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Database: UniProt
Entry: M7SVY2_EUTLA
LinkDB: M7SVY2_EUTLA
Original site: M7SVY2_EUTLA 
ID   M7SVY2_EUTLA            Unreviewed;       807 AA.
AC   M7SVY2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Putative atp-dependent dna helicase recq protein {ECO:0000313|EMBL:EMR68658.1};
GN   ORFNames=UCREL1_4326 {ECO:0000313|EMBL:EMR68658.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR68658.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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DR   EMBL; KB706200; EMR68658.1; -; Genomic_DNA.
DR   RefSeq; XP_007792248.1; XM_007794057.1.
DR   AlphaFoldDB; M7SVY2; -.
DR   STRING; 1287681.M7SVY2; -.
DR   KEGG; ela:UCREL1_4326; -.
DR   eggNOG; KOG0351; Eukaryota.
DR   HOGENOM; CLU_001103_9_2_1; -.
DR   OMA; TVENFVY; -.
DR   OrthoDB; 5474026at2759; -.
DR   Proteomes; UP000012174; 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   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   CDD; cd18018; DEXHc_RecQ4-like; 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; 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; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF150; ATP-DEPENDENT DNA HELICASE RECQ; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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, ECO:0000313|EMBL:EMR68658.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012174}.
FT   DOMAIN          80..264
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          291..434
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          19..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..743
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   807 AA;  90209 MW;  D36FA7DA304E1384 CRC64;
     MSDYDSGDDL LADVNIDTLV SSSKRSRPDD DSGHDQSEQD HVSKRTKVEG SDANLDAIAR
     QILKEKFGYD DFRHEQRSAI RSVLRGENTL VIFPTGAGKS LCYQIPGIAF EKLDTEDGSQ
     RSNGSGITIV VSPLIALMKD QVDALKRRGI AADCLDSTKT YEQSKDINAS MREGRLRLLY
     CAPERLNNEG FVESMKYVAG GVRLVAVDEA HCISEWGHSF RPDYLKVARF TKEVKAEKVI
     CLTATATPRV AEDVCNAFEI KETNVYRTSP YRPNLQLFAK SFKTKKEKYP KLLNFLNKYR
     GSTLIYVTAQ KQTEDLASQL RKSGFIAMSF HAGMKTEDKT RVQDEFMASR IPIVVATIAF
     GMGIDKADIR NIIHYDLPST IEEYSQQIGR AGRDGLQSHC VLYICREDFY IKENFARGDL
     PSRNSIQGLL EDLFSQEVIS VPNGEGFKVV HNQLSQDYDI RASPLTIILA TLELRFGLIR
     AITPEYSSYK YEATTKYGYF AQKETSRQGK AIFANAKKAV KWYDIDVGAV AWREGIPRND
     IVRRLNELHD AGALILRVSG VQNKYRILKP LPQSSEEIDD LAGRLHADME AREVDALNRI
     DQVASLITGS RCFALTLAEH FGTGLPNGRT TCGHCTYCLT GKPVTLTPKP RPEDRPVDID
     AIMKILDACD VRDDPRFLAR VAFGIKSPRV TRLKLDRLPE FASLEDHDFD SLLKEFTRAC
     DADAREPNAI RKPAVKRETS STRGKTTRGS SSQRGGSYSQ RGGSYSQRGY SSQRGGSYGQ
     RGSSQRGSYG QRGSYSKRGS YTGGVWY
//
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