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Database: UniProt
Entry: A0A194VXV9_9PEZI
LinkDB: A0A194VXV9_9PEZI
Original site: A0A194VXV9_9PEZI 
ID   A0A194VXV9_9PEZI        Unreviewed;       910 AA.
AC   A0A194VXV9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   13-SEP-2023, entry version 31.
DE   SubName: Full=Putative E3 ubiquitin-protein ligase ARI4 {ECO:0000313|EMBL:KUI69081.1};
GN   ORFNames=VM1G_04192 {ECO:0000313|EMBL:KUI69081.1};
OS   Valsa mali.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI69081.1};
RN   [1] {ECO:0000313|EMBL:KUI69081.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-8 {ECO:0000313|EMBL:KUI69081.1};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CM003101; KUI69081.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194VXV9; -.
DR   OrthoDB; 251172at2759; -.
DR   Proteomes; UP000078559; Chromosome 4.
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; 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   PANTHER; PTHR11685:SF404; RING-TYPE DOMAIN-CONTAINING PROTEIN; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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          394..594
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          398..447
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   910 AA;  103829 MW;  780E70C29B2F4687 CRC64;
     MARSQYVESP RSSRRRKNPP PAPEVDWARA EDELQDSPPR RSRTDRISDR NGRDRERLMY
     RETRQDEEII MRTPDSRASS SSLRPYHSEP RRRRSTPPHS TSSSKTSMRV HHTPHPPLSS
     MTRPPISQEL YRRPSISFRE SATAGYEDED SPPETRRSQS RPRSVHLVPS APVSRHTSRS
     FATPCVSELE SEGDETDTTY DSPEEEREPR RAETARLRSR TERSRSRVEP RRTLLRRRQR
     DEVSARPEED YDEIDSRHTP SLDEEPPARP ISRSRSRSRA PSARRITQEP QDSGSDDPSV
     DDLRNRFEAR VNRRDRSQSH KQEPRRRRSE SHAGPSPTPK RSSSKRYYDT EVVSMEKPDR
     HHPPSASLRR SNTVGGSQAA ASQHHSGFSL NVSIRTECVV CMDDIRSHKT AKLKCGHRMC
     HSCLKRSFKL SITDPQHMPP RCCTADNIPL KHVEKLFDNE FKKTWNKKFT EYSAKNRIYC
     IKRGCNEFIR PEDIHHADDG RKYGRCVRCR TKVCVKCNGK WHSARDCPKD EETVRFLAQA
     KDEGWQRCFR CKAMVELKEG CNHMTCRCGA EFCMICGERW KTCQCPWFNY DTVENDRLQH
     MQIPMPARER FGGRPTVDVP PSPPRDWAPP GAIPFSGSRP RPQNYEDEVL LRRLQEERDE
     AYARRLHNYQ DYDDDREDDF LGGFGDINGI GNAGGHHLNE DYRPRPRHIA VPQPPQPPPM
     PAMPIDPAPA MFDRSGTGYV QDVNRARGVR ANSLERRLAD RFNTDLRQNP THRGPATHGP
     PPTLQSAATI SLPPMASAMA SAAVPARRHT VEAGELYADE GLRARSGGTR SVERVTASGR
     TTRPVVFDEP EEMMVPLGMV GRNKYIREPP KASNLAGLTG SGRGMDRVFE WRTHVAPGPG
     PDTASVTSSV
//
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