ID RAD18_NEUCR Reviewed; 501 AA.
AC P33288; Q7RVG1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Postreplication repair E3 ubiquitin-protein ligase rad18;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase rad18 {ECO:0000305};
DE AltName: Full=UV radiation sensitivity protein 2;
GN Name=uvs-2; Synonyms=rad18; ORFNames=NCU05210;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C1-T10-34A;
RX PubMed=8097557; DOI=10.1007/bf00279551;
RA Tomita H., Soshi T., Inoue H.;
RT "The Neurospora uvs-2 gene encodes a protein which has homology to yeast
RT RAD18, with unique zinc finger motifs.";
RL Mol. Gen. Genet. 238:225-233(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: E3 RING-finger protein, member of the UBC2/RAD6 epistasis
CC group. Associates to the E2 ubiquitin conjugating enzyme mus-8/ubc2 to
CC form the mus-8/ubc2-uvs-2/rad18 ubiquitin ligase complex involved in
CC postreplicative repair (PRR) of damaged DNA. {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with E2 mus-8/ubc2, forming a complex with ubiquitin
CC ligase activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RAD18 family. {ECO:0000305}.
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DR EMBL; D11458; BAA02015.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA32973.2; -; Genomic_DNA.
DR PIR; S34825; S34825.
DR RefSeq; XP_962209.2; XM_957116.3.
DR AlphaFoldDB; P33288; -.
DR SMR; P33288; -.
DR STRING; 367110.P33288; -.
DR PaxDb; 5141-EFNCRP00000005008; -.
DR EnsemblFungi; EAA32973; EAA32973; NCU05210.
DR GeneID; 3878348; -.
DR KEGG; ncr:NCU05210; -.
DR VEuPathDB; FungiDB:NCU05210; -.
DR HOGENOM; CLU_028491_2_0_1; -.
DR InParanoid; P33288; -.
DR OMA; IPNTGPR; -.
DR OrthoDB; 6177at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097505; C:Rad6-Rad18 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
DR CDD; cd23148; RING-HC_ScRAD18-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; 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; PF02037; SAP; 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; DNA repair; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..501
FT /note="Postreplication repair E3 ubiquitin-protein ligase
FT rad18"
FT /id="PRO_0000056158"
FT DOMAIN 256..290
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT ZN_FING 34..72
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 186..214
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 111..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT CONFLICT 89
FT /note="A -> R (in Ref. 1; BAA02015)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..259
FT /note="ML -> IV (in Ref. 1; BAA02015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 54777 MW; 6476BF215EEC4644 CRC64;
MDVFGDEAFN VPDSTDWLGT PLACLMPVEQ AFRCHVCKDF YDSPMLTSCN HTFCSLCIRR
CLSVDSKCPL CRATDQESKL RGNWALREAV EAFKNSRKVL LEFARTPPTI QAILPDQAGP
SSPSKRKATE MEGPKEEDPE SKRPRRSTRS TRARAAELTA AILQEEQDTT PSADPDYVDQ
PPDDGLVACP ICLTRMKEQQ VDRHLDTSCP GSPQAASKRR PIPAQTPQPS TFPSFNTRLT
SQTNQKPPER LPALAYSMLR DTALRKKLSE LGLSTHGSRQ LLEKRHKEWI TLWNANCDSS
RPKKRSELLR DLDEWERTVG NPGTAAGGGG GQQGLGLMAR AQATGAQIKD KEFDGKAWAT
RYGGSFGDLI KQARQGIKRQ TLDGNGEKAD TKGGGGGEDV GPAELPTLQA REGESSAAPT
RMDIVPPSSP PRPGQVDDAD TEHDGQAPGK DAIAEDTAMR EQVIPGTPDK ERQWETSQQQ
QPPIPGDAQL SGMKKPNPET C
//
