ID A0A8H5MQU5_9HYPO Unreviewed; 803 AA.
AC A0A8H5MQU5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 14.
DE RecName: Full=Ariadne-2 protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPHYL_12377 {ECO:0000313|EMBL:KAF5539001.1};
OS Fusarium phyllophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=47803 {ECO:0000313|EMBL:KAF5539001.1, ECO:0000313|Proteomes:UP000582016};
RN [1] {ECO:0000313|EMBL:KAF5539001.1, ECO:0000313|Proteomes:UP000582016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13617 {ECO:0000313|EMBL:KAF5539001.1,
RC ECO:0000313|Proteomes:UP000582016};
RA Kim H.-S., Busman M., Brown D.W., Divon H., Uhlig S., Proctor R.H.;
RT "Identification and distribution of gene clusters putatively required for
RT synthesis of sphingolipid metabolism inhibitors in phylogenetically diverse
RT species of the filamentous fungus Fusarium.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
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:KAF5539001.1}.
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DR EMBL; JAAOAQ010000632; KAF5539001.1; -; Genomic_DNA.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000582016; 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; cd16449; RING-HC; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
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; IPR041367; Znf-CCCH_4.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
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; PF18044; zf-CCCH_4; 2.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50103; ZF_C3H1; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000582016};
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, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 52..79
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 87..114
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 115..133
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 590..803
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT ZN_FING 52..79
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 87..114
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 115..133
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 803 AA; 90501 MW; F60A2D09D15AC540 CRC64;
MGNTFERPTT PETQFIQRIQ QNLQQLEAQN YRTHILTDAL REQNRQHRRP ERRDRPPCRF
YAQGHCLHGA NCRYAHDGPV NRRRPDRRQR QPCRFYAQGI CSHGAACRFS HEGPRPVQET
CRFFAKGFCR RGATSNDVSK DDLPDLLDEP WTREIGGAWV EFGDGAAVTN VTLLSDFSAI
QMRHLPPRSS ARSVQELLAD VGINVSISDI NFIKLVENRN GMAIVKVKDP EFAKSACWKL
RTSIRAPDLE VTQIPVPLPD GSSFGLIDSR NVRCSWHRPT KNATLLFKNP AEAFDAYYKF
KNQELNIAGL PVAAQMPAAV DATQKDGPWQ MELEGLVATM PSEDIMNIFP PSGGPSEVQM
GDSSYDTDED IDSTIIKSLL YDIGALEEWE VFGSPTARRV KAQARFIEES EAIEAVSQLN
ETWLPFNPSG KLYLQHVNLV KFRVSTRVYG VVEDSIESLR KDWEPKFVSF SSVPERGYRV
LKLESQDREL FMQAKEALEQ IINGTTMTLN GKNLWSPDFK ADRGAYRRLQ EIERDLGVVI
IRDIKSSKFR VFGPEDKFVP ACEALDQLLQ ELQPQSTGHV TEQSQTEKAT EGDCAVCFCE
ADQPLATSCG HVYCTICFVN MCQVEASTIG DFSIKCIGDQ GNCKKAIPLH EIQNLLLSEI
FESVLEASFA SFMRRHQDQL RYCPTPECTQ VYRVAQPETS VPPIFTCTKC MTTTCTSCHV
SHPRKTCAEY KGDESGGMAE LLKAKEELGF KDCPKSCGTH ICWLCLKTFT DGDDCYQHMG
RVHGGIGNEG EHEDDDDDDD IEY
//