ID   Q0UY59_PHANO            Unreviewed;       831 AA.
AC   Q0UY59;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=DNA repair and recombination protein RAD54 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SNOG_03305 {ECO:0000313|EMBL:EAT90036.2};
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT90036.2, ECO:0000313|Proteomes:UP000001055};
RN   [1] {ECO:0000313|Proteomes:UP000001055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC   {ECO:0000313|Proteomes:UP000001055};
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA   Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA   McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CH445328; EAT90036.2; -; Genomic_DNA.
DR   RefSeq; XP_001793875.1; XM_001793823.1.
DR   AlphaFoldDB; Q0UY59; -.
DR   STRING; 321614.Q0UY59; -.
DR   EnsemblFungi; SNOT_03305; SNOT_03305; SNOG_03305.
DR   GeneID; 5970732; -.
DR   KEGG; pno:SNOG_03305; -.
DR   VEuPathDB; FungiDB:JI435_033050; -.
DR   eggNOG; KOG0390; Eukaryota.
DR   HOGENOM; CLU_000315_10_2_1; -.
DR   InParanoid; Q0UY59; -.
DR   OrthoDB; 5480555at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR   GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 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; IPR013967; Rad54_N.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08658; Rad54_N; 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   Helicase {ECO:0000256|ARBA:ARBA00022806};
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:UP000001055}.
FT   DOMAIN          233..411
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          566..723
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   831 AA;  93074 MW;  58E8BF8C73251576 CRC64;
     MHRTKAVAAG ECTPAKPAAR LYGGTPQSAD SLRKPFRCPG SATSTRVSEK PARKRRKVDY
     SGAGGEDGES DKPYSNDDRL ALATRDANRF PVFKAKDKDT LFKQRFSVPL LNKDIGAYNA
     NRPAPLLGMR LGTVFVARPL HDPSGEFAIV LYDPTVDDKP APKEEVEPKL SQQDKKELEA
     PLVHKSLAEI LGLKKKVDDE RPRVPVVIDP RLSKVLRPHQ VEGVKFLYRA TTGMIDPKAN
     GCIMADEMGL GKTLQCIALM WTLLKQSPDA GKSTIQKCVI ACPSSLVRNW ANELVKWLGP
     DAVTPFAIDG KASKDELIQQ IRQWSIASGR SVVRPVLIVS YETLRLYVEE FGQTQIGLML
     CDEGHRLKNG DSLTFTALNS LNVQRRVILS GTPIQNDLSE YFALLNFANP NYLGTRMEFR
     KHYEIPILRG RDANGTDEDV KKGNERLTEL LGLVNKFIIR RTNDILSKYL PVKYEHVVFC
     NLAPFQKELY NHFIKSPDVQ SLLRGKGSQP LKVIGMLKKL CNHPDLLELP QDLPGCEHTL
     PEDFVPKDAR GRDREVKVWY SGKMLVLDRM LARIRAETND KIVLISNYTQ TLDIFAALCR
     SRGYGCLRLD GTMNVSKRQK LVDKFNDPEG PEFVFLLSSK AGGCGLNLIG ANRLVLFDPD
     WNPAADQQAL ARVWRDGQKK DCFVYRFITT GTIEEKVFQR QSHKQSLSSC VVDSAEDVER
     HFSLDSLREL FQYRNNTTSD THDTFKCKRC RKEDGRQILK APAMLYGDTS TWNHFVNDGE
     NGPLGKIQDL LLRQETTNDL RDVTGKHGIA NGVQGKDAVS SSASMVLDTL A
//