ID A0A166TAN7_9AGAM Unreviewed; 2022 AA.
AC A0A166TAN7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=FIBSPDRAFT_1038371 {ECO:0000313|EMBL:KZP30411.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP30411.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP30411.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP30411.1,
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV417494; KZP30411.1; -; Genomic_DNA.
DR STRING; 436010.A0A166TAN7; -.
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; 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 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}.
FT DOMAIN 271..639
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT REGION 1716..1743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 292..299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 2022 AA; 229616 MW; 9784AB749BAB2135 CRC64;
MQQAEGLVAT LLQEQKEILK EYFEVLRDAS LAHIFKTEYF SQVPSSSKPA EVGLTVEEPQ
STGTSVLHSA FFSERAAGFG DWCLLLSTRA IKDLREARWD DQALVDNILK KMRELSNGNF
SGDNQKRLNG SSSEVPIYEA KTRDQRLIYQ VDCVPEYDSS SERQVLRIFG VYNHTQNDRL
WQSMGIQLAT KGEEYRRRCI YRKPHYPRDN VFVPGTFPLL EVPETKASKS ELDLPHEDLD
ALHSLLVLDK FVVFSQALLN SIVADKDVEH IFDVSPQEWE IIQHPSSCYV IGRSGTGKTT
TMLFKMFHVE NRSTMLGNKN SPKPRQLFVT QSRMLAGKVE EYFAKLMDAL TTARYSLEEL
AILAKSHRED AGLVDLDDQA NWRNDLPDRF SKLQDEHFPL FVTFDRLCGL LEADFMTVHR
TTDDDILNRA LGAQNEGAMV SYDLFRNTYW DRFPQHLTKG LDPSLVFSEI MGVIKGSEAA
LNSPDRFIHK NDYINLSHRT QSTFALQRNA IYDVFEVYMK HKHNAGHRDS ADRTHAILNA
LAAGIIPHKE IDYIYVDEVQ DNLLIDAQLL RYLCRNQNGL FWAGDTAQTI SVGSSFRFDD
LKAFLFRVEE HGNAPTTTGV SATIIHPQTF QLAVNYRSHA GIVNTAHTLI SLITSFWPHA
IDTLAQETGL VDGLKPIFFH GWNADTIRYE QFIFGASDGH IEFGAQQCIL VRNDRARDQL
RDEVGDIGII MTLYESKGLE FNDVLLYKFF ENSTATLSQW RVVLNALPPM SLGVPAPQFS
DTRHAAICSE LKSLYVAITR ARKKVWIVDC SDRGEPMRMV WESKNQVHSC TPGANVPQLA
VSSTPEEWAA AGENFFQHKR YIQAIHCFER ASMFREVDVA KAYSLRAQAR AIPTNQGVRR
RTAFTHAAEA FLQCAAATNK TNERRTYYTI TGDCFIILVA YRRAAEAYLA GEAFTKAAIS
YRKAGNFQEA VKVIKQHRRE MDTDVVNRVM DVARLDCFRD RDIEESQILS QTKELFEGDM
KQAMSFFSEY GFDSARATLL VQLGDPVEAA GIHFGAGRLN DGIKVLLKHK GSMPCAKFAA
KCTIEAFWKS LSFGVGVDDV ADRSTLNQWR KVAEQLDSSM LSQRELSEIA MFNAIFQKDT
KRLEQLGLEF YKEKNMHAAL LCLDHIFTNT PSLQGLSAGE TVKTLEMFFS YATLLRDIAC
FKDPCGNEQI RKVFGFVELR EDVFAMTPGS TLHREVANQQ MFFQDKDGHR TVSRNDASRV
IRRYLTDRLR QRVLEENKTC RAAKSLQPSA YPCIDALAGT CKTHGCQHAH IKPEDISLSW
YQNRVRAHLL QIQIYQTLHF IDLGPGTHRE DEQRYWLDRL YTEINPNLYV FGCRESLDLS
VIPGNEKALM IVLNWAKHMI YTADANAPTF LTNFLQAALL GLGQDSQGTL EAIRQAPYLA
YNFQPPTKLV RPLRYHRDGF YVMHDLARYL DKSDPLCVKS GVMFIRHFVT TMVPMRTSLA
CEIFEDLCTA FVVLMHPSLH GVTLPRSWLS RLLRNGRPRG DRHLHSELVE LILNLIGKLH
ASLGTENLPQ TEDAFGMVPV VSRQIYIFRL CRSLCLLGQN LNNRVLRDRI GHRIAYFNRR
GMQQPELYRR YFEANHWHHL SQAACDSMNG SPMDEIVQLY QENPRHHIGT PRGIRRIVFK
QAGDVPALLE FFDKPVSANS GMTSGTKIGS IASTLRHPPI TDQDTNLMTK SPPNRQEQSQ
PTADKIRRVV SPLADSQTSG QDVDFSTAAI VFSTDDHPQS HSIIRINPRP EDVELQETNA
PEEETDEPQM DLTVDADALA QSLQSTSGQV VSNAPTEEQI HAALRIQTAY RRLLRYRRTS
ARTGLSAARN RHFLKCRLES EKMDWPRGGF CLSPPRYRVL FLGPIPHLLV CLERARTVAW
EDALKAKMRV ATAKHEDLED VQKKVKTAND MVEKVCQLEQ ALGAQGVVHR SQDYTTLEQL
VCDAIHLTRK LSCAKQMEED LSLVAKAIIK QRQPPARNQN QP
//
