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Database: UniProt
Entry: Q2H3E6_CHAGB
LinkDB: Q2H3E6_CHAGB
Original site: Q2H3E6_CHAGB 
ID   Q2H3E6_CHAGB            Unreviewed;      1058 AA.
AC   Q2H3E6;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=CHGG_06819 {ECO:0000313|EMBL:EAQ90200.1};
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:EAQ90200.1, 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; CH408031; EAQ90200.1; -; Genomic_DNA.
DR   RefSeq; XP_001222914.1; XM_001222913.1.
DR   AlphaFoldDB; Q2H3E6; -.
DR   GeneID; 4391328; -.
DR   VEuPathDB; FungiDB:CHGG_06819; -.
DR   eggNOG; KOG0987; Eukaryota.
DR   HOGENOM; CLU_289670_0_0_1; -.
DR   InParanoid; Q2H3E6; -.
DR   OrthoDB; 1953012at2759; -.
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: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; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR046797; PDDEXK_12.
DR   InterPro; IPR049163; Pif1-like_2B_dom.
DR   PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR   Pfam; PF20516; PDDEXK_12; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   Pfam; PF21530; Pif1_2B_dom; 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          241..478
FT                   /note="PD-(D/E)XK nuclease-like"
FT                   /evidence="ECO:0000259|Pfam:PF20516"
FT   DOMAIN          908..940
FT                   /note="DNA helicase Pif1-like 2B"
FT                   /evidence="ECO:0000259|Pfam:PF21530"
FT   REGION          13..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1058 AA;  117735 MW;  415CA142E39F66A7 CRC64;
     MSNNPAIYHW LSSLPDCHEG HCGETTSVKH KPKRTRGEMT TPPSSTARTG SLSPGPKKRK
     IDDSRPDSHG PDPDPDATPR SGRSQRPSVT TLSMRTAFPP PSDSSAASAV SSRQDRSSRS
     SRRSASPVKN ITGLQRLDKP VLFDSLDDNA GLIQLPEDVR ELYYNIFAAT KYQSGIYPAE
     IRTEIEALYT GHPPPDSVYR KPGGGNDQDG IGQEEEHFFD YLPVSALFSG TAEGATSQAR
     IAHAEFYKVR AIKDRARECL ALRRAEAAWN TKVHEPLLEL ALSRRHTSVI CENATSARIL
     PCFLPCLITG EVAEGKMVDF VLAPNLGSES ELDIAIQNKL VELAKQMRSS GLISARLCVN
     QTDYPPLMRS PAAVTMETKV AGASLEEGRL QLGVWIAAWH RRMEMLGVGG GKSGPQLPTL
     PLILTHDHEW SLYFAVDRLD KIEIFGPMQI GMTDNLPNIY QLLTVLGFLG AWIDTTFRTW
     VINAFQQWLN IEEDGTGGKR LTARLLYYYP RYKPVRSHQQ YSDFCRVKLL LNHPHRQSEQ
     LLEVDLGLDN KGLGLPLPEE DEFERGEDAG DITLEDWQEV ARLVPDLQLP HNLPEERVPR
     VKVPGRDMET LQQRQVYDTV MRHYRAKNEN RQPPPLRLQI DGGGGTGKSY MVKVISSHLQ
     AEAASYGRVS PIVRAAPTGV ASNQIGGQTL HSMLRLPVDG NYRSLSETPT TLNALQRRFR
     GIHYLVIDEK SMLGLKTLAW IDQPLREVFP ENRDEFFGGL SVILIGDFFQ LPRVLNKPLY
     STRDDLKGIE IVGRNAYLSF DKSVFLTTIQ RQQGEDQAPF RRALEELRKA DVSVPSWELL
     ASRCSVKLSP EEVDSFADTL RIYPTKTQVV EYNHQHMLGL DSPAIQVEAK HEGVGAEKVE
     SSNAGNLAKR LPLCVGCRVM LTRNLWADVG LVNGAQGTVY DISWKEGTDD FMVGANSCSR
     EQFPLLVSYA ITVHKSQGIT LDKVVCDISA PEFASGLSYV AVSRVKTLRG LMFERPFERS
     RIYRETPSPA MGLKLSDHAT RQLQALDAVA GEVPSESN
//
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