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Database: UniProt
Entry: A0A015K0A3_RHIIW
LinkDB: A0A015K0A3_RHIIW
Original site: A0A015K0A3_RHIIW 
ID   A0A015K0A3_RHIIW        Unreviewed;       590 AA.
AC   A0A015K0A3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=SsDNA-dependent ATPase MGS1 {ECO:0000313|EMBL:EXX73060.1};
GN   ORFNames=RirG_063680 {ECO:0000313|EMBL:EXX73060.1};
OS   Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX73060.1, ECO:0000313|Proteomes:UP000022910};
RN   [1] {ECO:0000313|EMBL:EXX73060.1, ECO:0000313|Proteomes:UP000022910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA   Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA   Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA   Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA   Huang S.;
RT   "Single nucleus genome sequencing reveals high similarity among nuclei of
RT   an endomycorrhizal fungus.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008959}.
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:EXX73060.1}.
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DR   EMBL; JEMT01014880; EXX73060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A015K0A3; -.
DR   STRING; 1432141.A0A015K0A3; -.
DR   HOGENOM; CLU_017985_0_1_1; -.
DR   OMA; RIILSQC; -.
DR   Proteomes; UP000022910; Unassembled WGS sequence.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009378; F:four-way junction helicase activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18139; HLD_clamp_RarA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032423; AAA_assoc_2.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR021886; MgsA_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1.
DR   PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF16193; AAA_assoc_2; 1.
DR   Pfam; PF12002; MgsA_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022910}.
FT   DOMAIN          152..269
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          39..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  66418 MW;  9174BCD81719347D CRC64;
     MSSNNDDNDI MVCCPACNQY VDISEINEHM DNKCTKLEKT EVENQKSSKN TPPSKAPPKK
     IVITAKNDFF TAKSEASSNP SQKSQLPLSI KREKRPLISS SSSSRPSKQI KTKADTMPLA
     ARVRPSSFEE FIGQKEIVGN NGWLKELILR DKIPSMIMWG PSGVGKTTLA KIMAKLTKSI
     FKEYSGITHA TADIKKAFDV ARNEAALTGR RTIIFLDEIH RFNKAQQDLF LPYVESGGVT
     LIGATTENPS FKINSSLLSR CKVFTLNKLT IDEVQEILKR ALDKIRKQNI PNVQSEESST
     TLSENEDDIK VDEDALKYLA VMSDGDARIA LNALEIALNM KSKKHITKDD IEQVIQKSLL
     YDKDGEEHYN IISALHKSMR GSDANASLYW LGRMLTGGED PLYIARRLIV FASEDVGLAD
     NSALPLAIAT YQACQFIGMP ECEINLAHCV TYLAEAKKSV RSYKAYGLVK ETIKEEYNYP
     VPHHMRNAPT NLMKNLGYSA GYKYNPDFEG SVHQEYLPKE LKRKEFLDVF SPKKVDPETK
     YRESIKSEPG EQRIKTVPQM EQNVSTEIYE EIDFHYPFSG THSHDITDNQ
//
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