ID A0A165HAX6_XYLHT Unreviewed; 461 AA.
AC A0A165HAX6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Postreplication repair E3 ubiquitin-protein ligase RAD18 {ECO:0000256|ARBA:ARBA00015551, ECO:0000256|RuleBase:RU368093};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU368093};
DE AltName: Full=RING-type E3 ubiquitin transferase RAD18 {ECO:0000256|ARBA:ARBA00031783, ECO:0000256|RuleBase:RU368093};
GN ORFNames=L228DRAFT_245972 {ECO:0000313|EMBL:KZF23233.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF23233.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF23233.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF23233.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
CC -!- FUNCTION: E3 RING-finger protein, member of the UBC2/RAD6 epistasis
CC group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to
CC form the UBC2-RAD18 ubiquitin ligase complex involved in
CC postreplicative repair (PRR) of damaged DNA.
CC {ECO:0000256|RuleBase:RU368093}.
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 ECO:0000256|RuleBase:RU368093};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU368093}.
CC -!- SUBUNIT: Interacts with E2 UBC2, forming a complex with ubiquitin
CC ligase activity. {ECO:0000256|RuleBase:RU368093}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368093}.
CC -!- SIMILARITY: Belongs to the RAD18 family.
CC {ECO:0000256|ARBA:ARBA00009506, ECO:0000256|RuleBase:RU368093}.
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DR EMBL; KV407457; KZF23233.1; -; Genomic_DNA.
DR RefSeq; XP_018188788.1; XM_018332292.1.
DR AlphaFoldDB; A0A165HAX6; -.
DR STRING; 1328760.A0A165HAX6; -.
DR GeneID; 28897429; -.
DR InParanoid; A0A165HAX6; -.
DR OMA; IPNTGPR; -.
DR OrthoDB; 6177at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000076632; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006301; P:postreplication repair; IEA:InterPro.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039577; Rad18.
DR InterPro; IPR004580; Rad18_fungi.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR NCBIfam; TIGR00599; rad18; 1.
DR PANTHER; PTHR14134; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR PANTHER; PTHR14134:SF2; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU368093};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368093};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368093};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632};
KW Transferase {ECO:0000256|RuleBase:RU368093};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU368093};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368093};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 30..68
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 174..201
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT DOMAIN 239..273
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 107..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 50502 MW; 78B22BEF7AC3305F CRC64;
MAHTFDVPDS TDWLNTALPK LAPVETALRC QVCKDFYNTP MITSCSHTFC SLCIRRCLAS
DGRCPTCRAA GQEVNLRRNG TVEELVETFQ STRADILKLA RDAIFSERPK RRSTPPKRKL
GDTDLEADDT SRSSSRRTTR SQTQRSQSAA AADPAPITIE DDEDSEEQQP DDGLVACPIC
NRRMKAESVF SHLDRCDGKP ADPRSQSSTP KTPTQLQTIY PQRGIQSPRP PERLPKLNYS
LMKENALRKK FSELGIPAWG PKPLLERRHT EWVNLWNANC DSSRPKTKKE LLNELDLWER
TQGGYASGGA GSSLIKNSSI GGGGGGGGGN TVMRKDFDGA GWAASHSTDF QQLISEAKRK
RNAPQSVPAP VPASPAAEPE TDVNADRSIE GRVNGALSDL PLRDSNGKVI DDEGGTEKDV
DGPVHTSSLS PSRFKPALLS SSSKSMEERV FEQPDDPIED R
//
