ID N1RHL1_FUSC4 Unreviewed; 772 AA.
AC N1RHL1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Transmembrane E3 ubiquitin-protein ligase 1 {ECO:0000313|EMBL:EMT65164.1};
GN ORFNames=FOC4_g10011142 {ECO:0000313|EMBL:EMT65164.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT65164.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KB726990; EMT65164.1; -; Genomic_DNA.
DR AlphaFoldDB; N1RHL1; -.
DR STRING; 1229665.N1RHL1; -.
DR HOGENOM; CLU_010475_0_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000016929; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR22763:SF165; TRANSMEMBRANE E3 UBIQUITIN-PROTEIN LIGASE 1; 1.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000016929};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:EMT65164.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..772
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004111902"
FT TRANSMEM 409..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 708..766
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 504..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 85738 MW; DB24622C90EA3CEC CRC64;
MPQAQHPIAT LIFIVFIVWL VFPDSDYSSQ SLTLSDLAGE RLDHFQDALD VLNASRWGDF
VPVPGKDSKV KPSFLNLTGF RADDNLSWGG LKRFRERSLA FSRHAIPPVG QHNLWDTGHG
EPIWLNASGT VHGEWVKPKG SISRGYNSYN LSKIAPDMDW IGDNVPWARN ITGRTGRMML
RLEGNQTINE YEQLPTQSSV PVAGGLIRSV KGTTTIEDTH GSGHDWEMRL WGVHWPRQGV
VLMTTTSEKF EGIFGLPHLT PSEDFFQSSQ RLLNESIAHT IATKRENIYA DQTVPWTSDL
ENPLYTTNPS PHCEYVMYAQ VFPPSRTHFN IDSQESSRDT LESVIDAIES ELQSPVGAPI
PKIPKLQMSA IIYSPDCGFF LETKGPPDFG PSEAQHLTGM KIEVQLYQVK TWILVYAIVV
FGQVNLLKNQ MRESCTPSTM GRVSFWTIAI MLMVDGMTFT AAATWVSSAG ATFLPTLALL
FAAFLSMTIG GSFLAKVHEV QLPEARPRRE REANNMVDNT NGTELPTATT SDRSLLPEPV
TAHQPARPPP PRSQPQPVIV PSDQDIDAEI AAAAVPGATT AQRAEEAPQS FQSIIGRMIL
SSLSYFWIKE DNFLYARSDR HAFLVFCAWL WIQLIILAAQ DIIGPRFGIP AGWAPDAWDY
HPVLREDSLE AGGLPIGLVA DDTPGIERAR SSGDDGSKKQ STTRSIDCAI CREVLEVPVL
TAEDEDTGVA GVFARRLYMV TPCRHIFHSA CLEGWMRFRL QCPICREELP PL
//
