ID H6BP32_EXODN Unreviewed; 518 AA.
AC H6BP32;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=HMPREF1120_01453 {ECO:0000313|EMBL:EHY53259.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY53259.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY53259.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY53259.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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; JH226130; EHY53259.1; -; Genomic_DNA.
DR RefSeq; XP_009153720.1; XM_009155472.1.
DR AlphaFoldDB; H6BP32; -.
DR STRING; 858893.H6BP32; -.
DR GeneID; 20306092; -.
DR VEuPathDB; FungiDB:HMPREF1120_01453; -.
DR eggNOG; KOG0287; Eukaryota.
DR HOGENOM; CLU_028491_1_0_1; -.
DR InParanoid; H6BP32; -.
DR OMA; IPNTGPR; -.
DR OrthoDB; 6177at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007304; 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 CDD; cd16529; RING-HC_RAD18; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
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:UP000007304};
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 219..246
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT DOMAIN 299..333
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 108..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 56539 MW; B5FC83AB716D2E47 CRC64;
MQEPYEFTDS TDWLSTPLAA LAPLESSLRC QVCKDFFTTP MMTSCSHTFC SLCIRRYLSQ
EGRCPACRES DQEIKLRRNW VLEELVANFT ASRRGLLEFA RRAAEKTLAD DDNGGGAAES
QRPKKRRKVA NDHKDNTVPN GTTERRSTRS QSKKLTASQS QQSAAAPSST PESVIDVIED
SEEEGSLYEE TGQRPTTSHS PPSLANGNGS AATEPNDGLV ACPCCHRRMK ETLINSHLDK
CILGESTTPV DGGGGTTTRT SSPAPGPAPT PPQIAAPGTI AYTQKKPAKQ NERLPFINYS
LLTDNALRKK LRDLGIPTHG SRELMRRRHT EWVNLWNANC DSTNPVSKRQ LLHELKVWED
TLGRQGDKGT ASGFMAKDFD RDNYVKNQKS NFDDLIKQAR QRRAVASDRP PPTADNGTPS
AAEEHNGASD QGVKPQDHVK QPDGRASIAS IIMPESPNIV QGGHLNGTDD RLPRGKPSHL
PADTSLEQQA PSPSDSIPSR WPGSEGEPPD TPANGYAA
//
