ID   Q0UGD3_PHANO            Unreviewed;      1123 AA.
AC   Q0UGD3;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Helicase C-terminal domain-containing protein {ECO:0000259|PROSITE:PS51194};
GN   ORFNames=SNOG_09181 {ECO:0000313|EMBL:EAT83373.2};
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:EAT83373.2, 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; CH445338; EAT83373.2; -; Genomic_DNA.
DR   RefSeq; XP_001799482.1; XM_001799430.1.
DR   AlphaFoldDB; Q0UGD3; -.
DR   STRING; 321614.Q0UGD3; -.
DR   EnsemblFungi; SNOT_09181; SNOT_09181; SNOG_09181.
DR   GeneID; 5976383; -.
DR   KEGG; pno:SNOG_09181; -.
DR   VEuPathDB; FungiDB:JI435_013640; -.
DR   eggNOG; ENOG502RQPI; Eukaryota.
DR   HOGENOM; CLU_275347_0_0_1; -.
DR   InParanoid; Q0UGD3; -.
DR   OrthoDB; 1913603at2759; -.
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:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 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; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT   DOMAIN          953..1123
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..404
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..419
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1123 AA;  126119 MW;  DA8A24D306FF5724 CRC64;
     MAGRDSDDDS DTEWAPPKQP EWYKSKANTT SSNSMSQTNV REGYGITTLE VVELVEDLTS
     YVKKKDLLEK IQSEKSQSQL LKSLRSPTSK DWLAVAKCTR LRNAQIPKVF HEAAAGTIWT
     MMLAKVRQYG AKVKTEDPSN TPTPTLSETA QRRSSSVVSN RSTASITDKF GVASLTEPAI
     LNDANVALVD AVHHSVVKQF PMFRLMTKES QQKLEENYFE VRAQHLKYDA LIQHLSLPKY
     SDWYQAGTSQ VMDALTMTLI EDDDDLLGTV NSHIKSRRLG APSPPKKRGR HSKLIPDGPP
     LKRRKTEAAD SRHAKASGGR TKKDKDSEDS DTGSDVPRPR RRDRAAARAR SAERKRLGKE
     AQLKKTRDEE ELAKAKKEKE EKEARERETQ PDGPLDSDDY RSDSSSDIDP EDDSEDEEAT
     TAKDLAREQK ERLKALLNAN CDFTPYQLTD AYILYFKELS SDNGGIFANA MGMGKTRAMV
     LAVLMGHVHF KNWTEVQNAR AEGDATEHNA VDDDDKPCPT EGERTFHCAC ERSPSFNAEP
     RQAATMMTGW GRAADAWKNE VVAMDLANST WCDPSDPLAL RFCFFSDSPP ENMGRPTKEE
     AMEMRIDTTD AISKALAAAN KLVAPRSYVL GGVDHRETVY WTIPEANTPA VHPEATKHRP
     APSAARFVIV CGFGKVDKHV FRAYNTMSVT AQRTIIRKGG PHVEKRAILL PGHVTVWGRT
     VFDEFHNCKS EGTIMAKFYQ DIRSHNHGYQ WKAWALSGTP MEQGLNEILI FVSLALIGLQ
     NRKGVSNWFN ATDKRDSVTG DRIYKMEDAV YRSIAETPSH RTRQNTALNG LAMAKQWRNM
     IANVKHDASE HESSHEYKEL ISQGAAVAQR FMLKRTLKTR DPWGKPISGI KGDFLPYFQS
     CPCPDFLSTV QNAEQQCRDI LEKEGLDESE ASRRVIFNRF EMQAIASYPA LATLKAAQFK
     TYGSRKVKRF TSNSAVTWLG LREKFGDESV LVMQGGMTQH EINLKLAKWR DPDGPWIMVA
     SMAFAEAITL TEATHVVIME PQDRQNTQDQ FMFRVYRLGQ LAEMCVGIVY FNPDSELELK
     VLGKQDVKTT SRDKLQGGGS TVTDQRMDWH QTEPIVMSLE ALC
//