ID G4UYA8_NEUT9 Unreviewed; 1068 AA.
AC G4UYA8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=ATP-dependent DNA helicase CHL1 {ECO:0000256|ARBA:ARBA00017386};
DE AltName: Full=ATP-dependent DNA helicase chl1 {ECO:0000256|ARBA:ARBA00016387};
DE AltName: Full=Chromosome loss protein 1 {ECO:0000256|ARBA:ARBA00029709};
GN ORFNames=NEUTE2DRAFT_116659 {ECO:0000313|EMBL:EGZ69853.1};
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:EGZ69853.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ69853.1, 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 -!- FUNCTION: ATP-dependent DNA helicase important for chromosome
CC transmission and normal cell cycle progression in G(2)/M (By
CC similarity). May have a role in changing DNA topology to allow the
CC loading of proteins involved in maintaining sister chromatid cohesion
CC in the vicinity of the centromeres (By similarity). Has a specific role
CC in chromosome segregation during meiosis II.
CC {ECO:0000256|ARBA:ARBA00025396}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
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DR EMBL; GL891258; EGZ69853.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UYA8; -.
DR STRING; 510952.G4UYA8; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR OMA; QTHQFRD; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EGZ69853.1};
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 31..556
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 85..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 118671 MW; 6CA5035F7B65D1FE CRC64;
MASTLPIPDI NVIAPSFIQR DSQNSDNMRP PPTDFNHPYT PYPIQTAFMQ TLYSVLDRTV
AVPPQTTTNS TNNTVPSATF SSTAATLIPS NPSTSSSTPP LFNPTTAPTV HLENRATQPS
QSIAPQTTTS KDKDKGPSSS SSVPKGHAQI ALFESPTGTG KSLSLICGSL TWLRNHKRLQ
FEAEIEKIQQ QMEASGEPEW MVESAIKRKR EELAQKYEEM ERTLERIRQK EREMEKEGEE
GQARGGKRRK LNRGKGDEEE GGKKKESGGS RGLTASDEDK EFLIGDWRDE GGLDENDPMG
QLSKETRELL EKVGMGTAGG KKGANEGPVA EEEIKIFYTS RTHSQLTQFI QELRRPEFPA
SVPTPNPQEE PAKEIVKQIP LSSRQKLCIN PTVNKLGTLA AINERCQSLQ QSKTPKEQRC
PYLPNAANLK ATHEFRDTAL ATLPDIEDLY QTGKQLQICP YYASRAAIPG AEVITLPYPL
LLQKSAREAL GIKLEGNIVI IDEAHNIMDA VSNVHAAEIK YTDLKRAKLS LGMYYQRFHQ
KLTGENKVMV AQLQRVVEAL GVYIKTKLDK AALGHKADQE GIVLDTSLLL KTGGADQINL
YKLIRYVQES KLAFKIEGYI SYCEEEGRDT DDEEAETEIK ARQGRPPVLH TLCSFLTALT
NLSSEGRIFY EKIPPPRGEL QDMKLSYMLL SPTHAFSSIA ESARAVILAG GTMSPFEDYK
AHLFPDVPPE KITTLSCGHV IPPDNLCVWT LGSIAPNPKV DTGIGEDCFD FTFAKRSNPN
MINRLGLVLL NLCSVVPDGV VAFFPSYGYL EEVIGVWKTH EQAMGPKTIW ERLESKKALF
IDSKTESSEQ TLQKYSDVIH SEVRPLSPAG SRVKGAMLLS VIGGKMSEGI NFSDRLGRCV
IVVGMPYPNP HSPEWLARRE YLEANFIKRY TASQQTSTAT APLPAPVIPP PSNTTHHSTN
PSSSRNKDKH KPPNVRKLAA RDSHQFYENA TLRAVNQSIG RAIRHQNDYA AIVLIDNRFE
KEHVRAKLPG WIREGWDETQ RQAKEDGKVL KGLQGMMGRV NMFFRGKN
//
