ID A0A0F9YUZ3_9MICR Unreviewed; 952 AA.
AC A0A0F9YUZ3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA replication ATP-dependent helicase/nuclease {ECO:0000256|RuleBase:RU367041};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU367041};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367041};
GN ORFNames=AAJ76_5000119063 {ECO:0000313|EMBL:KKO76282.1};
OS Vairimorpha ceranae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC Vairimorpha.
OX NCBI_TaxID=40302 {ECO:0000313|EMBL:KKO76282.1, ECO:0000313|Proteomes:UP000034350};
RN [1] {ECO:0000313|EMBL:KKO76282.1, ECO:0000313|Proteomes:UP000034350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA08 1199 {ECO:0000313|EMBL:KKO76282.1,
RC ECO:0000313|Proteomes:UP000034350};
RX PubMed=25914091;
RA Pelin A., Selman M., Aris-Brosou S., Farinelli L., Corradi N.;
RT "Genome analyses suggest the presence of polyploidy and recent human-driven
RT expansions in eight global populations of the honeybee pathogen Nosema
RT ceranae.";
RL Environ. Microbiol. 0:0-0(2015).
CC -!- FUNCTION: Key enzyme involved in DNA replication and DNA repair.
CC Involved in Okazaki fragments processing by cleaving long flaps that
CC escape FEN1: flaps that are longer than 27 nucleotides are coated by
CC replication protein A complex (RPA), leading to recruit DNA2 which
CC cleaves the flap until it is too short to bind RPA and becomes a
CC substrate for FEN1. Also involved in 5'-end resection of DNA during
CC double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
CC {ECO:0000256|RuleBase:RU367041}.
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:RU367041};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367041}.
CC Chromosome {ECO:0000256|RuleBase:RU367041}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|RuleBase:RU367041}.
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:KKO76282.1}.
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DR EMBL; JPQZ01000005; KKO76282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9YUZ3; -.
DR VEuPathDB; MicrosporidiaDB:AAJ76_5000119063; -.
DR VEuPathDB; MicrosporidiaDB:G9O61_00g008360; -.
DR VEuPathDB; MicrosporidiaDB:NCER_100239; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000034350; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:InterPro.
DR GO; GO:0006259; P:DNA metabolic process; IEA:UniProt.
DR CDD; cd18041; DEXXQc_DNA2; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR022765; Dna2/Cas4_DUF83.
DR InterPro; IPR026851; Dna2/JHS1_DEXXQ-box.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR014808; DNA_replication_fac_Dna2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR047187; SF1_C_Upf1.
DR PANTHER; PTHR10887:SF433; DNA REPLICATION ATP-DEPENDENT HELICASE_NUCLEASE DNA2; 1.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR Pfam; PF01930; Cas_Cas4; 1.
DR Pfam; PF08696; Dna2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU367041};
KW ATP-binding {ECO:0000256|RuleBase:RU367041};
KW Chromosome {ECO:0000256|RuleBase:RU367041};
KW DNA damage {ECO:0000256|RuleBase:RU367041};
KW DNA repair {ECO:0000256|RuleBase:RU367041};
KW DNA replication {ECO:0000256|RuleBase:RU367041};
KW DNA-binding {ECO:0000256|RuleBase:RU367041};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU367041};
KW Hydrolase {ECO:0000256|RuleBase:RU367041};
KW Iron {ECO:0000256|RuleBase:RU367041};
KW Iron-sulfur {ECO:0000256|RuleBase:RU367041};
KW Metal-binding {ECO:0000256|RuleBase:RU367041};
KW Multifunctional enzyme {ECO:0000256|RuleBase:RU367041};
KW Nuclease {ECO:0000256|RuleBase:RU367041};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367041};
KW Nucleus {ECO:0000256|RuleBase:RU367041};
KW Reference proteome {ECO:0000313|Proteomes:UP000034350}.
FT DOMAIN 78..236
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 248..325
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 656..930
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01443"
SQ SEQUENCE 952 AA; 109950 MW; BD84399328A28715 CRC64;
MSEISNKKFK FEFKSSISFW SDTNKDNFEK DLQIAESELS FTSAEINSKT ESFKPSNIKF
IIRDIFKSED SITLYGDDVV CTVDGEWCSI DFEINTKITV MSCLCCDKDL QKIIKDSYIH
VYVNDEENYL FIEDDLLTIT NLVSSIRCIN NPYLNGKIAD IGFTFNDKCL VNGIILHEIM
EDCILNQNFK LSYITKSISA GIKKNLMNIY CCNTSEKVVR DDITSLIGNI ISFNKQNLVF
NECEKRIASL SMNLKGNVDA VGLENNIVLE IKSGKSMDIS HKAQVILYSL ILKEKYRTNF
QSYLFYITAN NFVNVDIKHS EVKSLMILRN KLAMHNSITN CSCCEYDPCR IIQKILNLSD
SHWLKKMWNA LEKEESFRLK ETWHLVKFKK QCNQIVVFAY DSKNIVVDDI YVNIYTEDLV
KLCKGIINEM DSIFLHVSLS EKINLEKNNN YYISFGNSDV FFKFMRYSLI YIAYFRYLQK
NKTGGFFLPD EDKGFFEEED SFEYFSSDEI ETSKVAMGDS VVEKNNNTIV KNNVNTANKT
RDCCLNKHSF DDTCTNKYDE IEKDLKKKYT ENLASSSLDS GIFSSLDRQI NHVIDDQKKL
SLETNSSSFA YFTPLPPEPK RYKYQIPEIY MSKFLRLNEN QKAALYSALN CENYKIVHGM
PGTGKSSVIV LLIKILVYLN KKVLLVCYTN LAITNILSRL KTIRSYRACK ENINFSSVQE
IKTYFRNVDL VASTCFGFRD PIFLERSFDY CIIDEGSQQH LLLTLIPISL CQKFVIFGDH
LQLKPLSKSC TDLNMSLFEY LLDVNHSELT IQYRMGPNIM RLSNELFYDG KLQLGRSIED
SVCFIDSSTI EYSKFIKDVY DTTILCYFNS QVKITKELTD CQVETVDRFQ GSEANNIIVV
FDPVVKCDVI ESKERLNVAL TRAKRSLILI GDLTKMKDIY IINRLLQILN IV
//
