ID A0A2N3N2Y3_9PEZI Unreviewed; 812 AA.
AC A0A2N3N2Y3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 02-APR-2025, entry version 27.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=jhhlp_006846 {ECO:0000313|EMBL:PKS06772.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS06772.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS06772.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS06772.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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:PKS06772.1}.
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DR EMBL; NLAX01001033; PKS06772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3N2Y3; -.
DR STRING; 41688.A0A2N3N2Y3; -.
DR VEuPathDB; FungiDB:jhhlp_006846; -.
DR InParanoid; A0A2N3N2Y3; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000233524; Unassembled WGS sequence.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
DR GO; GO:0043130; F:ubiquitin binding; IEA:TreeGrafter.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR GO; GO:0097039; P:protein linear polyubiquitination; IEA:TreeGrafter.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd20336; Rcat_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; IPR002867; IBR_dom.
DR InterPro; IPR051628; LUBAC_E3_Ligases.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22770:SF13; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 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; PS50089; ZF_RING_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233524};
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 338..559
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 342..395
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 511..563
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 91762 MW; 67B188210E0F5C18 CRC64;
MDDGSPPPGD TNNGASHDLE PPTAASPETP QSPSVHFAGI RSHKVRIKIE DIDDELPSLV
AYLRLGARTT KVEQAVRLFL QDPENVEDED ENSGSERPAP MINPSDTIVL YKDGQLLCNE
DLLNPPSKIH YRVYYSGETP GDLTPRLYFN SPDKRCAKIF VKNRESLLDD ITNSGLTVDG
LRNKISNKLG LADPNVVAVS ACGGMRPGPL EGGHWEIKRV QSWLCRDIAI EIIPNIQYVV
VRGCSKQYLY HPPPGKLNKE GTTVGNIKKW LRETLIPGVH RKCKSQIHVE SADILVKDWY
LELKNDSSPV PWGSLLDFSL PRGVAEAFIE EQNWLSPIKH TCVVCWDSKR GDEMVDQVTK
LCLHGPKVCI KCLQQWIKSA FLENGWERVN CPSCTEPLSF HDVRAHATKT VFERYDTLLA
KKLLSKVQNF YWCLSKGCNS GQVHLPSGRS DNSSCPKNLF QCHACGGRQC TLHGVKWHEG
RTCREYDAMN PSKSKQDKAS EATIKEISKE CPKCKRNIIK SVGCNHMTCH CGHQWCYYCR
EAWEYNEERS LVCKHKPNCP EHNSNPFFYE QLMHDPPVGH GPPPAVAATA FPAVVRPRVE
PPPMPPRALQ RAEPDPEEFR HHALPDRFHD PPTSAFSPLP RAMSQFMPPS ERHRLPLPHP
APVPAPFVPA TDLWSEDDDV HPFAPAPRMR PRETQATNHR GHRASWIPQP TTEQALSSWP
AQPRGIAPRF MVGAIDYTLP PRDHRRSLPA PEQRRNLLPG AEQRRALPAP EPRREMPRGE
RQSYVPDNAQ RRPHVYAPRF SPRQMMNRPW GE
//
