ID F4S053_MELLP Unreviewed; 1023 AA.
AC F4S053;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Rad4 beta-hairpin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MELLADRAFT_117666 {ECO:0000313|EMBL:EGG01997.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; GL883134; EGG01997.1; -; Genomic_DNA.
DR RefSeq; XP_007414831.1; XM_007414769.1.
DR AlphaFoldDB; F4S053; -.
DR STRING; 747676.F4S053; -.
DR EnsemblFungi; EGG01997; EGG01997; MELLADRAFT_117666.
DR GeneID; 18926064; -.
DR KEGG; mlr:MELLADRAFT_117666; -.
DR VEuPathDB; FungiDB:MELLADRAFT_117666; -.
DR eggNOG; KOG2179; Eukaryota.
DR HOGENOM; CLU_003639_2_0_1; -.
DR InParanoid; F4S053; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000001072; 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; 3.30.70.2460; 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:SF0; DNA REPAIR PROTEIN COMPLEMENTING XP-C CELLS; 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 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:UP000001072}.
FT DOMAIN 557..607
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 609..672
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 679..753
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 114722 MW; 0C8A7732D0AB6496 CRC64;
MNNDRIFPRP SSSEAEDDDD EEMDWEEVDV QEEADLSADN DDSLSRPDTT AFNIVLSKSG
ANSTHKRKNP NSAMERMIRH ETHRAHTLAL LAAGRFRNLL LNDQLLQARL LSMVPLSLVN
AFSSFSPQTH PSEIDRSRLF DSAIKDLVSW WWQSFEIVES LESVRLRTWT EAEALYDTIQ
SSSKTSSAKG KGKEVEDDPF LNLLETGEPI HGSKSLMKRA VLMKGSRDMS AQLFTSLLRA
LNVPARLVFS LQPVTWRGAG GGGKSSKTDT PNDLSTEEQT GRSRTPRDKG ATGSVSTAKK
TRSDNKTKKS DQSKMLSVAS QASKSKPKQG EWAMKATKAA KAAKMKSINS SATSSRHYVL
TSADGNSTDD QEIPLAQKLA SRILEPNQIG GSSPSESHHP DGWRSRPVGK ASKVTPIVKL
RKARPVKSKH WTKSPSPEPA QMNRPPVFWT EVYSRPLREW YCVDVTRKRT RCKNLMEPTK
SNPENRMLYV IAFEEDHFIR DVTARYAHSF GATTMKSRLP PKKGSPDWFE KATIKLKRPY
KLRRDEKEDE EISKAQVTEA LPTTVGGFKD HPNFALERHL RREEVIHPRK TVGIFRGEQV
FPRSSVVVCK SAETYMREGR RIKGGQEALK LVKPRTVTIN RKREEELLKM EGQEVALQGL
FAEWQTELLI PPPIVNGIIP RNGYGNFDLF APHMLPQGAK HLPYKGIAKT AKKLQVSYAD
AVVSFEFHKR RATPVIQGII VPELEAEFVL DAYFASEDIA QEKEFSKLQE RCLKRWKKII
LALRIRRRLQ EEYRNQSIIV SLANAPQEGP SELNNIGIQP EETVIVPIRP AVQSTQSKRP
ADADGYELYA DHRVNTMAMP GPSKPSYVNG HKRGRSESVE IDLENKEPRP VSPRKRRMKK
GVPKSPQPSL DVPMMMDVQL DPGIPIKYDK AGRDNDDGIS SPLSSPPLAS QRTSGSVSAS
KPEPRRRSGR QPATVVSKDK VVEEETGAID TSRGRASRAS AVRASKKIQQ PSQPSDRVLR
SRR
//
