GenomeNet

Database: UniProt
Entry: M7TV65_BOTF1
LinkDB: M7TV65_BOTF1
Original site: M7TV65_BOTF1 
ID   M7TV65_BOTF1            Unreviewed;      1789 AA.
AC   M7TV65;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=BcDW1_6170 {ECO:0000313|EMBL:EMR85175.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85175.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(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};
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DR   EMBL; KB707917; EMR85175.1; -; Genomic_DNA.
DR   STRING; 1290391.M7TV65; -.
DR   HOGENOM; CLU_000335_0_4_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR   PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02889; Sec63; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00973; Sec63; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EMR85175.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          451..625
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          668..853
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          51..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1371..1434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1498..1569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1685..1763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1400..1414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1502..1519
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1526..1559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1692..1720
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1789 AA;  198519 MW;  440AB9FED5C2F447 CRC64;
     MDRSWDPHLQ RIANGTIGNT SDGVPHHEDG KDAGFSTNFF IGKDSQQLPP GPGFTFGPSP
     MQHNQQVSGP YGQDVDVRGR YNNTGGHNQS SGYLMAPREE PPTAGFSFAP APRQPGQRMS
     SLGQNTDVRA SYDLPVHDPL QGYLSRPSFE LSQPMQRLAP HSTAGIGNGQ GRLSLPRFSS
     HVGGQAQSKA RERKEPRDLT STDDHFKQQI LQDIELKPKP RNIPARLSNS GVGEGQSPLT
     QLANNMISQT SMLMPRALGL SPSKQNIFQS QLERPLQFQQ KNQQVSTPPS TRMDLGAFAY
     KPPERMNTTL NSSPLQLPVS SPSARVSSRR NSNRRLPPHN TKETGQGFEH QYTAPHTPHN
     QASPSNRYAL SSTASQAQEM GRGVETFGFS PAKTYPGSVG QFKNDHQIIP FGNGPPKAHG
     IQLVSPHELP DRFRQVFPYE LFNAVQSKCF AQIYKTNNNI VISAPTGSGK TALLELAICK
     LVESYGSGQF KIVYQAPIKS LCSERMRDWT KKFSHLNLPV AELTGDTSNA EMSRVGNASI
     IITTPEKWDS ITRKWTDYQK LLQLVKLFLI DEVHILKDAR GATLEAVVSR MHSIGASVRF
     VALSATVPNA HDIATWLGRD SSSRQLPAHR ETFGEEFRPV KLQKHVHGYE SRANDFAFEK
     ILDGKLPALI QKYSCKKPIM IFCFTRKSCE VTATILAEHW TRQRVVDRAW PTPTTRTVVG
     SKDLQELVGC GVAYHHAGLD AQDRCAIETA YLKGDISVIC CTSTLAVGVN LPCHLVVLKG
     TVCFQDSGLV EYSDLEVMQM LGRAGRPQFD DSAIAIIMTR MDKADRYKKM ISGQDILEST
     LHLNLIEHLN SEIGLRTIKT AYEAKVWLGG TFLSVRMRQN PKYYKFSGVA PSRDADEQLE
     LVCERDIKLL QEYELVTKEE NFSCTDYGAA MSRYMVQFET MKLLLSIPRH SKTEVILNTI
     CQAAEFKDLR MKPNERSSLR EFNKSPMMKF PIKENISTTG HKIFLMIQVQ LGGIEPLTNN
     DFRVISRQFA METNIILERF QRLIRCVIDC KAVDCDSISV RCALDLSRSV AANYWENSSL
     QLRQVPQIGP ASLRKLAGNN VNTIEKLSGL DTAGVERVMG KNPPFGKKMK DILIEFPQLT
     LTAQIVGRAF SKQGEQPKVK VNAVLGYSNP KIPNWSGRIP SITFIAETSS GTLVFFWRMN
     IKKLSNGGSK QEFTVELSSP DDEIKCWLAC DEIVGTLKSC VLQHHVPASE FPPPKAMIER
     PSIKRSKAQE LGICDEFNDG IDEDAMLAVA KQIEGGRRAS SDYGSDAFID IDTVGLDNSK
     ENKKFNEEVV ELEPVKMENG KWACNHHCRD GNTLKNGQIC KHRCCREGLD KPRKVTRKKS
     STGITGDQGS KIDDKIKGSV TKPSMSNPQP PGMKQLSKLT KKPKLMQSSG PSSDQDIVEV
     VDLSRTLLPV TYPDVAPRDY RKLHNLHTSI QKDTSVRLPK GQPRFSYASG KMPNFSFMYN
     DGSKNDEKDE PEHFDSDEYE FPSPSALLSS EKQASKGVSI SATQLPPPAM SVDISRQDGN
     EQQAHSDDPF EDSFGSLEAA MIGLDDSINL RTGPAAPNAP ATPKLNTSFA NNVFDFAAFN
     SEEVNEQQFS SPLMNQIQRK HQEGEMDEMD IGMPSIKRQQ SSPWMKDFQN GDVMGYDQWG
     ENENEGYDGP VLPQMKRRKI DGGDEDGDRG GMESIGKDPE DALKSTSGSS APAWANKTGS
     GIMGSDIGNG GDDEQKGNLK ANVRQEPAWV GEMDPDFIDM FRGYVDFVD
//
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