ID B2W3K7_PYRTR Unreviewed; 1116 AA.
AC B2W3K7;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=DNA repair protein rad5 {ECO:0000313|EMBL:EDU47964.1};
GN ORFNames=PTRG_05057 {ECO:0000313|EMBL:EDU47964.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU47964.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS231618; EDU47964.1; -; Genomic_DNA.
DR RefSeq; XP_001935390.1; XM_001935355.1.
DR AlphaFoldDB; B2W3K7; -.
DR STRING; 426418.B2W3K7; -.
DR EnsemblFungi; EDU47964; EDU47964; PTRG_05057.
DR GeneID; 6343302; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_7_1; -.
DR InParanoid; B2W3K7; -.
DR OMA; YYVFHGP; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
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:SF51; SINGLE-STRANDED DNA-DEPENDENT ATPASE (EUROFUNG); 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:UP000001471}.
FT DOMAIN 477..667
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 938..1097
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 125567 MW; 10C44D93E7289B33 CRC64;
MQPSQLNVDM TDNASSDVIS DSDELVVHGS AGSQNDVAIS NFVEPLSLES LPEVPFKRSL
PELTEHVPGD NATPHNSSQA PPAPQIPQFD PRSLLNPRSS SAKRPASSGG ESDHGRTDPT
ITNQVSLVER LHNVQERAAT PVKRVKTDDP RNSKSNRSSA NVGSTLDLQN KNGQSSSPHP
QQGPAIDLTM SDDEDDVQVI GDNGNDDVCI GKLKQTYIQA HLVPFPDPKK FAGNHGGQSR
IKVSFRRGGG NKGNQIIMVL DGASKEFGKV DMKTAQGLAP LVDSSNASGL KWIAWTEPRR
KLPNEGPPGT PISALISMTL QLYCPRKNAD NIGRFLKSRN LILEAPVFEL ARHDYYNPQT
KQSFQRSQVG QPDFQPSGQY AVGAPTHNYV IRSADEIRAE MDDVFDKVIS TSKEVPMREP
SPLITTELYP HQKQALHFMV EHEQETIGDD VEDPLWKPHF DNNGRQSYVH RITGSKVAKI
QRNLGGILAD EMGLGKTLSI LSLICDNASI AAAQQFCQKK PPPRPVPAML QATINSRATL
LVCPLSTMTN WKEQIKEHFP MGKSTLKWTR YHGSERFSMT PEMLANHDII LTTYHIIAKD
LMDKKRPLPY INWFRIVLDE AHTIRNATNQ SRAACMMMGQ RRWAVTGTPV QNRLEDLGAL
FNFIKLTPFD NSQGFNQYIL QPFKNADPMV VDKLQLLVGA VTIRRTKEII KEEIPKKMDY
VVRLKFSKDE QQLHDWFEKD TQRKVLAVTQ GDKIGGQSYA RILTAILNLR LICAHGRDLL
SEQALKTTDG MTYEQPMQLE EDEQETPQLT RHQAYEMLNL LQSTSADDCH YCDGKKSLLD
PDSADEDEEG NVPDTIGYMT TCYNLVCPRH LKTLREEWKK TLQPDGLAQC PICDDVNRPT
ALELKRADFY SFLEEQDKIR KDPKLAKKLG SYTGPHTKTK ALLDDLEEFR NWSDQHPDER
PIKSIVFSSW TTHLDLIEIA LKNAGHTLVR LDGRMTRENR DKSMQALRED PSIRVMLVSI
GAGGLGLNLT TANKVFMMEP QFNPAAEAQA VDRVHRLGQD REVTIKRFIM EGSFEEKMLE
LQNKKRDLAD MTMSKERKSK QESTRQKMEH LRSLFK
//
