ CQFVHGDLQY
DSPLPEPARL PELDEARNSD ESISLASDSD ATKVEEPPPP KVRHPRPRLN EVCRKARRKQ
CPWGYKCHRI HENLEYDDPV DVCSPDNETV ALQNDKPPSP SPSPIPVEPR PIPKPEWSVT
IHEHIRLKLD HGFIIQDIQT GFETAWLYID GLPPTIREST ILTLLTPHGP AEIKSVSRRD
GSALARALFE DHVDARNAAV SLDGTKQFGG RTIHACLSLT PEASGGNVRD TTVVIEWDAP
SVTAYGGFRT LEQAQTAVAS TRLPFRERNV RAAIFEGMPQ VGMYTVKYWN LPVEVYQDKD
ALEELGAPRD LMWDLLTYKS DKEAIALVRR ILGYQFDVKE WEPVEGPYMD GIIQVYASFE
SPAVAKQAAE HMHLRKPAAI KGLKLRARHL KNLVFRVNSR VFTRIRGDLC DLRDALTSKD
DKLVIVPRTG DYQIRLTSTD MKQLGKMKKD FDAVLRGDTV VMDGKAAWDK FFEYPAGIIW
AKDLRRQYPS LDFYFNVPLR RITLRGPVHL RAKAKEDIIF QIKKLRSRTC TTINIPGDLV
AHFVAKQFPR LREELGAANI HMDLWTRTLV VHGSAHMAST ARNAVQAVRA VRRPSSTTRS
SCPICFEDVQ TPVLFRCGHA HCRGCLREYL QAATEARFFP LTCLGGGGQC TEAFPLGCAK
DILTQGEFEG VVHAAFSAHV AAKPKEWHHC PTPDCPQVFR TAPPGTMLQC PECLTRICAA
CCGESHDGEP CAEDDSDDEQ AFRKWKDSAG VQACPGCNVD IERSEGCNHV TCIRCNTHIC
WECLATFPRG EGIYDHMRSQ HGSIGLIPFF
//
