ID Q9P978_NEUCS Unreviewed; 834 AA.
AC Q9P978;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Rad54 homolog {ECO:0000313|EMBL:BAA93079.1};
GN Name=mus-25 {ECO:0000313|EMBL:BAA93079.1};
OS Neurospora crassa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=5141 {ECO:0000313|EMBL:BAA93079.1};
RN [1] {ECO:0000313|EMBL:BAA93079.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR {ECO:0000313|EMBL:BAA93079.1};
RA Handa N., Noguchi Y., Sakuraba Y., Ballario P., Macino G., Fujimoto N.,
RA Ishii C., Inoue H.;
RT "Characterization of the Neurospora crassa mus-25 mutant: the gene encodes
RT a protein which is homologous to Saccharomyces cerevisiae Rad54 belonging
RT to the Snf2p/Swi2p subfamily.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AB032901; BAA93079.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9P978; -.
DR VEuPathDB; FungiDB:NCU02348; -.
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:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
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}.
FT DOMAIN 242..420
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 575..728
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 93508 MW; 2B7B8FF4ED9A8DFC CRC64;
MSASMVSTPK AASKDNSTNS LALTQRSKFP TPQSLDKLTK PFKCPGSATR TVAVDRPARK
RRKIDYKGAG GEDDEDGADK PYTNADRLAL ANRDANKFPV FAVKDKSQVF RKAFSVPLIN
KNTTAYNPNR PPPTLGLRQG AVFVAKPLHD PCDEFAIVLY DPTVDDKPKD TAPEAIEEKK
EEPEVKVDAP LVHKSLAEIL GIKKKVEGEH PRVPVVIDPR LAKVLRPHQI EGVRFMYRCV
TGMIDEKANG CIMADEMGLG KTLQCITLLW TLLKQSPDAG KSTIQKAIVA CPSSLVRNWA
NELVKWLGAD AITPFAIDGK ASKEELTRQL RQWAIASGRS VTRPVIIVSY ETLRLNVDEL
KGTPIGLMLC DEGHRLKNGD SQTFSALNSL NVSRRVILSG TPIQNDLSEY FALITVANPD
LLGTRLEFRK RFEIPILRGR HADASEAERK RGDECLVELL AIVNKFIIRR TNDILSKYLP
VKYEHVVFCN LAPFQLDLYN YFVASPDIQA LLRGKGSQPL KAINILKKLC NHPDLLDLSA
DLPGCEQYWP EDYVPKEARG RDRDVKPWYS GKMQVLDRML ARIRADTNDK IVLISNYTQT
LDLFERLCRN RQYGCLRLDG TMNVNKRQKL VDKFNDPEGD EFVFLLSSKA GGCGLNLIGA
NRLVLFDPDW NPAADQQALA RVWRDGQKKD CFVYRFIATG TIEEKIFQRQ SHKQSLSSCV
VDSAEDVERH FSLDSRELFT YRPGTKSDTH DTFKCKRCKP DGRQYMKAQA MLYGDTSTWN
HFVNHWEGED AAGKSGKGGD PNGGSGGMKS IHDHLLRQEV GERDVSAVFQ YISH
//