ID A0A0C9THL0_PAXIN Unreviewed; 838 AA.
AC A0A0C9THL0;
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=PAXINDRAFT_180755 {ECO:0000313|EMBL:KIJ15140.1};
OS Paxillus involutus ATCC 200175.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ15140.1, ECO:0000313|Proteomes:UP000053647};
RN [1] {ECO:0000313|EMBL:KIJ15140.1, ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ15140.1,
RC ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler 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., 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 (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
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; KN819338; KIJ15140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9THL0; -.
DR HOGENOM; CLU_001103_12_5_1; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000053647; 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:UP000053647}.
FT DOMAIN 148..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 370..521
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 700..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..88
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 742..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 91208 MW; D2C7F38DC4598138 CRC64;
MFGSYDSDHV GSDDMEAILE FSRVQNRGEV GVAGPSKETA QPSYLRKHEL SARLSALESE
IQGVDEQVQK LKALRQSLLA EKQEVLRQTQ AISHAQPATT AAINGKGKAK TSGTIDYAME
FDWAPQLKGT MKKVFGISSF RLCQQGGCNA NMDGRDVVCV MPTGGGKSLT YQLPALLTPG
CTLVISPLIS LITDQILHLR EAGVEAAMLT GGTSKALANE IQQRLTAMAS ARGGGQQGDI
KLCYVTPEKI AKSKGFMSLL RKLVEGGKLA RIVIDEAHCV SQLGHDFRPD YKKLSALRQF
FPHVPILALS ATCPPRVLQD ILKILHMKPV VDGKAAPREG TVYFSAPLYR KNLHYSVVPK
PSSAKEVVSA MSQYILQNHE HDSGIVYCLT KKDAETVATS LQDVSNGRIR TGVYHADVAD
GQKEGLHRQW RDGSIQVVCA TIAFGLGIDK GNVRFVLHHT MSKSLDGYYQ ESGRAGRDGQ
DADCLLYYRP QDATRQSSIT CTDTDGTAKL HDMLRFAQDM QECRKILFAK YFSASSDLSM
TSWTTEESSA MDKCGHCDNC TRAPETIEHK DVTIEAWQIL KILEAVDAQG GRQTIAGLSD
LARGLGGGSF EASGKRKKSK EKVQLDYDAV AGGKVGLSKD DIETLTVQLL VSRYLGEAFS
STAYTVNVYV IPGELALRLT RLTRAEVVHG NGPRIHCSFK RQTRKGKASA AGAGTKRKTA
ARDGGDGGDV SVATVAGSSR PRKRLSLHDP VHPESEEEED RHVPGLAKKK KRLHAEAGKE
DEEDEDFTNA IRMVNEAEPS DAESDVEDGG WEYSLRPSKV DKQPYIDSGV ISLSSDSD
//
