ID A0A0C9TK46_PAXIN Unreviewed; 962 AA.
AC A0A0C9TK46;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=PAXINDRAFT_158355 {ECO:0000313|EMBL:KIJ07676.1};
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:KIJ07676.1, ECO:0000313|Proteomes:UP000053647};
RN [1] {ECO:0000313|EMBL:KIJ07676.1, ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ07676.1,
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:RU363044};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU363044};
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|RuleBase:RU363044}.
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DR EMBL; KN819816; KIJ07676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9TK46; -.
DR HOGENOM; CLU_307388_0_0_1; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000053647; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd18037; DEXSc_Pif1_like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049163; Pif1-like_2B_dom.
DR InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR InterPro; IPR011320; RNase_H1_N.
DR InterPro; IPR037056; RNase_H1_N_sf.
DR PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR Pfam; PF01693; Cauli_VI; 1.
DR Pfam; PF05970; PIF1; 2.
DR Pfam; PF21530; Pif1_2B_dom; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF55658; L9 N-domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU363044};
KW DNA damage {ECO:0000256|RuleBase:RU363044};
KW DNA recombination {ECO:0000256|RuleBase:RU363044};
KW DNA repair {ECO:0000256|RuleBase:RU363044};
KW Helicase {ECO:0000256|RuleBase:RU363044};
KW Hydrolase {ECO:0000256|RuleBase:RU363044};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW Reference proteome {ECO:0000313|Proteomes:UP000053647}.
FT DOMAIN 122..479
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 779..926
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 962 AA; 106495 MW; F5D3208445366DF4 CRC64;
MPKTARKKYY AVRVGREGPT IYDTWAEVSR WPGAIHKSFT SRAEAEQWVS TPHPMEHTLP
DGGYPWQTTT ASTPSSRTIL DAAESSRHTP NLEPIPRDLD AVHTPNIVLS QEQRAVLEMV
QRGENVFFTG SAGTGKSVLL REIVEVCGGR GHAGLAITAS TGIASVNVGG TTVHSWAGIG
LGQEEGMFVI VGEGCEPLFW MKVRRPYQYG TTFANHSAQV SMIDGVLFDK LLPPVPDLDK
HGNPVPPAFA FEAGSWSRCI KRPVVLTKVF RQKEQAFVDM LNLMRFGRLD DETIQAFYKL
SRPLHYDDGI GPTQLYPTRA EVNRANQTRL HALPGQVIQY DATDTAGSDS NGVRVSEQQM
ERLLERLVAP RVIQLKVGAQ VMLIKNMVQG ELVNGSVGQV IRLSTSQEAM KNHTEIATEE
GLRGSQREAR QVTTTYDGSV WPVVRFTNGR ELLCIPTDFT VDNAYGEMEA RRRQVPLILA
WALSVHKSQG QTLERVKVDL SRTFEKGQAY VSLSRATSMN TLEVLNFIPS KVMVHPRVLA
WQNDLEQEEL MKGLEHDGGY WSDMDADEVQ GAFWVTTRNS EDTTFDFYGY MSNTRRYYAV
RIGREGPRIY DTYTEVSNFK LAPCPIVPAP VEDFANDSQF AAATLGLSGS SGKGFDNIHD
AQKWLTEYQY HFGSGSPLTT VHTNINVSLN ISAATAVNEG AASASTSTTT TTTTTFATTA
DRPWKQGSTQ NTSVFNVQGS PHQGYERQRF DQMQAPPPVT EPEIELSDEQ RDILAMIRAG
RNIFFTGPAG TGKSVLLRAI IRYLRSVHGG AVAITAPTGI AGLNIGGQTI HSWAGIGLGK
EPCDQLKRRL SGFARRRWMD AQALIIDEVS MLDGRLFDKL EAIARYIRNT ERPFGGIQLI
LSGDFFQLPP VPDQDSTSRI EATFAFQAKT WRQCVDHMAI LTKVFRQKDN SGLPLPEHFA
VG
//
