ID A5E036_LODEL Unreviewed; 919 AA.
AC A5E036;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=DNA repair protein RAD4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=LELG_02973 {ECO:0000313|EMBL:EDK44794.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK44794.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK44794.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPC family. {ECO:0000256|ARBA:ARBA00009525}.
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DR EMBL; CH981526; EDK44794.1; -; Genomic_DNA.
DR RefSeq; XP_001526415.1; XM_001526365.1.
DR AlphaFoldDB; A5E036; -.
DR STRING; 379508.A5E036; -.
DR GeneID; 5233182; -.
DR KEGG; lel:LELG_02973; -.
DR eggNOG; KOG2179; Eukaryota.
DR HOGENOM; CLU_003639_3_0_1; -.
DR InParanoid; A5E036; -.
DR OMA; RKWISID; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR Gene3D; 2.20.20.110; Rad4, beta-hairpin domain BHD1; 1.
DR Gene3D; 3.30.60.290; Rad4, beta-hairpin domain BHD2; 1.
DR Gene3D; 3.30.70.2460; Rad4, beta-hairpin domain BHD3; 1.
DR Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR InterPro; IPR018327; BHD_2.
DR InterPro; IPR004583; DNA_repair_Rad4.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR018326; Rad4_beta-hairpin_dom1.
DR InterPro; IPR018328; Rad4_beta-hairpin_dom3.
DR InterPro; IPR042488; Rad4_BHD3_sf.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR PANTHER; PTHR12135:SF3; DNA REPAIR PROTEIN RAD4; 1.
DR PANTHER; PTHR12135; DNA REPAIR PROTEIN XP-C / RAD4; 1.
DR Pfam; PF10403; BHD_1; 1.
DR Pfam; PF10404; BHD_2; 1.
DR Pfam; PF10405; BHD_3; 1.
DR Pfam; PF03835; Rad4; 1.
DR SMART; SM01030; BHD_1; 1.
DR SMART; SM01031; BHD_2; 1.
DR SMART; SM01032; BHD_3; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT DOMAIN 445..504
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 506..565
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 572..658
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 650..677
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 30..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..752
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..810
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 919 AA; 105753 MW; E6968C0C2DE85AC8 CRC64;
MSDNPNHYHK QLLREARLAK RNTNNNSSDG DNEEPRRKKR NVKKQSLNKK TTELREEQDQ
HSFDESSDSN DFEDIDLGVR EPPSDASSAE SEDFEEISLD TGHSYQFDEQ SNNGSAAEAD
ALTIQIRAPE EEDFEISKTG KGRSKVNFVS KEERRRRVQI HKEYIALMLI HLILRNRWCN
AKDIGKKLKR ACVTTQTQQL LTYDSKNSPL LGSRKLLDAL KKIMAIYSEK FRITVQGLVR
KDWQELGVIQ EAEVVTKNLF KKLVANYRGS RDVAAQGFVT LLRALGLNAR LVFSLQPPDY
TIITSPTKLL EEHTKSNVQF MDSPYPIFWV EVYDKYKNSW ISIDPIVMKI IETCPKRKKS
SFEPPATDER NQLHYALAID KVGRIRDVTR RYCINYNAKT IRKRISFRSS EDEDWYENLL
QAANRGKKRS VCDIYEMKEF HERDLAEGMP NNLQAFKNHP LYALESQLRQ NEVISPKDKS
SVCGTFRIKS SGKLVDVYKR SCVKRLRSAK AWYMRGRILK IGAMPMKTKS SGVGNGGGNV
AHESNTDDEE VRLYAESQTK LYIPKIEFED RIPKNAYGNV DVYTESMIPE NCCLIRISDT
VSLKLLQKTA QFLGIDYAKA ITSFDFTQRG KGGARTPNAK EGGIVVLKIH EEATRVAVDF
MIEMEEYERK MQVEENALKN WRFFLLKLRL QNRLNKSHGV VNDDSDTIQF ASPKKKRGEE
IKRNEAEEEE ETGEEEEVEE ADEVEEEEEQ EDYYDGGFVV DDHAIGLNDS TQLQGGVFKE
SSYINKVSDR NGIDDNSDEE EEEEEVFDGG FIVSDSEPND SRNHNDAIRH DKEEEKEGAK
EETSYDKEVG QEYKEMRSSS RGLRSTRKRV HKYVEENDEL EDDGQRSSQV YDDDDSLSEA
KFSEPSSDQS SMDFEYESE
//
