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
//