ID A0A423V8U6_9PEZI Unreviewed; 1067 AA.
AC A0A423V8U6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=VSDG_10056 {ECO:0000313|EMBL:ROV87258.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROV87258.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROV87258.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROV87258.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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:ROV87258.1}.
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DR EMBL; LJZO01000088; ROV87258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423V8U6; -.
DR STRING; 252740.A0A423V8U6; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR CDD; cd10567; SWIB-MDM2_like; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR041888; RING-HC_ZNF598/Hel2.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR044288; ZNF598/Hel2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF02201; SWIB; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00151; SWIB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000284375};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 7..63
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 205..282
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 333..373
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 71..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 114692 MW; 4101588179395E72 CRC64;
MSSTLNSEEI AQYTSIIDGI LATADLATIS RKKVRQALER ALGGKDLSDQ KNAIKVLIEQ
RFDAISEAQA APEAMPTPPH KHDDEDNKNG LQNGTTHMDE DADADADADA DADEDASAGE
IQVSTAPSKK RSSSMVEDED ARLARELQAQ ENRLARGRQT RGGNSTPKAK PKTKKKSSSK
VKTGDDSDVD TEDSGTAKKR KAGGGFQKEF NLSFPLQEVV GAERLSRPQV VKKLWDHIKA
NELQDPSDRR QIRCDEKLQA VFKQTTVNMF SMNKLLGNQL YPLDDSAKDD QETEGPKVAK
ETLLRPPEPK PKLEAGEGQD AGDAGDDDDD DVCFICANPI QHHAVAPCNH VTCHICALRM
RALYKNKDCA HCRTPAPFVI FTDDATRRFE AYTSADITSA DDNIGIRYTN EEIVGDTVLL
LRYNCPDLSC DFAGLGWPDL HRHVRSVHQK KMCDLCTRNK KVFTHEHELF TDKALHKHMA
HGDDRPGDIA QTGFRGHPLC GFCGERFYDD DKLYEHCRNK HERCFICDRR DSRSPHYYMD
YNALEVHFGK DHFLCLDREC LEKKFVVFDT EIDLKAHQLS EHADSLSKDV RRDARVVDIS
GFDYRQPYQE ERRGGRSGGG REGGRGRGGG GEREGRGRGR DPNAESLPRS SAQPLRRDEV
AFQRQMAIHS AQSISNRTFG GQLTTASNTP NPTQAGRNQQ RNGASSSAQQ PQPLADALTA
MSVTDQANMS PAERARLVRH GAVIERASNL LGNDATKMST FRSHISSYKS GTLTAPQLID
AFFSLFGDTS ASSLGTLVRE VADLFEDKSK AAALHKAWQD WRAINEDYPS LPGLGGMHGA
TTSSSGWAGA AAAGPTLHPG TGAGAGGRER HTTRVLKLKN STQNRRGSGA GVPGSAAATP
AAPSSVQWAG QSRAPAATSS AAFPALPSAG KPSASKSTPL WIGGTQPAGS SVAGSSTSSA
RASGSSTPVR RTVGGGGGPA PATSSRDAFP SLPAAPKVQT TLFGYGNGRG VRRDFGQASS
NFSWNGGQSS SGAGEASGSG EQDDAAGATG GGGKGKKKGK KVLVAWG
//
