ID A0A8H7CZI0_9AGAR Unreviewed; 992 AA.
AC A0A8H7CZI0;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 15.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=MVEN_01053000 {ECO:0000313|EMBL:KAF7353681.1};
OS Mycena venus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Mycenaceae; Mycena.
OX NCBI_TaxID=2733690 {ECO:0000313|EMBL:KAF7353681.1, ECO:0000313|Proteomes:UP000620124};
RN [1] {ECO:0000313|EMBL:KAF7353681.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCC161011 {ECO:0000313|EMBL:KAF7353681.1};
RA Tsai I.J.;
RT "Mycena genomes resolve the evolution of fungal bioluminescence.";
RL Submitted (MAY-2020) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF7353681.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JACAZI010000008; KAF7353681.1; -; Genomic_DNA.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000620124; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; cd22585; Rcat_RBR_DEAH12-like; 1.
DR CDD; cd16449; RING-HC; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.1370.210; -; 1.
DR Gene3D; 3.30.70.330; -; 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; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR041367; Znf-CCCH_4.
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; PF18044; zf-CCCH_4; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 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; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:KAF7353681.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:KAF7353681.1};
KW Hydrolase {ECO:0000313|EMBL:KAF7353681.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleotide-binding {ECO:0000313|EMBL:KAF7353681.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000620124};
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 4..31
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 92..119
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 684..894
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 688..727
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 4..31
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 92..119
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 31..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 155..182
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 61..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 111267 MW; A6B44CB5E9FD4FB0 CRC64;
MPSAAKSRAC KYFQQGRCTH GDNCRFTHQI EDGALPLPPR VNTTHKQRKR DPGPDIPGPS
TIPNERASIS VSTTAQSEPP SLLSPQTRSR AKRSELPCHA WRDGHCPKGA KCWYAHDPQV
QEAERLRREH VARVAEQRAL EMERQRTAWL ARLPEQEATE RARQNELEAR KAEIRRKEAA
QTLQHIVLGT TLVTYSAGIS IQQIVTGFDA CRIQIRNLPL DATHDEIKAL FTQQGVDQAR
LFITGIKELP DKHLEATLIT GSEEGGAIAA GLEDIEFRQE RLHFEVTENT RSDGMGSATS
KDSDTLTLSW RAPSNSVVVT FSSINEATAK VKELNRQICD GRRVRVEMNQ PPPGCVRGAD
WQRAVKISGL PAFISPQTVT QFTGSYLIKF LKPISYDVGS GLRLLRLNME RVAGGELKSF
DVVAQDDVEG NITVKARFDS WETAKRVQDS LAGRQVYLGG CFLRLWLPNP LQYIISIPHR
QYQAQKRMWD SLTGSEPGGS TSNKTAYVRI FPTQNGKVQI KVLGEDKKAV GSLKVRVENL
VGGEQLSVGC WHRSFKTPAG TQFLNSIFDR TGAYARADWK LGVVKVYGDT ASVDQARDVV
KAEVDRLDSL EWSIFLKKQS IRFFVQRGMA ALKEALGDDN ATLVISPRAS KIVIRGGEDA
RQILTRLIDE SLEEAAGSIQ RTMTGASCPI CYDEISHPVT LGCNHTYCMG CLRHYLSTAA
DSFPLTCLGN EATCETPIPI PTIEQFLPAS QFHQLLEISF LRHIERHPQE FKYCKTPDCN
QVYRCSPIPT PITCPSCFLT VCSSCDEEAH EGISCADKRL QSDPGDQERR NDEWARARGV
KRCPNCSVWI EKTEGCNHMT CKCGSHICWV CMGVFDGGQI YEHLNSDHGG FFTVPPEEPA
RRYLEADDEA LARALARQEE VRRQQEQAFA RRRLAIIEEA RRQETALRQE MVYRQEVGRQ
RQQTLYQEQR RAAAATAARR ERQESGWGCV VM
//
