RAD18_ASPFU
ID RAD18_ASPFU Reviewed; 418 AA.
AC Q4WZJ6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=rad18; ORFNames=AFUA_2G16700;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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}.
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DR EMBL; AAHF01000001; EAL93969.1; -; Genomic_DNA.
DR RefSeq; XP_756007.1; XM_750914.1.
DR AlphaFoldDB; Q4WZJ6; -.
DR SMR; Q4WZJ6; -.
DR STRING; 746128.CADAFUBP00003173; -.
DR EnsemblFungi; EAL93969; EAL93969; AFUA_2G16700.
DR GeneID; 3513356; -.
DR KEGG; afm:AFUA_2G16700; -.
DR VEuPathDB; FungiDB:Afu2g16700; -.
DR eggNOG; KOG0287; Eukaryota.
DR HOGENOM; CLU_028491_2_0_1; -.
DR InParanoid; Q4WZJ6; -.
DR OMA; ERTQGGH; -.
DR OrthoDB; 1013108at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002530; Chromosome 2.
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 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; 2.
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 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..418
FT /note="Postreplication repair E3 ubiquitin-protein ligase
FT rad18"
FT /id="PRO_0000056152"
FT DOMAIN 236..270
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 173..200
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 110..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
SQ SEQUENCE 418 AA; 46205 MW; F9041F65FEFBF0DA CRC64;
MEQTFDLPDS TDWLETPLSL VSPLESSLRC QVCKDFFDNP VITSCSHTFC SLCIRRCLST
EGKCPACRSS DQELKLRRNW AVQELVEAFQ NARPSMLELA RKAANSRLDG GYVTGQPAAK
KRKVDQEDGP DASGSEGIRT RSQSRRGNSQ AEPVVVDAIE DDQDKEYIPE DGLVACPICG
RRMKNEAVFQ HLDICTGDPA PLKQASFGSL QPMSPASRKS KDVTDKPPER LPTINYSLLK
DNVLRKKLKD LGIPNWGPRP LLQRRHTEWM NLWNANCDSK APKSKRELLH ELAVWERTQG
GHAAPSSESS NTVMRKDFDA AAWSNNHGDE FKRLIANARK RKDAVIRTTI PQAAPARDGT
STASAPEQST EMSTPPEVAE RLQTQTVPEG TSVATIAENE TGTIQTPNIT QVVSSPPE
