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Database: UniProt
Entry: E4ZRH0_LEPMJ
LinkDB: E4ZRH0_LEPMJ
Original site: E4ZRH0_LEPMJ 
ID   E4ZRH0_LEPMJ            Unreviewed;      1207 AA.
AC   E4ZRH0;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Similar to DNA repair protein rad5 {ECO:0000313|EMBL:CBX93817.1};
GN   ORFNames=LEMA_P034910.1 {ECO:0000313|EMBL:CBX93817.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; FP929116; CBX93817.1; -; Genomic_DNA.
DR   RefSeq; XP_003837257.1; XM_003837209.1.
DR   AlphaFoldDB; E4ZRH0; -.
DR   STRING; 985895.E4ZRH0; -.
DR   EnsemblFungi; CBX93817; CBX93817; LEMA_P034910.1.
DR   GeneID; 13285153; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   eggNOG; KOG1002; Eukaryota.
DR   HOGENOM; CLU_000315_3_1_1; -.
DR   InParanoid; E4ZRH0; -.
DR   OMA; LRMFVSH; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45626:SF17; HELICASE-LIKE TRANSCRIPTION FACTOR; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT   DOMAIN          452..645
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1005..1159
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1181..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..330
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..835
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..854
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1207 AA;  136434 MW;  F584875E6A4730AA CRC64;
     MQEQDEIQQS VEHDVDSADM ATPSPMSQHI PFPSYTHAST SRNTQGRYST SQHQDEMHDA
     LYEEAPMGPA PGGPEDSSTL FVSERSPSEQ RATQRAHTAR PKTPARLPMQ ASVQKKRDLA
     LKRTPAHPTN IDPDNETYLD AVLQNRLPVV TGGAPSVDED IMSDRQALAE YQKKKRYYDD
     LRRNSGSGHL SFRHDVEWLQ IQGAERARRM KRDRDLALAS EDGGEHGQVF PQVRSMLQMH
     GEPEEEEASD HDFDFGRPGP RKRVRRDGPG KPISMIDAEL QSMQVGMEAH EETAGRKKKK
     GKGPDDSPAT SSRGKTKNRN RNRPSRAKGA IRGGHGKTAK DKRELERAAL EASSLFNSNI
     FAQQAGPDAS EQPCFTSRNK QSGLKELIAS VPLGNLKKAK NEMNMLLTAT RAFNGHGSVK
     PMPENSLWSV KGMKTTLKHY QILGTAFMRR RETSAEEPRG GLLADQMGLG KTLMMLANIV
     NGQPPRGSSE LKTTLLVASP ALLSQWKSEF EQHTERNLTI LRYGAGYRID STNPDEILSG
     HDIILTSYTE VMRSYPKNDP PIECQTAEQK IAWWKEVYET QRGVLHRMRF LRVVLDEAQA
     IKNHMGRTSI ACRALMATHK WALSGTPILN SLTELYPYFK FLGVPHTGSF KIFKHNYCDN
     KDPENTERLL VRLSQFMMRR THADEMFGAP ILKLPQADQH TYWCEFNPVE RCIYEIVQRR
     FTKRINMWSQ QNVLEKSYSN ALVMLLRLRQ LTSHVLMLQF VMRDLLERED IECIKEITQE
     HSADTTTQSG KTILAIRKQL DAHAIVARKK RLAAGREYND DCVPEDEDGE DGEDRLATDD
     EHASAEEDGE PSSQRSHPHN YVSGGKFGKE YNFKPFLRSL ETGDSWEKAK KKSRCGWCSK
     QPRSPWITSC GHLICNKPCL EQSHLAAAEE ERQHGPCKAC GVTPSYIHPC DPDEFDTPEA
     VAQGTRSKAR RKKNSQQVCA GQEDIAKDWL VAQGDDVLPS AKTIAIKAQI MNWTRKNPQV
     KIIIYTQFLA MISILARICH NEKWKIEQYH GGMTLHARDK AIASFAEDPD IRIMLASLRC
     GGLGLNLTMA SKVIMMDPWW NSASEQQAFC RVFRIGQLEE TSMSRLCVNN TVDKQLIAMQ
     ERKDAEIKSV MENDGKKVSR MTIRDLMKLF GNLEEDAEGR PFIMVDNPDP RGGYRADRDD
     EGYADDF
//
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