ID G4UMX9_NEUT9 Unreviewed; 1919 AA.
AC G4UMX9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=NEUTE2DRAFT_90105 {ECO:0000313|EMBL:EGZ72141.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ72141.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ72141.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL891236; EGZ72141.1; -; Genomic_DNA.
DR STRING; 510952.G4UMX9; -.
DR HOGENOM; CLU_001161_0_0_1; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; IPR044574; ARIP4-like.
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; PTHR45797:SF1; HELICASE ARIP4; 1.
DR PANTHER; PTHR45797; RAD54-LIKE; 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:UP000008513}.
FT DOMAIN 978..1168
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1351..1501
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 109..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1828..1919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1861..1878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1890..1904
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1919 AA; 214685 MW; 15D9935A26E89B17 CRC64;
MAELNENEPF HWDVERVVKE LCTPERTWDA PAPHKLPDPE RLAFKLRELD IDGETLLMYP
DEYGWPTFWE MLGIKKLAHH LSIGKAIKQF RETSTLYYRQ KRDIDLPKGL LSTTPAIKPD
PLDPSEPTPP LVDNSIPEPT AAAIDGPVSE PSPAGVGNAA TDASPAIVNN TAVEANSVML
NDAASEPTPG VVSAPASETA SVMTGSAAVA PTPMEGVICH HAAPAEQAQD VQMSGIPDQS
PESPEKRGLG NGLRQDTEEA SRDPERPLKK RRIAPTIVST VAPAQARSFI PTEGDMFYHP
LLDIPSSQTG ASQTGASFRS ATLPTSTFLS DANFDRFLDV EDSKFSYLGS SALRSEDIAS
LPYNFESDDD GDDKEASEEF TWVRSGAVPP ARALQVARVM RKFFRKRSPF VNEDEEVVLD
FGEDDDGMSV DSETYREYEQ EEQERKAHQS MHGSPRLSKV QAEEAIEDAI QRLEVSWETI
KKPKFERRAW KIWQDARRNR TRLSLITFAK NQLRSLEVRL GNMKNELLNQ KWFKEDKIEA
KAEGFLEESV YDRKYQTWLL NLLENPHEPP KPSTLPRLKP EPKKERETLA SDEELLTSDS
EEEDQFIEDD LSSVDHMIID PKETIPSTRP STPVRPLNPS TETNHIPEEE ENTIAQPSTV
DDETGAVNKV EPTTPQRIIH TIPAEPIEIL SSPSDVDQLA NLPPLTDVDT IGKLGTQFWA
KHRDGERLVI AALWSWSPLR QSEIFDTIQD RGDKETWKEH IQPLIDRAAT GISRIDVDPD
SISLILALLF LTYSDFSEGR LKIRSTTLRC VTCQKLNREY LRFGEFFEFL QNCIRYFRSE
PKSPTPMEMT SAESPEATQD IPMDITSESE HMDTDLEELS SQFPLSSAKK GRRPKHDEKA
KKLRVDSKAL LKQMDERRKL LRAKLAETGS VPSDKSRLII NETKESDDLP LIYVHEEIGG
RIKDHQIDGV RFMWDQIVVD SNSRQGCLLA HTMGLGKTMQ VITLLVAIAE ASQSDDPRVV
AQIPKDLRVG RPLILCPSGL VENWIDEICK WAPKDILGNI TKIDAATVPP SERVLLIKGW
ARSRGVLVMG YELFRSLVSG KEDNVAELLH SSPSIVICDE AHRFKNKTSK LYAVVQDFHT
MSRIATTGSP LTRNVMDYYS MINWVAPNYL SDVGEFNQKY AEPISAGLHA DSTDAQKKLA
RERLQILKAI VAPKVNRKDI QVLVDELPQK REFILTIQMT KVQRDAYREY LETAQRNKGN
DLYRTACVWG LIASLKLLLA HPKIFKSKME ERLSSNPALA KGKQRITNDE DPDSDENDEP
LDLSRDTLRN VLAKVSIRGI DDIVHSTKVT VLLQILKECK QIGDKVLVFS QSIPTLNFLQ
DLFKQKKINY KRLDGKTPVS QRQAAVKEFN AVDSLDVYLI STRAGGVGLN IPGANRVVLF
DFGFTPAEEQ QAVGRAYRIG QEKKVFVYHL KVGGTYETAI HNLAIFKRQL SERVVDKKKP
IPSSTRMREY FITPPENLEQ KDLSAVKGLD PEVLDKVLAS AECSSIIREI DSTETFEREE
VYEFTAEQHR ELNKQIELEE LRINNPEEYK RQMSTGSGFA LPSLPPNLGT PISTGVPLHL
RDKHNPATPG SAPSIPLSAA NNISASTQAG APIPRVASTA IASQTVASSP SPANGQVAAL
NPILGTNTHY KVAEAPRKPA TLKAPEIIPK PRKPEDTTPK LLEALGEVHR KLRDDGYDMS
VHPQDLVMQI NSECDRQDMA AGTLPRMDKL RSLCKAVTES TRFGEALLAG YLTPNEVVAM
GMAQMKAKIA EFQTMTDDCF KQELWARHKA SHAPKSTADV TVKTEKTKMR PPLAESDAID
GIARSSSTST TTKATPSRTL TEEIERKKKK KKKKEERKKH KRRLQPGGTA DMPLVIDDD
//
