ID Q8SRI7_ENCCU Unreviewed; 766 AA.
AC Q8SRI7;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 130.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN OrderedLocusNames=ECU07_1130 {ECO:0000313|EMBL:CAD25646.1};
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD25646.1, ECO:0000313|Proteomes:UP000000819};
RN [1] {ECO:0000313|EMBL:CAD25646.1, ECO:0000313|Proteomes:UP000000819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1 {ECO:0000313|EMBL:CAD25646.1,
RC ECO:0000313|Proteomes:UP000000819};
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
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:ARBA00001665,
CC 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; AL590447; CAD25646.1; -; Genomic_DNA.
DR RefSeq; NP_586042.1; NM_001041664.1.
DR AlphaFoldDB; Q8SRI7; -.
DR STRING; 284813.Q8SRI7; -.
DR GeneID; 859472; -.
DR KEGG; ecu:ECU07_1130; -.
DR VEuPathDB; MicrosporidiaDB:ECU07_1130; -.
DR HOGENOM; CLU_001103_15_0_1; -.
DR InParanoid; Q8SRI7; -.
DR OMA; ISKWGHE; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000000819; Chromosome VII.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
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; 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; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 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 Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 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:UP000000819}.
FT DOMAIN 246..421
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 450..590
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 729..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 86812 MW; CD5AC2C8A939E220 CRC64;
MKSRKYEMEK DEFFINAVLE DCEINDFSWE FSEITSNSDI RSSVRALDGF DSDSDVELIS
RMDVESPLCE KEGGDDTSSG SGLKRNLGKL ELGGVPGKSV LRRADACLDG EIGDRCLSLE
SRVMRGDVDY EYYSSLGEDL SDISIVSVEE AQGSGDGCGR SPGERRDAVV ERFPDSCSLN
NDCIRATFLK SSLEDKGDVD DSFPAHVLEE SSLSSSEDSE AKSIEEFYLR EVFKMKEFRT
NQREVIQACL SGKDVFVLMP TGGGKSICYQ LPALVYDGIT IVVSPLLSLV QDQIRNLLQK
GILALPINSN LSRAERDLVF QVLGGDELIC KIFYVTPELI AKSGHFHDVL SGLVCRGRLK
RFVIDEAHCV SQWGHDFRPD YKELGSMRAR YPSVPIIALT ATATQKVEMD ILENLGIRGC
ETFKMSFNRS NLRYEVRAKT STVELDIASF VQTHFPDCCG IIYCTSKKEC EMISEKLGKY
MGTAFYHAGL SKNERNSVQE KWNRGEFKVI VATIAFGMGI DKKDVRFVIH YCIPKSLEGY
YQETGRAGRD GLESVCVLFY TYGDKKKISF MIEKGDGGYE QKQRQREDLE AVIQFCENKT
DCRRMQVLAH FGERFDPQMC RKTCDNCRRE GVVKKDYTRE ARDLILLVYT SSRITLCQAV
DVYKGLSNKK SREYSGSEYY GKGKRLRKTT IERILRSLIS HGYIQERIEF MERRFSWSYL
VAKKTSVDRL ELAEEEDEGH RTPRDGKKRE GPKGGTSRKG MKKIKR
//
