ID   A0A2H9TNS8_9FUNG        Unreviewed;      1594 AA.
AC   A0A2H9TNS8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|SMART:SM00487};
GN   ORFNames=PSACC_00811 {ECO:0000313|EMBL:PJF19418.1};
OS   Paramicrosporidium saccamoebae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC   Cryptomycota incertae sedis; Paramicrosporidium.
OX   NCBI_TaxID=1246581 {ECO:0000313|EMBL:PJF19418.1, ECO:0000313|Proteomes:UP000240830};
RN   [1] {ECO:0000313|EMBL:PJF19418.1, ECO:0000313|Proteomes:UP000240830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSL3 {ECO:0000313|EMBL:PJF19418.1,
RC   ECO:0000313|Proteomes:UP000240830};
RA   Quandt C.A., Beaudet D., Corsaro D., Michel R., Corradi N., James T.;
RT   "The genome of Paramicrosporidium saccamoebae is the missing link in
RT   understanding Cryptomycota and Microsporidia evolution.";
RL   Submitted (OCT-2016) 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|ARBA:ARBA00000600};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00000600};
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:PJF19418.1}.
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DR   EMBL; MTSL01000065; PJF19418.1; -; Genomic_DNA.
DR   STRING; 1246581.A0A2H9TNS8; -.
DR   Proteomes; UP000240830; Unassembled WGS sequence.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   CDD; cd18042; DEXXQc_SETX; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR024481; Helicase_Sen1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF525; HELICASE SENATAXIN-RELATED; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 2.
DR   Pfam; PF12726; SEN1_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240830}.
FT   DOMAIN          1094..1365
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
FT   COILED          1220..1247
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1594 AA;  178193 MW;  60C207AE904FEDDA CRC64;
     MREPAEKDVA DIMDLIAQKY RNPSDLQIDR EIFMRGIKLL KESPCIWCRH TRLAGELLRL
     LSFPQNECQS WFCERTIESL QSCSDCMEKY YAARPELKAA FSKLYETHTL EAFWEKVSEF
     DAARIGSALG AFLEERIDAK TPALLYALYE LLLFPDHLQI AVLHEDFSQV LTALVTSKRM
     IRINRVLPGV IACLFDTNQS VRQWASSVLK DSKIERPDNF PAGSIDVGKL VEDLDSSNPD
     NFASLILVSR WGPTNLPQSS VCSLLRQLLK SLGNPARCTT TVDAINFVLE SHTDLPEPIW
     SLLVDSICKS AYLKDILLGS ESHAGVKLIW IHALRQWSIF HSNVQLLIAI GDSIIPIVTL
     IHSQSSLQCL FKLLADMIRD DILPLLLPRY EQQLYRLLSA CMHQAKVLNM LDPHVTSTMA
     EICWNLDSYL WQSEGSTEFR GFARMLADLM KMETHSGIVI RESLRLLIRS KVDCAAFAVK
     RQFLIAIICD RLPLDAFTED AATTVILMVL HYSGRSVSQV QKLLKSYPQY FIDGFMRLQR
     NGIPKSLSFE VTRLFLDSFL AVFFVDDSGA TIVDLFPESN ALLNSVLQLS VRVSLIVASD
     GSNGSVDRTM GQNLERLLDF IVRIRKSIKP QNRKLALKST SLNGEEFTRL ATTHFNYAGS
     DTKIDSSRAS RIISVLIDFA RCCSIRISPT VVGLLGLLLT TVKFGSEDRS RLNNYIDSYE
     MATSIILPRP PADPAKAELS GKRPPLFTDE DVEKHALSEF NSAQDRRRER ALPVALRSNV
     IPIALKPMTK IGQLRADAIR DAPPVPKRRG ISGPINKPQK IEYIRSSTSE SDPDEDYGGL
     GFSKTPAVPL DIPIANRSVK LIDLAEGSNN KKGTSKSDSM GHVTETNLIR QFHRTILHFN
     LGDIESLPDD ATICNVPGTF ADAAHYTSIF EPLLFIECRA QLARSREESV NNETLSLRIA
     GVAHVDDFHE VVLQDDRDRD DDRVWMCDQD YLIVFFDNPR ETQTAIIVQS GTKGGVLEIV
     IRLSIPNEKA AVQIELREGL KLKFQKIGNV ITSLREYTAM HMVGHLTLAP AIFSPKLASV
     KAIGVSTELG GISKALDINM SQARAISAVV QNVNPITLIQ GPPGTGKTKT IEALLGVLLG
     RVGVDNKTKV MICAPSNAAI DEIVRRIRHG LVSGAGHRFK TKILRIGSLD MISDQVKDLT
     LDSQVDALLA ASTANSIKLL ETQRRSCDEL KNSLHNAEQA RREDQIKSLK TLLWEARENV
     RKNTKFLDDT RSNLRKKILG DAQIVCCTLS SSGHDILSRI DFDYLIIDEA CQAVELSCLV
     PLQHNCRQCI LVGGIRKLLL IILDPNQLPP TVISQMAGVF SYEQSLFVRL QKQCPESVLL
     LDTQYRMHPE ISRFPNSYFY QGHLVDGPSM ESVNKRPWHS TRLLGPFRLF DVSGSEGTWK
     RQSGVESRSK MNAAEARIAA DLISMICHSA PNIEDGFQGQ EREVIIFSCV RTGENKGIGF
     LNDTRRLNVA LTRAKCSLFV LGKVSTLIQN PIWKAMVDDS KARDCFVPYN SRTWDDAARA
     RRPMNLYARK FDNSRPAELP VVKAPTVIQI APDE
//