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Database: UniProt
Entry: A0A2P5IAJ3_9PEZI
LinkDB: A0A2P5IAJ3_9PEZI
Original site: A0A2P5IAJ3_9PEZI 
ID   A0A2P5IAJ3_9PEZI        Unreviewed;       714 AA.
AC   A0A2P5IAJ3;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   02-APR-2025, entry version 24.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=DHEL01_v202081 {ECO:0000313|EMBL:POS79521.1};
OS   Diaporthe helianthi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=158607 {ECO:0000313|EMBL:POS79521.1, ECO:0000313|Proteomes:UP000094444};
RN   [1] {ECO:0000313|EMBL:POS79521.1, ECO:0000313|Proteomes:UP000094444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7/96 {ECO:0000313|EMBL:POS79521.1,
RC   ECO:0000313|Proteomes:UP000094444};
RA   Baroncelli R.;
RT   "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL   Submitted (SEP-2017) 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:POS79521.1}.
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DR   EMBL; MAVT02000107; POS79521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5IAJ3; -.
DR   STRING; 158607.A0A2P5IAJ3; -.
DR   InParanoid; A0A2P5IAJ3; -.
DR   OrthoDB; 9977870at2759; -.
DR   Proteomes; UP000094444; 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   CDD; cd22584; Rcat_RBR_unk; 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   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094444};
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          201..403
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          205..250
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          400..460
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          595..640
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   714 AA;  81255 MW;  528205B62F77ADFE CRC64;
     MGSLATQLPT AQNASPADPV ITQAPHELDD LSYLVEVLRS VETEQHIEQD LINRAAELGI
     SLPPPPSSPS EDLSCPGPES DAALSSTHAR NTSSGSDNTA DTAMTSNPPS RPGTGAGQRE
     NPPPLPSSRA RSRSLNFSTY DKYLAQLEPN LCQPKILKRP PTPTDNTPSL FSVSTRKSYI
     SIKNGLKAKV RWKRQSHTPS TTLSCICCRD DFNKQNDLQT LPCGHTYCGN CLRIMIEQST
     TDESKMPPRC CTQPIPSTTI RNLLNRDEQQ LFLKAVQQYS TPWEARIFCP NPCCNEFIPP
     RSRIDPKHPF DVVCRECRTR VCIWCKRDAH PVGQDCPNDH ELDQVLRMGE KSGWRRCYKC
     RTLVELTQGC THMTCRCKAQ FCYICGAVWD PAVGCPNFCN GEEELERRRM EEAAREAELE
     AEKAAREAAA AAAERERHQA EKRTQACEEF KRLKEEQEDE KWRFRTFERK TKWVMWTRHE
     ERKHKLNEKY SDQIDKMKER HAKTEQHLEE RQIAAEIELR ASLEQAEKSV RIRVKHMEAY
     CKALGRSSMS GAGSDMPPRV ITERHLRELG QQHNALEGMA RLHQAKINVL RDRQAKRMEE
     LLERQESELQ KQREKRDQEM EDLVAELANE EDALAKVFKD RKGRLVRRWE LAIEILRVTK
     EKETGVKFAP MPVPAWAAEA PSCVDGPGPE DDGLAVVHEE EEKRGDTEAT AIKS
//
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