ID M1VWJ7_CLAP2 Unreviewed; 1751 AA.
AC M1VWJ7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Related to QDE3 protein (Involved in gene silencing) {ECO:0000313|EMBL:CCE31392.1};
GN ORFNames=CPUR_05245 {ECO:0000313|EMBL:CCE31392.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE31392.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE31392.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE31392.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE31392.1}.
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DR EMBL; CAGA01000030; CCE31392.1; -; Genomic_DNA.
DR STRING; 1111077.M1VWJ7; -.
DR VEuPathDB; FungiDB:CPUR_05245; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_16_1_1; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000016801; 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 Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016801}.
FT DOMAIN 867..1048
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1079..1220
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 69..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1580..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1458
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1713..1730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1751 AA; 193445 MW; DE8ECB617D1318DC CRC64;
MAARMTSIRT LKDIAFVPSI GLGAGFRQLS LLVGRISSSG SSLLGFMTRN NLANQVSWLL
QNITLSRPPQ PALPPANNTS VSRESQSFQL ARGESQSVIS TTRSSETVID RRARPSSNVS
TLTGWGEDSI DIPQVIEVAD DNMVRLTSTS KSKRPSLISH THNPLPTPLG TDEARPKSRH
DAHDQHTGLS TPKNKRHKSP RKLVPASAPS PQFTDFDGDE FECLDLTTDF TGDNTPKNNH
VQFRDAGSTL RSPLPAKSSR KRKSNDLSRT DATQEENFPD VYHVLGTEPP ASTPANRSAT
HRAGLSSVTK SGRKRHAKET PARLSRDISS DPLQDLIVDM SSPSRRVIDR RDHSETSRSP
RKSAARRPER SDESCKKRKA YHDNPYEGIL PSVVEQESSP RQAELIRKDD CIPDSDEECL
APPQYNASVA SQPPKPSSSS ESASNPSKNL LSDYSRGSPS LASCDDTLQR TIPPDQTPKV
LECLNQNSQI VAARRETIVL EIQRNGADFM RAVTERWPKE KRGEIKREKE RLQRQQKAVQ
ELSDSLESYG KLCAQREKLA QQVALSYADG IDTEEDEARL DELTDVIQER EVALARLVVS
AGFDESHVPM LASNGSSAGN TRSNVVFGTQ SLGSPAIDTS RTPLLNQGSA GGASTQVVQQ
TQSSGSSQHM ARAAPLRNQS LMAEEAGDRF AERAFPRQTP TRSGASRAQM VADVPTPEEE
DEVEFDEFDE SELRLSVPSA SARFRSTDTV SRNDNTATRR THQPRDNFSD FSNDDEVLAF
AEGLDTRQSF ENEPAISRTV FSEMSGNVMP PAKSKVPPIG RLCAGIVVPE LRMPPELMKH
PWSPEVQKML KDRFRMKGFR HNQLEAINAT LAGKDAFVLM PTGGGKSLCY QLPAIVKTGK
TRGVTIVVSP LLSLMQDQVT HMKALGIQAV AFNGECSAEY KRQVMSAFEE RSPEHFVELL
YVTPEMVCRN AAFNNAMQTL YRRGKFARLV IDEAHCVSEW GHDFRPDYKI LGQVRQRFPN
VPFMALTATA TKNVIVDIKH NLDMTNCQVF VQSFNRPNLY YEVHPKTSNT KATECIASLI
NTKYPDVTGI VYTISRKQAE EVALKLRTEG IAASHYHAGV DPQQKVRVQA EWQKGEIKVV
VATIAFGMGI DKPDVRFVVH HGIPKSLEGY YQETGRAGRD GLPSDCILFY GKADIVMLKN
FVDLGEGNAE QKERQMVMLN RVASYCDNKS DCRRTEVLRY FGEDFQPSQC QKRCDNCRAA
LVFEQQDFST YAIAAIQVVK AQERLTANQC ADILLGRRYP NGMPHLSDEH FGTAKGLKKH
EVVRVIDKLS AEKAFDELNV VGNYGVAIQY VQMGPTSHLF LNGRRKLMLT IPVDEKKASG
SSKAKKPTRK NKAKDSDMSA MQSTYVSSPI EKRKRRTRAV ESESNDENDY PMTSHGYEND
GFVVEEEEEE EEEDDDDTFE PLPKHRPAAA PTKKRTAPAP GPPILKNKSL EDLQEIHQDV
VNTFVREARK IEEHIRNKKE LRRPLFTEND FRQMAIHWTT SLDAMSRITG INAEKVWEHG
PRLLPVLKRH HSWYQEITGA KEEEEDANDQ VRQERADPDI VDLISSDIEM ATEDDLVQPD
GAADSHYFQP QPRPEVAAFH SKLQGLSSQQ PSQFKAKAAA PYARGGGRKT PGFKKWSRKS
GGSGSGAAAG GGGGAAAPRR RSGGASGAKR GGGSASASAS TASRATAGSS GGRRNGKLVK
KSGGTIGLMP P
//
