ID A0A2H3H7D2_FUSOX Unreviewed; 885 AA.
AC A0A2H3H7D2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0008006|Google:ProtNLM};
GN ORFNames=AU210_006582 {ECO:0000313|EMBL:PCD38096.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD38096.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD38096.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD38096.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD38096.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD38096.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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:PCD38096.1}.
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DR EMBL; MABQ02000004; PCD38096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3H7D2; -.
DR STRING; 327505.A0A2H3H7D2; -.
DR OrthoDB; 1462937at2759; -.
DR Proteomes; UP000219602; Chromosome 5.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
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 16..72
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 823..884
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 97..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 98402 MW; CBB44A82C916315E CRC64;
MEPTNAGLDL EKELTCSICT ELLYQPLTLL DCLHTFCGAC LKEWFTFQAA TAERAPNPPA
PGTNIFTCPS CRAAVRTTQH NATVVTLLDM FIAASPGKDR SAAEKEEMAR KYKPGDQVLP
TINTHRTADE RRIDAEDRSR HQRRGSRRPR ADEGGRHSSD QLHVEGERRR RRSESRQRQI
EHQSSIRSLI SSGDMSERDI EREIESFARQ IQEEGLLDGL DLDNIDLSRD DELSRRITEA
YRRRQRDRTR QEARRNNGNN YPPLTRYAEN AAAGDPRMLA PEGGRPRERS RPHSRSASAA
SATSAASQTE ERSRPPTSTN LANLEVQEPI RRPRRRTASG GRSSTTPVFP TTAEPRPAAR
SSTDLGSRPQ ASDITQSRPS FSEGRSTSTP IHTVPFPNPT EAASFSNNTG NMSFASRQGT
SQSASVPPLF SHHDAAAGRA NRPRPVDLAI VHQTVTSPIS SPTVSGYQRT RSQLYPEPSV
SCSRCNKQHI EYELHYNCSI CANGQWNVCL NCYRAGKGCH HWFGFGHGAF SKWEKIRQQK
GDASLPQPHT LTALRYRPPR SSPGGADGRK TLTADDPRHR LESGTFCAKC SAWTNECYWR
CDICNEGDWG FCNDCVNQGR SCTHPLLPMA HEATQSNQHR PGSPPRSPGR PTAATIFKGP
NASSIKPFEY LSFTTRCDLC QEPIQPNQAR YHCYQCTSSL VSDAAPGDYD ICSSCYGNLI
VQRQISPENG HSGWRRCLNG HRMVVIAFTD GKSGRWRYIA QDLVGGQGLK PEAAEKAEHR
EKGLQKWVWH ENGQDLARLV TKDVSETAPS ESGFAKSLPP DGGVGLKATA RFGWYPRPGA
DDELLFPKGA EIKEIEDVNG EWFFGAYMGT RGLFPAPYVR LEQDA
//
