ID A0A433P9H6_9FUNG Unreviewed; 560 AA.
AC A0A433P9H6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 02-APR-2025, entry version 20.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE Flags: Fragment;
GN ORFNames=BC937DRAFT_94214 {ECO:0000313|EMBL:RUS14191.1};
OS Endogone sp. FLAS-F59071.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Endogonomycetes; Endogonales; Endogonaceae; Endogone.
OX NCBI_TaxID=2340872 {ECO:0000313|EMBL:RUS14191.1, ECO:0000313|Proteomes:UP000278417};
RN [1] {ECO:0000313|EMBL:RUS14191.1, ECO:0000313|Proteomes:UP000278417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FLAS-F59071 {ECO:0000313|EMBL:RUS14191.1,
RC ECO:0000313|Proteomes:UP000278417};
RX PubMed=30485448;
RA Chang Y., Desiro A., Na H., Sandor L., Lipzen A., Clum A., Barry K.,
RA Grigoriev I.V., Martin F.M., Stajich J.E., Smith M.E., Bonito G.,
RA Spatafora J.W.;
RT "Phylogenomics of Endogonaceae and evolution of mycorrhizas within
RT Mucoromycota.";
RL New Phytol. 0:0-0(2018).
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:RUS14191.1}.
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; RBNK01007264; RUS14191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433P9H6; -.
DR OrthoDB; 442087at2759; -.
DR Proteomes; UP000278417; 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; cd22584; Rcat_RBR_unk; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 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; 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 SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000278417};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 187..418
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 191..258
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 106..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..123
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..140
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..560
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 560
FT /evidence="ECO:0000313|EMBL:RUS14191.1"
SQ SEQUENCE 560 AA; 60859 MW; 958F844788553A7D CRC64;
MSTLLIHPPP STEIRVHNPR ISSSRRKKRI GGHSTLLEQF KMLAEDNIGS IDDAFCEIAV
ILGPDGFMLD DSVIEGFLMK WIEDIEDDQG DALMEHVFEL LAIPTPGKGK KKARTRPTIR
RSRPPLLLAS SSSRSSTSSH SHSKGKSVAR LTRIPTLHFE DQPISLSMLE EHEEAVRLLA
EARQQRPTYE CGVCFDSFQL AEDVAGAVAG AESSSSGGSA VVLGTLLPCT HGFCAGCLSE
FLSHKLKEQN LTFPITCPGF KCTGTVSDTV AERVLGRDGM DAWWQKVVES GLQNVIYCPH
NGCGAPMELD PDVKKQTGPV ECWECHRGFC GNCLATWHTG LTCKQYQALP PSQRNPEEVA
LLNLATSMSW HRCPKCRALI ERNQGCNHMT CRCKAEFCYR CGNNWVNNMC SVNCHNWNDT
QLQEERMRLG IKYFGEDAEE AEKAKGAEKP KLKVAPKINT RATSASSSAA GPSTTVRALS
NATRAHTVKT ATRRPVVANP ELHARVSAVK RAHQLPGPTI VGVGRANNAS SAAPRERARS
GLGAEGTARA GARAGARAGA
//
