ID G4UL05_NEUT9 Unreviewed; 898 AA.
AC G4UL05;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGZ73598.1};
GN ORFNames=NEUTE2DRAFT_86972 {ECO:0000313|EMBL:EGZ73598.1};
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:EGZ73598.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ73598.1, 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 -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; GL891217; EGZ73598.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UL05; -.
DR STRING; 510952.G4UL05; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR OMA; ETTVWRL; -.
DR Proteomes; UP000008513; 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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16509; RING-HC_HLTF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.70.2330; -; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF11; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G06590)-RELATED; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 343..501
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 657..695
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 734..886
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 101069 MW; 8988B2D07CD1A175 CRC64;
MPKRPYTSGV GAAASDRRDE ARRRRLNADS SSSGPSQSHS QATPSSQHRP PEHVQAIHDT
LNWLSTQPDI LESDDEAEVI DLTQADPGPV LEFYGHFDGK IVGVRYYNGV ASPGEVVVCK
REPQNQYDPN AIRVDNVLGT QIGHIPRTVA AKLAPYMDNG DLVVEGMLTG EKEFYDCPVR
LYFYGTSAPL QRARLEERLK KDKLVKATQL NQTRKANEEQ RKKRTLELRG NGTYGFPSQT
QEPEPQVTME QLAKMSEVTN FRSGGDMIKS LAMSEEDLAN LPMASQPEKL RAKLLPYQLQ
GLAWMISKEN PTMPAKGSTD SVQLWQHTAD GRYYNMATGF YNKSPPQLMS GAICADDMGL
GKTIQIISLI MTEGLGTGPT LIVAPVGVMS NWKQQIRRHV HEEHQPKIVI YHGSKRKEFA
KTLQDQNVVI TSYGTLSDDA LVKTRWRRVV LDEGHSIRNA KAQVAQNACK LEAKSRWVLS
GTPIINTIRD LHSLLKFLRI TGGIEQSEIF NTVLTRPLAN GEPKGEALLK SLMKDLCIRR
KKDMKFVDLK LPEKTEHISR ITFWPDEQKK YDALLSEAQG VLENYRTQSK RSQGQFQGVL
ERLLRLRQTC NHWVLCKKRI TEVLELLADK DVVDLTDENR AILQQALQLY IESQEECPIC
IDPLSNPIIT HCKHVFCRGC IDKVIEVQQK CPMCRAPLSE DKLLEPAPEH SATQDEEELE
SETKSSKTEA VLALVKGTLD KEGSKIIIFS QWTSFLTIIQ HQLDEAGYTY TRIDGSMNAA
QRDAAIRALD YDPNTRILLA SLGVCSVGLN LVSADTVILA DSWWAPAIED QAVDRVHRLG
QTRPTTVWRL VMDNSIEERV LDIQKEKREL VGKAFQEKQD GKKKVKETRM ADIMKLLS
//
