ID   A0A397JPU8_9GLOM        Unreviewed;      1456 AA.
AC   A0A397JPU8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=Glove_13g219 {ECO:0000313|EMBL:RHZ89657.1};
OS   Diversispora epigaea.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX   NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ89657.1, ECO:0000313|Proteomes:UP000266861};
RN   [1] {ECO:0000313|EMBL:RHZ89657.1, ECO:0000313|Proteomes:UP000266861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT104 {ECO:0000313|EMBL:RHZ89657.1,
RC   ECO:0000313|Proteomes:UP000266861};
RA   Sun X., Fei Z., Harrison M.;
RT   "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT   epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL   Submitted (AUG-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RHZ89657.1}.
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DR   EMBL; PQFF01000011; RHZ89657.1; -; Genomic_DNA.
DR   STRING; 1348612.A0A397JPU8; -.
DR   Proteomes; UP000266861; 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; IPR046700; DUF6570.
DR   InterPro; IPR025476; Helitron_helicase-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR   Pfam; PF20209; DUF6570; 1.
DR   Pfam; PF14214; Helitron_like_N; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000266861}.
FT   DOMAIN          222..354
FT                   /note="DUF6570"
FT                   /evidence="ECO:0000259|Pfam:PF20209"
FT   DOMAIN          513..724
FT                   /note="Helitron helicase-like"
FT                   /evidence="ECO:0000259|Pfam:PF14214"
FT   REGION          385..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..416
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1456 AA;  167878 MW;  C3DF4B8CC3C67E86 CRC64;
     MDVFNFIDVA YADFGDNRYL NMDDIILDDY KSKRKRQKAV RRADVGYRQH ERERQRKRRE
     IQRAKKREIC VEEDIRAIDA RVPLRVLEMN DEYDLLEEQY ADWPRPISKA VANNALAEFR
     ESVGYDSLRE LPCAVCSGLC LNEHSTTVSV REINLLLLEA SKYYENPFFE IDFVYGHPYI
     CESGCKILLD KDRFIERGTD GKNEDPFDLR ICNGCKRSLD AGNTPIFSLA NMWIGTTPRC
     LQGLTIPEQL LIFTGYMCIN LIQITNRKHT HHKIKGHVIT FTQEPTSLST ILPLPLYRLC
     DRIKVIFVGE ERPSEKQLKK MLCVRKNKIV TALGWLMDHN VLYKNVKLDK TALDSLPVNG
     VPTALLATTV MVNVEPEKVE HYTGYVTDPI DGNEMNNNLD DVDEEELSDE ESTSELCDST
     DNSAELRNSG MTYADGVPIS EQERTLKLLE KLIQESTVEQ ISSHAILMPH LKIPKNEYVD
     PSLLPAAFPI LFPYGVGGHE DNFRKYRIPF NQYIRHLLQL REPKFRHYRS FIFATFDILR
     RREIASETYL TAKQTNFERS ANLISKLTLN DVKIAIEQKR NDQPITNGAI LELTKNVNVV
     SKKIMGSPYS RNFLRNEIRA VIIRDGSPLL FVTINPADLH SSINRFCINL KKSKYLKNLK
     SILGTCIIVM MYAGKEIDVN TLLPEDFPTV TERARLAHLD PTAVAKYFNI VIEKIIKFIL
     GYKKPGVVYW GAPDPIELQN RLKFDDFRER LMLYVNDIVK EDVSYLFPNG DYLTDEMLDA
     EYKAPKTNLE KKIHPSILPI PDPRSPSFDE EFRFDVLRIA KRTLFHRCTK SCKKYRRGRT
     SDCCFDFPRE LVEAPGKIYP ELGIIALQRR NAYINNHNPY ITASCRGNND IRFIATVKLA
     LVYIHYITDY ITKSDMNTHN SFLICAMTLN NFVTEVPSSD ESSNDFMLRS RKLVTMCLNK
     IVGQTEMTGP QISAYLLGFK DHYTPNIFVL IYLNSFETYL TSRYPIRNSP ELMFSENSDT
     SSDEDELDLE NSSECDQTND EIIIHPQHLT HIQIHWSRES DKIPVLCGKG VPPKNDLKNI
     ERYGLCILLL FKPWTNADDL MGKYNSWHEA CNTFLQNPNL STRLRSIINN IELLHRCAEE
     TVLDRRLRQV ARENPEIANI RRIERSVMEY DDTGDAEILI DQYDFDVDNS ISLNPYEIMR
     TGLRDAKFVD DAMLHLYLKD KFNNKKIVQQ NFREEADVSN NDKQKNYVRP SCEDDNRLVK
     TWQKIIASKK GIEQVNKNTD SEKNHVSQPT SHLTLQSMFR KFSSDLNDEQ KKAFSLVCNH
     REQNYPGNPN KPPQLLMYLG GAGGTGKSKV IKAITEYFNQ IGQKQTLVLC APTGVAASNI
     GGCTLHSLCG FKFDNDDNSY KYNFPQGILK KTLQERWKNI EYLILDEVSM VGQKLMTKLH
     ACIKEAKHFQ NDEIXR
//