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Database: UniProt
Entry: S7XKV0_SPRLO
LinkDB: S7XKV0_SPRLO
Original site: S7XKV0_SPRLO 
ID   S7XKV0_SPRLO            Unreviewed;       889 AA.
AC   S7XKV0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Type III restriction endonuclease {ECO:0000313|EMBL:EPR79669.1};
GN   ORFNames=SLOPH_2009 {ECO:0000313|EMBL:EPR79669.1};
OS   Spraguea lophii (strain 42_110) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Spraguidae;
OC   Spraguea.
OX   NCBI_TaxID=1358809 {ECO:0000313|EMBL:EPR79669.1, ECO:0000313|Proteomes:UP000014978};
RN   [1] {ECO:0000313|Proteomes:UP000014978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=42_110 {ECO:0000313|Proteomes:UP000014978};
RX   PubMed=23990793; DOI=10.1371/journal.pgen.1003676;
RA   Campbell S.E., Williams T.A., Yousuf A., Soanes D.M., Paszkiewicz K.H.,
RA   Williams B.A.P.;
RT   "The genome of Spraguea lophii and the basis of host-microsporidian
RT   interactions.";
RL   PLoS Genet. 9:E1003676-E1003676(2013).
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:EPR79669.1}.
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DR   EMBL; ATCN01000162; EPR79669.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7XKV0; -.
DR   STRING; 1358809.S7XKV0; -.
DR   VEuPathDB; MicrosporidiaDB:SLOPH_2009; -.
DR   HOGENOM; CLU_001666_4_2_1; -.
DR   InParanoid; S7XKV0; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000014978; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   InterPro; IPR018999; UPF1_CH/ZBD.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF525; HELICASE SENATAXIN-RELATED; 1.
DR   Pfam; PF13086; AAA_11; 2.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF09416; UPF1_Zn_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   4: Predicted;
KW   Endonuclease {ECO:0000313|EMBL:EPR79669.1};
KW   Hydrolase {ECO:0000313|EMBL:EPR79669.1};
KW   Nuclease {ECO:0000313|EMBL:EPR79669.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014978}.
FT   DOMAIN          409..573
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          355..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   889 AA;  102562 MW;  66D38623C6C7296D CRC64;
     MYCMKCPSQT NIKCLDCITE GDNTGKYYCN SISCTNTLSA SHILSHLIAC SHKQIMVNDV
     KVECVQCKNN NVFALTIQTG NDKRKKKQHS GSVKTESHAS INYNENFYLC TSCIKPTKFN
     TKKSHPIKYI VSNKQLLLFD TLVTRLRYNY GSYCRIYSEL IDREMEAEKK KKEDQKICAP
     SIRFNIKTDN ADHKKGKEHN RGNTSISNII FLKVNLDRYK VNIGDEVEIY KYSGKKKKSI
     CKGIIAGLNL AEEELKIKVQ HLDVLYEYYT KNPIDTLVEF NFKSVCYDRM KRSIKRINKN
     VDSDIQQIIY NGIKQNDIDY KDSYELIYEN NTEDSTKQTI IEKADDSSIS YKYESDSDSI
     GSLSENSKDD SENNAAESLS TLTLDNYIKN KIYLKKMNYK LNKSQIEAIS LVLRNKISII
     QGPPGSGKTL TCANIVYNLY KLILEERFEE SLQYSKGQNK SLKKKILIVS PSNVAVDNIV
     KELIKLNVKV LRVYSKNREN IENENDNISL HKLVEQKLDK EKKNNNHNNE MDRYLFYQKE
     IIKEYDVICS TCVTAGTKFF KDFNFPYVLI DEAVQAVEPL CIIPISYGVK KLILVGDHKQ
     LGPTILSHEA KNRGYNMSLF ERLIKIGVQP HILYTQYRMD PMISEFISNR FYNGCLISDN
     NYSNTIKEKM IEKSKNNNIK NKSKICISPI LTNLISLMPT FFYHTPGIEN KLSTTYYNIN
     EIDIILSLVK YLLSLNIQQS DIGIITMYDG QRSAITKIFN NNNLNTIDIF NIDGFQGREK
     NIIIISLVRA QNEHNEEDNI NTDNSKNLGF IGNNRRMNVA MSRGKDMLVL VGDCDRLNKS
     SSNWKKTLEY YHKHNLIVQG NINNLKKYRS KDLDSEIKFD LKNILKEIQ
//
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