RAD18_EMENI
ID RAD18_EMENI Reviewed; 443 AA.
AC Q02398; C8VCP5; Q00178; Q00183; Q5AWM1;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
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};
GN Name=uvsH; Synonyms=nuvA, rad18; ORFNames=AN7309;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=7651340; DOI=10.1007/bf02190798;
RA Yoon J.H., Lee B.J., Kang H.S.;
RT "The Aspergillus uvsH gene encodes a product homologous to yeast RAD18 and
RT Neurospora UVS-2.";
RL Mol. Gen. Genet. 248:174-181(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=L20;
RX PubMed=8868425; DOI=10.1099/13500872-142-3-505;
RA Iwanejko L.A., Cotton C.M., Jones G.W., Tomsett A.B., Strike P.;
RT "nuvA, an Aspergillus nidulans gene involved in DNA repair and
RT recombination, is a homologue of Saccharomyces cerevisiae RAD18 and
RT Neurospora crassa uvs-2.";
RL Microbiology 142:505-515(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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. {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 UBC2, forming a complex with ubiquitin
CC ligase activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAD18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB35098.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA90033.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA61360.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; S79392; AAB35098.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z49875; CAA90033.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z49834; CAA89995.1; -; mRNA.
DR EMBL; AACD01000127; EAA61360.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001304; CBF78646.1; -; Genomic_DNA.
DR PIR; S55494; S55494.
DR PIR; S57328; S57328.
DR RefSeq; XP_680578.1; XM_675486.1.
DR AlphaFoldDB; Q02398; -.
DR SMR; Q02398; -.
DR STRING; 162425.CADANIAP00000127; -.
DR EnsemblFungi; CBF78646; CBF78646; ANIA_07309.
DR EnsemblFungi; EAA61360; EAA61360; AN7309.2.
DR GeneID; 2869846; -.
DR KEGG; ani:AN7309.2; -.
DR VEuPathDB; FungiDB:AN7309; -.
DR eggNOG; KOG0287; Eukaryota.
DR HOGENOM; CLU_028491_1_1_1; -.
DR InParanoid; Q02398; -.
DR OMA; ERTQGGH; -.
DR OrthoDB; 1013108at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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:0006281; P:DNA repair; IMP:AspGD.
DR GO; GO:0006312; P:mitotic recombination; IMP:AspGD.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 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 PANTHER; PTHR14134; PTHR14134; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR TIGRFAMs; TIGR00599; rad18; 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 2: Evidence at transcript level;
KW DNA damage; DNA repair; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..443
FT /note="Postreplication repair E3 ubiquitin-protein ligase
FT rad18"
FT /id="PRO_0000056156"
FT DOMAIN 239..273
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT ZN_FING 30..68
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 175..202
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 106..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT CONFLICT 209..210
FT /note="FG -> YR (in Ref. 2; CAA90033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 48907 MW; DD3327065D3511B2 CRC64;
MEPTFDIPDS TDWLDTPLTL LAPFETSLRC QVCKDFFDNP VITSCSHTFC SLCIRRCLST
EGKCPTCRSS DQELKLRRNW VVQELVEGFK NARPSILQLA RMAQTGTDDS GDLAAEEPAS
KKRKIEPNAI VGTDGLPEEG IRTRSQSRGA SRQPQATPVQ VIDDGNDEDY MPDGLVPCPV
CGRRMKEEAV FRHLDSCTGT AEELKPAAFG SLAPGPRKSF LAATGKPPER LPVINYSLLK
DTVLRKKLKD LGIPNWGPRA LLQRRHTEWL NLWNANCDSR TPKPKRELLR ELDVWERTQG
GNSVTPTDPT NAVMNKDFNT EEWSANYDTD FKALIANARK KNDAVIRSTI PNASQANSDT
PRSAQLVDQP IEASLTPQDV DEKSTMNPQD AIDNRTEVPP VPDPPQALSG IDRAVNSPMK
NVTEGDAQAI PISSSASTHK TPH
