ID A0A0D0DTV2_9AGAM Unreviewed; 842 AA.
AC A0A0D0DTV2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 08-NOV-2023, entry version 32.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN ORFNames=PAXRUDRAFT_31795 {ECO:0000313|EMBL:KIK97438.1};
OS Paxillus rubicundulus Ve08.2h10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK97438.1, ECO:0000313|Proteomes:UP000054538};
RN [1] {ECO:0000313|EMBL:KIK97438.1, ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK97438.1,
RC ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR EMBL; KN824936; KIK97438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0DTV2; -.
DR STRING; 930991.A0A0D0DTV2; -.
DR HOGENOM; CLU_001103_12_5_1; -.
DR InParanoid; A0A0D0DTV2; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000054538; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase 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; 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; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF72; ATP-DEPENDENT DNA HELICASE Q1; 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 SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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, ECO:0000256|RuleBase:RU364117};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW Reference proteome {ECO:0000313|Proteomes:UP000054538}.
FT DOMAIN 148..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 370..519
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 697..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..88
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 745..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 91907 MW; 332BD501E53B7E46 CRC64;
MLGGYDSDHV GSDDMEAILE FSRVQNHREM GVAGSSEEAA QPSYLRKHEL SARLSALEYE
IQGVDEQVQK LKALRQNLLA EKQDVLRQTQ AISHAQPAIT AAINGKGKAK ASGTIDYAME
FDWAPQLKGT MKKVFGISSF RLCQQGVCNA NMDGRDVVCV MPTGGGKSLT YQLPALLTPG
CTLVISPLIS LITDQILHLR EAGVEAAKLT GGTSKALANE IQQRLIEMAS SRGGGQQGDI
KLCYVTPEKI AKSKAFMFLL RKLVEGGKLA RIVIDEAHCV SQLGHDFRPD YKKLSALRQF
FPHVPILALS ATCPPKVLQD ILKILHMKPV VDGKAAPREG TIYFSAPLYR KNLHYSVVPK
PSSAKEVVSA MSQYILQNHE HDSGIVYCLT KKDAETVAAS LQDVSNGRIK TGVYHADVAD
GQKEGLHRQW RDGSIQVVCA TIAFGLGIDK GNVRFVLHHT KSLDGYYQES GRAGRDGQDA
DCLLYYRPQD ATRQSSITCT DTDGTAKLHD MLRFAQDIQE CRKILFAKYF SASSDLSMTS
WTTEESSAMD KCGHCDNCTR APETVEHKDV TTEAWQILKI LEAVDVQGGR QTIAGLSDLA
RGLGGGSFEA GGKRKKAKAK VQLDYDAVAG GKVGLSKDDI ETLIVQLLVS RYLGEAFSST
AYTVNVYVIP GELALRLTRL ARADVVHGKG PRIHCSFKRQ ARKGKASTAG AGTKRKTGAR
SDGDGGDVSV TTVAGSSRPR KRFSLDGPAY SESEEEDRHV GSLAKKKKKR LQAEVDEEDD
EDFTHAIRMI DEAEPFDVES DVEDGGWEYS LRPPVQGALR APSKKVNETF YIDDDVISLS
SD
//
