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Database: UniProt
Entry: A0A2P5IAJ6_9PEZI
LinkDB: A0A2P5IAJ6_9PEZI
Original site: A0A2P5IAJ6_9PEZI 
ID   A0A2P5IAJ6_9PEZI        Unreviewed;       654 AA.
AC   A0A2P5IAJ6;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=RWD domain-containing protein {ECO:0000313|EMBL:POS79514.1};
GN   ORFNames=DHEL01_v202097 {ECO:0000313|EMBL:POS79514.1};
OS   Diaporthe helianthi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=158607 {ECO:0000313|EMBL:POS79514.1, ECO:0000313|Proteomes:UP000094444};
RN   [1] {ECO:0000313|EMBL:POS79514.1, ECO:0000313|Proteomes:UP000094444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7/96 {ECO:0000313|EMBL:POS79514.1,
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   -!- 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:POS79514.1}.
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DR   EMBL; MAVT02000108; POS79514.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5IAJ6; -.
DR   STRING; 158607.A0A2P5IAJ6; -.
DR   InParanoid; A0A2P5IAJ6; -.
DR   OrthoDB; 4338126at2759; -.
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:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20354; Rcat_RBR_RNF14; 1.
DR   CDD; cd23134; RING-HC_ITT1-like; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 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; IPR047548; Rcat_RBR_RNF14.
DR   InterPro; IPR006575; RWD_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
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   PANTHER; PTHR11685:SF457; TRANSLATION TERMINATION INHIBITOR PROTEIN ITT1; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50908; RWD; 1.
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: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          9..154
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          189..464
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          193..238
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          316..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  72000 MW;  25EF42140838DF03 CRC64;
     MDNEDQRDVE LSTLAAIFPE IQRLDDNDPY TFVLDVPVNP TKAVTVFFPA ATEAQGLNLG
     AALEAGAATT QPDTNGVDSH ELSHLPAVRV QISLPPEYPA TKPPAAGVST QPSWLPLGTA
     KKLEDDCARL WEELGRDLVA FTYLDHVQQS ADDVFGLVSE VGALQISPEH KIAVLDYDIE
     AKRVAFENGT FDCGVCLDPK KGAKCHRMID CGHVFCTECL QSFYNNAIKE GDLAAVRCLE
     PSCAKERAVA EASNSQKRSK RKTFISPSEL LQIPLEPDMV KRYVTLKYKT ELESDKNTVY
     CPRPWCQGAA RSKKRKKPEG FELHQAEDNS DSENEEAPQA DTGKGGKPKP HVDRLAVCED
     CGFAFCSRCY QGWHGDLVVC APRRDDGELS AEEKASLDFI SLHTTPCPTC ACPAQKTHGC
     NHMICYRCQT HFCYLCSAWL DPSNPYQHFN QQPNGKIGSC YMRLWELEEG DEDGQNFFAG
     GRGGQQGPGN EREIAIEEAI IGDEGVDHQQ QPEPRPAPNE NGRRVDVERE GPLVLRIDAA
     PPAPGAARQP APVPQHRGGA HNRGRGNPAG GARQQAAQHG RGGRGMLFRP LQNQNLNLGP
     NGGVRHFIRR DRHVPAQQLR DEAGQEEVQA GEAAWIRHFI QLALNDNEDL IDDE
//
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