ID   A0A166DXW3_9AGAM        Unreviewed;      1280 AA.
AC   A0A166DXW3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=FIBSPDRAFT_895935 {ECO:0000313|EMBL:KZP15183.1};
OS   Fibularhizoctonia sp. CBS 109695.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX   NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP15183.1, ECO:0000313|Proteomes:UP000076532};
RN   [1] {ECO:0000313|EMBL:KZP15183.1, ECO:0000313|Proteomes:UP000076532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP15183.1,
RC   ECO:0000313|Proteomes:UP000076532};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
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DR   EMBL; KV417607; KZP15183.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166DXW3; -.
DR   STRING; 436010.A0A166DXW3; -.
DR   OrthoDB; 2909243at2759; -.
DR   Proteomes; UP000076532; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR039904; TRANK1.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR21529; MAMMARY TURMOR VIRUS RECEPTOR HOMOLOG 1, 2 MTVR1, 2; 1.
DR   PANTHER; PTHR21529:SF4; TPR AND ANKYRIN REPEAT-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Helicase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1280
FT                   /note="DNA 3'-5' helicase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007872429"
FT   DOMAIN          485..860
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   BINDING         506..513
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1280 AA;  143691 MW;  28120B7393601008 CRC64;
     MIEDALAFSL ILLLPVMPSL LNLASLSPEA LRNETTQLEA LQKIGWALNR NNADQIILLL
     ASKPGLLDLA CFPSAAKAFA SSLGGTLLRQ LSNYLFSVRR VLPPGTQEKL DASRLKVDKI
     PIILTSLSDA NHLSGSQVTS RKKAKIRAAI ENPEVFRTLG ISLPSSAQQA EGLVATLLQE
     QKETLKEYFD VLQDASLAHI FKTEYFSQVQ ITSSGGKPAE VGLTVEEPQS TGTSVLHSAY
     PAVQPKKAAV LSERAAGFGD WCLLLSARAT KDLRELRWND QALLKIILKR MRELSNGNFS
     RDNQKRLNQS SSEVPIYEAK TRDLRLIVTI LFLRSSAIAD KFTQYQVDCV PEYDSSLERQ
     GTSLLTSMAD PAQSGLPSVL RIFGVYNHTQ NDRLWQSMGI QLATKGIEYR RRCIYRKPHF
     PGDDIFVPGT FPPMEVPETK ASKSELDLPH DDLDALHSLL VLEKFVVFSQ ALLNSIVADK
     DVKHIFDVSP QERAIIQHPS SCYVIGRSGT GKTTTMLFKM FLVENGSTML GDKNSPKPRQ
     LFVTQSRMLA GKVEEYFAKL MEALATARYS LEELAILAKS HREEAGLVDL DDQANWRNDL
     PGRFSELQDE HFPLFITFDR LCGLLEADFM TIHRTTGDDI LNRALGEQNE GAMITYDIFR
     DTYWNHFPQL LTKGLDPSLV FSEIMGVIKG SEAALNSPDR FVRKNDYVNL SHRTQSTFAL
     KRGTIYDIFK VYMKHKHDAG HRDSADRTHD ILNALAAGRL VPRNKVDYIL KAYSYISYVD
     EVQDNLLIDA QLLWYLCRNR NGLFWAGDIA QTISVGSSFR FDDLKAFLFR VEERNSPTAG
     VSATVIHPQT FQLAVNYRSH AGIVNTAHTL ISLIAFFWPR AIDTLVPETG LIGGLKPVFF
     HGWNADTVRY EQFLFGTSGE HLEFGAQQCI LVRDDRARNQ LRDEVGDVGL IMTLYESKGL
     EFNDVLLYNF FENSAANLSQ WRVVLNTLPP TSLEVGVPAP RFDDTRHAVI CSELKSLYVA
     ITRARKNVWI VDCSKKGEPM RMVWESKNQV HSCTPGADVP QLAVSSTPEE WAATGKKLFQ
     HKRYIQAIHC FKRASMFREV DVAQAYSLRA QARAIPTNQD VQRKTAFTHV AEAFLQCAAA
     TKKPNERRIY YTIAGDCFII LVAYHRAAET YLAGEEFTKA AISYRKAGNV QEAVEVIKQH
     RRDMDADVAD SGMDFARLSC FRDPDIEVFS LLWGAERVER CDSVAYLRYE PRRGCSPNGC
     LEVSAVENEI YDINTQDLGT
//