ID Q2GUR6_CHAGB Unreviewed; 2536 AA.
AC Q2GUR6;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=CHGG_08288 {ECO:0000313|EMBL:EAQ87035.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ87035.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|RuleBase:RU363044};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU363044};
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|RuleBase:RU363044}.
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DR EMBL; CH408033; EAQ87035.1; -; Genomic_DNA.
DR RefSeq; XP_001225944.1; XM_001225943.1.
DR GeneID; 4394502; -.
DR VEuPathDB; FungiDB:CHGG_08288; -.
DR eggNOG; KOG0987; Eukaryota.
DR HOGENOM; CLU_228281_0_0_1; -.
DR InParanoid; Q2GUR6; -.
DR OrthoDB; 2612816at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR046700; DUF6570.
DR InterPro; IPR025476; Helitron_helicase-like.
DR InterPro; IPR018289; MULE_transposase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR47642:SF2; PHD-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03184; DDE_1; 1.
DR Pfam; PF20209; DUF6570; 1.
DR Pfam; PF14214; Helitron_like_N; 1.
DR Pfam; PF10551; MULE; 1.
DR Pfam; PF05970; PIF1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU363044};
KW DNA damage {ECO:0000256|RuleBase:RU363044};
KW DNA recombination {ECO:0000256|RuleBase:RU363044};
KW DNA repair {ECO:0000256|RuleBase:RU363044};
KW Helicase {ECO:0000256|RuleBase:RU363044};
KW Hydrolase {ECO:0000256|RuleBase:RU363044};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT DOMAIN 185..282
FT /note="MULE transposase"
FT /evidence="ECO:0000259|Pfam:PF10551"
FT DOMAIN 735..822
FT /note="DDE-1"
FT /evidence="ECO:0000259|Pfam:PF03184"
FT DOMAIN 1179..1317
FT /note="DUF6570"
FT /evidence="ECO:0000259|Pfam:PF20209"
FT DOMAIN 1441..1626
FT /note="Helitron helicase-like"
FT /evidence="ECO:0000259|Pfam:PF14214"
FT REGION 511..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1998..2022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1119
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2536 AA; 285767 MW; 25C6B1FA522AD8B0 CRC64;
MRPCGPLPPP VVYATLDELS ATVDAHAAKN GYKIVKNGIN SGRARFRCAK GRKWASKAKP
ENVSHNHGWN DTTAFAQNGA QALKPHHEKI IELANSGIRP AQILSAIQAD EIGVFGKDIH
NLIQQHRRDE LHGRSPLQTL YEDFLVSSDS EFEYQDARDA EGHVTSLTIA PKSGLELRSK
NPHLLLFDST YKTNYHSMPM FNGCGVTQEN KTFNWAVIFV SGEKESDYKG ALESAMRILQ
KYDIPDSGCI VSDRELALLK ALSKSSWGMI PHLLCKWHVN MNVLAKTRQF FPAATRENGV
YKRHPKFKEF LQEWSSLLAA STPEVYESLV TRFQDPSRHP EQAIKYALNT WLTPWKKNQR
