ID A0A2D3V839_9PEZI Unreviewed; 862 AA.
AC A0A2D3V839;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Related to RING finger ubiquitin ligase (Tul1) {ECO:0000313|EMBL:CZT18744.1};
GN ORFNames=RCC_04588 {ECO:0000313|EMBL:CZT18744.1};
OS Ramularia collo-cygni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT18744.1, ECO:0000313|Proteomes:UP000225277};
RN [1] {ECO:0000313|EMBL:CZT18744.1, ECO:0000313|Proteomes:UP000225277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URUG2 {ECO:0000313|EMBL:CZT18744.1,
RC ECO:0000313|Proteomes:UP000225277};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; FJUY01000006; CZT18744.1; -; Genomic_DNA.
DR STRING; 112498.A0A2D3V839; -.
DR OrthoDB; 51730at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000225277; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; 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 Ligase {ECO:0000313|EMBL:CZT18744.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000225277};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..862
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013629104"
FT TRANSMEM 383..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 413..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 798..856
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 510..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 96576 MW; 87B39F74E09A6029 CRC64;
MADRRGALVP LLILLYIFLP RDTGSPQRST VVDDVPAQEQ LALAVVQNST WDADFGTLGH
ELNVTGVEPE RGFSWDCLSR IKDRAREQLQ YALGDFGPRT LDGETVPEDR ATPLYNDVTG
YLHGKWKRSK LQEGISPPHL NLSXYAPLNP LGQPGLPTRF DRNVTGHEGD ASVRFMETLQ
VDVPSARNTT RMSIELKITD DDTYDSWEAV MHGVYFQDIG QAILTTTSDK FKGIFLLPHL
ALSNRTFEHS KALLNESISK TILKQIDGQL SSRNPWSSHF DPSMDSRFLT PDCDLVVYLQ
QMAPVGFDEY SPSTMTFLEN ELKSPTGAIV RGVPDLRFSM LAFSPDCGYV LESSGPPESF
VQDGNHLSGP KMEIQYQHSR QHLLLYTLLL SLQLFLLMRQ MREANTPSVR SRVSFYTIVF
LIFGDWSVTL SFVVVSTIYS GIWFNLVATA FLGFMSVVFF GMRFLSLLWD VQAPERERRV
RAEVEEEQAR EEAFTATLAR IRAERTATVQ EHVSATDAHS QATTETPPES IPQPTATIPA
SAPPNVRVEP GGLPLPVTAT RPALVDTGAT PIFMPSDQAG FEEVGLTSGP PVDLNARVAA
RMPRLSSLFT RFYLLLLFTL FLSINATAWP APIRRVYFTL LSLLYVSFWV PQILRNVQRN
CRHALNWEFV IGQSILRLLP FAYLFAYKNN VLFTNTDYYS LAILVVWVWA QVLLLVSQEL
VGPRWFLPQG DWAPPAYDYH PILREDEEGA TMPIGFSQAT ADGSVPSSPI QERGDASRRG
SVAKETKEKG KRVFDXAICM QDLEVPVIEA GAPKDTSLGG GLLARRMYMV TPCRHIFHSA
CLEGWLKYRL QCPICRETLP PL
//
