ID A0A0C3ALS3_9AGAM Unreviewed; 975 AA.
AC A0A0C3ALS3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
DE Flags: Fragment;
GN ORFNames=SCLCIDRAFT_44971 {ECO:0000313|EMBL:KIM65902.1};
OS Scleroderma citrinum Foug A.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Sclerodermataceae;
OC Scleroderma.
OX NCBI_TaxID=1036808 {ECO:0000313|EMBL:KIM65902.1, ECO:0000313|Proteomes:UP000053989};
RN [1] {ECO:0000313|EMBL:KIM65902.1, ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|EMBL:KIM65902.1,
RC ECO:0000313|Proteomes:UP000053989};
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 (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|Proteomes:UP000053989};
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; KN822020; KIM65902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3ALS3; -.
DR STRING; 1036808.A0A0C3ALS3; -.
DR HOGENOM; CLU_001324_0_3_1; -.
DR InParanoid; A0A0C3ALS3; -.
DR OrthoDB; 1386573at2759; -.
DR Proteomes; UP000053989; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR025476; Helitron_helicase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45786; DNA BINDING PROTEIN-LIKE; 1.
DR PANTHER; PTHR45786:SF79; HOOK MOTIF PROTEIN, PUTATIVE-RELATED; 1.
DR Pfam; PF14214; Helitron_like_N; 1.
DR Pfam; PF05970; PIF1; 1.
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:UP000053989}.
FT DOMAIN 273..446
FT /note="Helitron helicase-like"
FT /evidence="ECO:0000259|Pfam:PF14214"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIM65902.1"
FT NON_TER 975
FT /evidence="ECO:0000313|EMBL:KIM65902.1"
SQ SEQUENCE 975 AA; 110663 MW; 3D9A13C62F93A8BA CRC64;
WLIGPIRNPT LKWGDYHRGR RHTCRTCNIE LLTGEKSGFC CGPNGSRYHN VPSLPPLPDE
IQAITTHPDI SRLSRMLNLI FSFASLETTH PFPSISGLPG FLAIQGRVYH RIRPTHVNSA
IRWLLFDGFT QNIPYADRAA YLPSTWIPAV QQALLRVNPF VAGLQHLSSL SAITCPDAHL
LLIDSGQEIA ALIALNNTAR TETRPRQLVV SRADGYTQKI PTVSRLWEPL AYPLLFPHGT
PGWGLIDRHI DSTDLENLVG NDGPDEPPTT QMWHYRARLL REPRFKIFGR LANEYAVDMF
SRDLECRLNY IQQNQTRLRM QDFELMAHDG DMPSSANIYL PSSFLGSKRW IANQIADSLT
IAATLGNPTF FVTMTCNTQW PEVQSQLLPG QNFTDIPVVV ARVFKQKLTL LLRTIKNMFV
NAGRQIYSVH CVEFQKRGLP HAHIIVKFAA SCKTPDEIDC IVSAEIPSNP SDVELVQRFM
LHQHPAPNRP PSKYCQRELS DGSRKCRFGY PRPLQPTTTI NGEGRIQYRR RHPGDEWVVP
HCLPLLRKFK CHINFEVAST SHLFQYLFKY IHKAPDSTRY RITENDNESI NEIEEYWDAR
YLSAGEAVWR ILGFHVTKKE PSVTSLPVHL PDLHSHHQYH RSTGLASTVS LLDRYFIRPS
GTFTNNDGSL VNFDDITYIE YFSTFRLGKL DTMCNAPSFH ERNVVVNSPS MLVIQRNESR
LHLCRLQTIR PSQGEIFYLR TILQHRSALS FEDARTVSSH LHPTFQEAAN AMGLFANQNE
AELAIQEGIL TLRTPRQLRI LFVHLLVNDC IVTPLALWNT YNIAMAVDHT LRCGNNNDIG
TSQALHEIAT LLEEFGRTPS DYGLPEATEH STEILHEIIR WGPQYESLSI RANTARQSMT
LEQQNIFDQV VHASLNYEPF LAFIDGKAGR GKTFLVNAIC DKLRSVGRIV LPTATAAFAA
QLYSGGRTTH SMFKV
//
