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Database: UniProt
Entry: A0A8S9B626_9HELO
LinkDB: A0A8S9B626_9HELO
Original site: A0A8S9B626_9HELO 
ID   A0A8S9B626_9HELO        Unreviewed;       563 AA.
AC   A0A8S9B626;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   02-APR-2025, entry version 9.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=EG329_002838 {ECO:0000313|EMBL:KAE8442805.1};
OS   Mollisiaceae sp. DMI_Dod_QoI.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae.
OX   NCBI_TaxID=2728926 {ECO:0000313|EMBL:KAE8442805.1, ECO:0000313|Proteomes:UP000423986};
RN   [1] {ECO:0000313|EMBL:KAE8442805.1, ECO:0000313|Proteomes:UP000423986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DMI_Dod_QoI {ECO:0000313|EMBL:KAE8442805.1,
RC   ECO:0000313|Proteomes:UP000423986};
RA   Lichtner F.J.;
RT   "Venturia inaequalis Genome Resource.";
RL   Submitted (JUL-2019) 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:KAE8442805.1}.
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DR   EMBL; VXCB01000141; KAE8442805.1; -; Genomic_DNA.
DR   OrthoDB; 1431934at2759; -.
DR   Proteomes; UP000423986; 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; cd20335; BRcat_RBR; 1.
DR   Gene3D; 1.20.120.1750; -; 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   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SMART; SM00647; IBR; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000423986};
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          304..563
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          308..362
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..488
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  63873 MW;  B002EF86519FA61A CRC64;
     MSKMKRLLRS FSKRNLRNEE ENEVDSSPRT ENFQRRPVWS IDEEEPWSFN RLNDGEAAEQ
     SSSRNAPQVS GFEQYRKDMN IPPSRTPQKK PDTRFIHELE AESNTWAQGH SSSSSEANDP
     LQAIYGTADI QFFGSQYGLG AAKVESPDEI ASAYHDQMVE QVAALNFYEE MMRNAAPDIQ
     RAATGKAETL WGNTLKSAAT AEPDLASTSE YPASRDIQDD QNSQKPEITK TGMFGVADAE
     EFWRTVMSIA TTPDTPAVPA AESSKAAALN SVPQELPTEV HSVAIPSFFP ATATIPTDTS
     AERLPTNCII CIEDFTPDFS APPWITHACT HPPSVCLPCL AKCIKNDLDN KIWNQIKCPE
     CDVTLVYEDI KRLADPETFV RYEELSFRSA VSSDSDFIWC PSPSCGFGQL HATGQKHPIV
     RCLKCGFRSC FKHGVAWHER LTCDEYDEML QNPIGFKSAL EREEEERIAE EERQRQRHEA
     ELARARAQQE AEAERRRWEE MRREEAEQRK REEAERQRQR EEVLRKQMEE QASMSTVQNT
     TKRCPGCSWP IEKNRGCAHM TLS
//
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