ID A0A2C5Z8K6_9HYPO Unreviewed; 1669 AA.
AC A0A2C5Z8K6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDD80_7217 {ECO:0000313|EMBL:PHH78195.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH78195.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH78195.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH78195.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHH78195.1}.
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DR EMBL; NJES01000088; PHH78195.1; -; Genomic_DNA.
DR STRING; 2004952.A0A2C5Z8K6; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000226431; Unassembled WGS sequence.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000226431}.
FT DOMAIN 784..965
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 996..1137
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 28..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1515..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 514..541
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 36..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1373
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1669 AA; 181729 MW; 6420FFA6C6F136D7 CRC64;
MTRNNLAEHL TWLMSNVSST KPAAHVFPAP SQLSQAPPPT RSQTSQTSTA SRSRAPDPVD
FPPVGDPEVI GHGLSVSRQS TVEAHSGSSM GRLTSTTKSK KPLLVSQLPQ QLPTPSATGD
ERARQRKAGR AVQDAGGGGA STARSRAQSN KQTPRPATSS GLNLDFTGFD DDDLEVMDLT
EETVASGGSL EFGDDVKLWD EKTAHWSSPA PCRSARKRKC HQPGPEEEFP DIYQILGTNP
PASTPRTGSA AGHHASALGS SRSRRGEAGN ESARSHSAKS RRVADLSLVI EELSSPSRRV
AERRDQLTSD KTPGSSSRDG PKRRRVSVEP PVFALSSGDE AARPVKPGCV PDSEDEFVTP
PSRSANTRFA DEESGGKSIV KAEADNCERE TVVGGSAPGV SAVDAAMAAL HSPPSGHAPK
LLTLLSADEQ ALNRCLASLE SRIQQNGRDF SRAVIERWPR EKRDAIKSEK ERLLKQRSAV
AELSGSMESY KAICERRESL ANQVAQSYAN GLDTDEDEIR LDELTDQVQE MEQQLIRILT
DAGLDRTSFF EPSNDAVDVL GTQPSYGGAM DTSGESTVIA AAGTQVVQQT QLPRPRRNEA
VSAEEDSWDE GVAQELNQFK ADQSSKGKAV ARHISFDVPD DLFSELGDDD AAPLPAPRRP
QSKSVSAPPN TTSALPRARS HTDNFSDFSD DADMLAFAQD YETRQSGRGP TPRRSRQVLS
PASGNATSSS SKVHGSPKRS MPPASAVLSI PPELMRHPWS PEVQRILKDR FRMKGFRHNQ
LEAINATLGG QDAFVLMPTG GGKSLCYQLP AVVKTGKTRG VTIVVSPLLS LMQDQVEHMK
ALGIQAVAFN GECSTEYKRE VMSAFEERNP EHFVELLYVT PEMVSKNTAF TRAMESLYRK
GKFARLVIDE AHCVSQWGHD FRPDYKTLGQ VRLKFPEVPV MALTATATKN VIVDIRHNLG
MARCQTFSQS FNRPNLFYEV QKKKTNADAT DKIAALIKAK YANATGIVYT ISRKQAETVA
ETLRDQGIAA RHYHAAIEPR EKAQVLASWQ KGLVKVVVAT IAFGMGIDKA DVRFVMHHGL
PKSLEGYYQE TGRAGRDGKP SDCILFFGKA DIRVLKKLIQ DGEGSAEQRE RQMVMLNRVT
SFCDNMADCR RSEVLRYFGE DIGPEQCQKQ CDNCRSGLVF ELQDFSTYAI AAIRVVQKQR
RLTAVQCAEI LLGKKYPKNE EELSGDYFGV AQGLKKHELI RVIDRLSAEK ALNEDNVVGN
HGMAIQYLQI GPTARQFLAR ERQLKLSIQV DEAPAASKTG KTTRKKKSRQ SPPVQSTYVS
SPMLDRQRSR PQQRASSDDH GLTSNGYVND GFVVSDQEMR DCDDDDDDQD DEDAFEPLPK
HRPPRPPAVK VSGRRNTLGP QITVDERLSS LPEIHQDLVN AFVIEAQKVE ERIRNAKELR
RPLFTERDFR EMAMSWTTSL DKMSRIPGID AAKVAEHGPK LLPLLLQHHD LYKQILAASG
ADQDDEVVDL ISSEVEADGD DDDDGDGLAK TGIDSHYFGA PSANPPAQTA QVQAFHNRLQ
GLESQQSAST PSSRPSKPAS SSTFRGGGPN RKFSGRRWQK RSGNGGSSGG NGGTAPRRRP
SAAASARRAS GSSSGPAARS AAGAGAGASL KRDGRLGKRA GGGIGLMPL
//
