ID S3CF86_OPHP1 Unreviewed; 1095 AA.
AC S3CF86;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=F503_05851 {ECO:0000313|EMBL:EPE10756.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE10756.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE10756.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE10756.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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; KE148146; EPE10756.1; -; Genomic_DNA.
DR AlphaFoldDB; S3CF86; -.
DR STRING; 1262450.S3CF86; -.
DR VEuPathDB; FungiDB:F503_05851; -.
DR eggNOG; KOG0287; Eukaryota.
DR eggNOG; KOG2911; Eukaryota.
DR HOGENOM; CLU_284010_0_0_1; -.
DR OrthoDB; 6177at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000016923; 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 GO; GO:0007034; P:vacuolar transport; IEA:InterPro.
DR CDD; cd23148; RING-HC_ScRAD18-like; 1.
DR Gene3D; 1.10.287.1060; ESAT-6-like; 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; IPR005024; Snf7_fam.
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; PF03357; Snf7; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 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:UP000016923};
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 32..70
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 197..225
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT DOMAIN 263..297
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 105..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 117163 MW; B473C2AB9690C037 CRC64;
MASHDGGDVS DSTDWLGTQL ACLMPVEAAF RCHVCKDFYN SPMITSCNHS FCSLCIRRCL
SVEGKCPVCR ATDQESKLRG NWALRDAVDS FVKARSTILE LARNPPAAQI QQQPTKRKVD
AAAGSVSSAA GGSQEEPQAK RTRTSARLSK TKAAEAVANI AHDESEGDEE VVEVQAPKPR
GGNSADADTD YKPDDGLIEC PICGTRVKMT LINSHLDNNC STGTSNPKPT PAFSKPTGST
TFKPLFSGAA PIKAPERLPS ISYSLLTDTA LRKKMSSLGL SSIGPRLLLE RRHREWSTIW
NANCDSARPK RKQELLRDLD VWERTVGALV AGGGGAATLT SRPIVAATQQ AAMIKDKNFD
ASAWKEKHNT SFQDLIANAR KSRSKTHEPK GEEAKEDATA KAEEGKAALE AAPQASEQLE
TEDAVMGIAI PDSSPPSPVS DRTDDAPAGP GEATQDAAQP HMGYDAPKAS SQSADVMVVE
LVNTGIPASS RDSTSPHLTG NALGRSRAIF NTTLYTIRTI HDTPLLIPPA QPATARVPNL
PRMASNAQRI QFLIDQEDGF TRTRLPALYS DFRSLRASNP DSYAINAAAW RRALAALVRG
GMLPAAASTT SKTQPKLGAT GATSTAARNF LILTAGEPLL DALHSERFKR PIALEAVIDE
AVQDHDLIPL EGFLRSKESI YNRKSWASWA VGTAVSLPWH ALSWGLRQAG VIEGSGVVAQ
HGGASSAPVS YYDGGKGRLT PNQFVVLANI EQAATAFMDK VAAVDATLLS PFERVWSVSQ
FKRTFSAAGA VLDQTHLPVG AAVQQPRLSD MDLNVLLAFL ARDKNAIVYD GHVVKLRAAE
SGNANANVIT EEDRAVAQLR ELIDSLTHQT SVLSRRIDDL TVAAKDAVVR KNRVSALAAL
KQKKQVESAL AARFATLGQL EATAAKLEQA SDQVQVVAAM DTSAEALKFL NEQVGGATGV
EGVVDRLRDQ MEAADEINRI IIDSGPTSTS AGALGIAIDE GEIDDELAAL EQQERKKTEA
VDQKRAEEEA AEKEDAQRAA AEETRRRLAL AGAIPEKVPN QASSEDVDAA LEAITTESFR
NMSLKNDEPQ AELAS
//