SALDINTAQS TNKTRTDINQ AVFSWIRGQV SVHALELLSR EISALPARNE PLKDTCGPCP
LSTTHGPPCR HVLYSHLTSH GPLEMTQIHQ HWWNYQSWTG SEESQVPLPL NPLKVKGKGR
PVGAIATHKK GEGANGTKRL PSAFEIEQAE EQATAVPPST APAVMQSKGR KRKQAAVIPD
AEEVTTTSEN GGNTAEPKVT STELGLRRIE QHGEDTYKPG TAAPRAYQRV IAGLEYVDPE
VEDLHDAILA DADTAKAADA EDDGLILLDA SIATTPVPAM TVRENWVHRL LDRHPHLKTK
YSRKYDYQRA LCEDPEKISA WFARVQKTIN EYGVLDVDIY NFDEAGFQMG VASTSNVVTR
SDRRNRPVVI QSGNREWTTV IECINATGWA LDPLIIFEGK VNISTWYEDS LLPKTWRIGV
SDNGWTTNEL TFEWLREVFE PQTRKRTVGQ YRLLILDGHG SLLCVVRNCG AFLDLFQQAD
KPCSTAAPHF PQHPTPSRTI SQRSSYQRSS CRAKRPVAFL AVVCVTLRIL FWLQRMPVMA
GFRCFNGGRC VAGSAEGVPA LSRREKYRPV LRSSWQWQAC VKLPGVPGSA CGSSASTAAI
SAMSAIGRGE SAALSLPDPV HLAPRQNLTH RVLASMYHEG GRLDTDTPEM AAARGQISAI
QRQHRVQRRQ GEEPSQTPTM SGLLRQQQPA NAEDGPASAQ QRDDAPSAVR DDEDNPQATQ
PQLPRVGRIP ARHRPPPSSP PRSHGRQRGR PRLSRNLVGR PRGHRSAAVP PRDESPPRQF
DEPGPRFTGG DQETPLLAED IAVKRELDEA LAAETMQRCL QNKLDFGAVP PELPQLEPLE
ELCIARVHVS VNVFTVYDAS LRESVLANQR QVRGQQYKYR GHVVHFLRDV GKVYSELPLL
PKDLDIVILR PRGSEAVEQM DRQFRNRFRV RRAAVETWLR FLADNHLGYR NFTCNYDLSQ
LPEDGDVFDQ LNIHEVAESG GLPADSGPVE EPEEDREVVD EAAVPNMLIH GSELNQLQGR
VNDRATEVNE QVPLESVDPQ AAHQLQMPSI RRTPLDEFNQ KHALLSLACP TLFPRGVADF
DGRFAKHHSF RFIALNTLMR QQARGHSRFY VSKNHRTPLT KEALQEALAD PDTPEAQAIL
NRISRYAGVI KDTRPFWYRR RRECKSFAHC LGVPSAFITL SPADLHWQSL YQHMPEYEEW
KALDEPRRMA KSRRLLRENP HIAAWHFHSR NSLCRKIVLK KKFNVPDFWY RYEWQGRGSS
HSHGLYWFHG SPAPDMATPE ARERFARIWG YHVTAVSPQQ EQGADEGNPL SVDPLETPVT
WEWLNRIVNR CQRHHCSSTY CLRVTKEDAQ RAREAAGEIV GEERPAPEPT CRFLFPRPVR
GAAEVIEMAG KGWWSFEAER NDTHLNQYNP LLSLCWLANT DCSPCTSAEA VINHAAKYCS
KSETQTSTYA QIAQSILPHI SDNNPMISFV SKMMNKLIGE RDYSAQEICH ILLGLPLQED
SRVVQSVDCR PRERHARAID ITADGDIEES RTVYEKYLRR PDHMEDVSYF EFLQNWNFKA
RNPVRWAIWQ APALPRVLYY YPRYKPVRSH QQYSDFCRVK LLLSHPHRQT EDLSQVDDRQ
FDNHASAYRY CLEHHDHPDD HYGTVDEPDP SPDEEEFEPK GDAGDITLED WQEVARLVPD
IELPDERADL LGRRDLDAQL RGETPGNYDV EDMPLTARDT VNTQQRQVYD TIMRHFRAKN
ENRRPPPLRL QIDGEGGTGK SYMVKVISSH LQAKAASYGR PSPVVRAAST GVASNQIGGQ
TLHSLLRLPV DGNYRSLSET PTTLNALQRR FRGIHYLVID EKSMLGLKTL AWIDQHLREV
FPENRDEFFG GLSVILIGDF FQLPPVLNKP LYSTRDDLKD IEMVGRNAYL SFDKSVFLTT
IQRQQGEDQA PFRRALEELR KADVSVPSWE LLASRCSVKL SPEEVDSFAD ALRIYPTKAQ
VVEYNHQHML GLDSPAIQVE AKHEGVGAEK VESSNAGNLA KRLPLCVDCR VILTRNLWAD
VGLVNGAQGT VYDISWKEGA GVLRDPPEVI MVAFDDYGGP AFTMPNGSRS VGITLDKVVC
DISAPEFASG LSYVAVSRVK TLGGLMFERP LDHSRIYRET PSRAMGVEGE ELRIDGEGEV
LLISTPPPRQ LPGKSY
//
