ID Q2H9J7_CHAGB Unreviewed; 743 AA.
AC Q2H9J7;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=CHGG_03107 {ECO:0000313|EMBL:EAQ91172.1};
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:EAQ91172.1, 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; CH408030; EAQ91172.1; -; Genomic_DNA.
DR RefSeq; XP_001229623.1; XM_001229622.1.
DR AlphaFoldDB; Q2H9J7; -.
DR STRING; 306901.Q2H9J7; -.
DR GeneID; 4388962; -.
DR VEuPathDB; FungiDB:CHGG_03107; -.
DR eggNOG; KOG0987; Eukaryota.
DR HOGENOM; CLU_001613_0_1_1; -.
DR InParanoid; Q2H9J7; -.
DR OMA; ANCMAPP; -.
DR OrthoDB; 5474774at2759; -.
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:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; 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 CDD; cd18037; DEXSc_Pif1_like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049163; Pif1-like_2B_dom.
DR PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR Pfam; PF05970; PIF1; 1.
DR Pfam; PF21530; Pif1_2B_dom; 1.
DR SMART; SM00382; AAA; 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 319..484
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 80798 MW; 217885F65314960C CRC64;
MFSRAVEANK AAPAKQSLSQ QLFPSSSPSP APGKRVENTI DGMFTKKPHA PAANGPSRST
TTTKPLQSHP LNVPPSAPRN PNGKSLASLY GRSDSFKEEP EVVDLRDDTP QYTNNTAQII
SIESSFALDE ADFSNDEDLE LDFQPATALP AIPSQQHQAT AENRDAHPPA SNTSALSWPD
SSPSHLRPPS PGTAALPPQN SSKRASPGED DDRALSAPKK TRRELPGRWS TLESLENTYG
AAAATPAPKK KEDGLWNTSA SAVGERKKQL KAQLKESGKG EASVDDMQEA VKSHTVKAKA
TAITLSNEQR HVKSLVVDKG QSVFFTGPAG TGKSVLMRAI IQELKRKYSK DPERIAVTAS
TGLAACNIGG MTLHSFSGIG LGKEDTNTLV KKIRRNPKAK TRWLKTKTLI IDEVSMVDGE
LFDKLSQIGR IIRNNGRPWG GIQLVITGDF FQLPPVPEGG KQRESKFAFD AATWSMSIDH
TIGLTEVFRQ RDPGMPTPQT LSGKSYRYDA KDTGDDKVRD RLLANMMAPP TIELKKGAQV
MLIKNMDETL VNGSLGTVVG FESEATFEMR GGEDDDDDDS ETKRRARVFA NALAQAAKGR
DNTEYPVVAF HAVDGTQRRI LCVAEDWKVE LPTGEVQASR RQLPLILAWA LSIHKAQGQT
LERVKVDLGK VFEKGQAYVA LSRATSKEGL QVLNFQKTRV MAHSRVVEFY DKLYSVEVAL
QKKAAGPITN YTVKQPVPAG ASS
//
