ID A0A0P1AL02_PLAHL Unreviewed; 986 AA.
AC A0A0P1AL02;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Dna-binding protein smubp-2 {ECO:0000313|EMBL:CEG41368.1};
OS Plasmopara halstedii (Downy mildew of sunflower).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Plasmopara.
OX NCBI_TaxID=4781 {ECO:0000313|EMBL:CEG41368.1, ECO:0000313|Proteomes:UP000054928};
RN [1] {ECO:0000313|Proteomes:UP000054928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma Rahul, Thines Marco;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCYD01000553; CEG41368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1AL02; -.
DR EnsemblProtists; CEG41368; CEG41368; CEG41368.
DR OMA; WSSQAMY; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000054928; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18044; DEXXQc_SMUBP2; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 2.40.30.270; -; 1.
DR Gene3D; 4.10.1110.10; AN1-like Zinc finger; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035896; AN1-like_Znf.
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; IPR004483; SMUBP-2/Hcs1-like.
DR InterPro; IPR048761; SMUBP-2_HCS1_1B.
DR InterPro; IPR000058; Znf_AN1.
DR NCBIfam; TIGR00376; IGHMBP2 family helicase; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF21138; SMUBP-2_HCS1_1B; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF118310; AN1-like Zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000313|EMBL:CEG41368.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054928};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 209..409
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 699..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..864
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 110614 MW; 0C17119DE0093364 CRC64;
MPKTTETSAD ALALLPVTLE TWLTSTRRLL SIEQQEEVDA MRKELTTLDD RDNPNVLTHL
TLARYSTGLF GRMILHLSLP SLHLRQAKPH HFTVGDLVQL RVQKSTSIPT GIVSRVEEHA
ISVAFNSEHD EIDELALSAT TLTLDRLVNT ATFAKLTDTL DQMTKLDFGT ANKVIDVVFS
NRDPSWNTLI PEFQPLHTQL NTSQHEAIRF ALASKDLVLI HGPPGTGKTT TVIELILQLI
DKYESKVLVC APSNIAVDNV LEKLASACSK LRKKLNLVRV GHPARVLPQT LKYCLDAKIA
NAEGTEIVQD IRKELTLMQN KLQKTREKTV KYELRREMKA NRKEIRVREQ NVVSEIIKQS
NVVFATNVGA ASKLLKDVTF DVVIIDEAAQ ALEASCWVPI LKAKRCVLAG DHLQLPPTIK
SKVAAAKGLE VTLFDRVTRN ERLKCVVKML DTQYRMHEDI CNWSSQAMYK GELKSFSAVA
KRKLHELPHV TIKKDDDVLN ATLLLVDTAG CELDEDEENA EDVKGVHLSK SNEGEARIVA
KHVQMLLSAG LKEDEVAVIT PYNKQVQTLK GLLLNSFPKL EIRSVDGFQG CEKEAVVMSL
VRSNASRQVG FLADDRRMNV AITRAKRHVA LICDTDTISS HRFLATIVHH FEQFGEVRSA
YEFLEDDTVQ GSVDDVMAMT GNFSKTLVVG VSEAKTKRKT KTSKSMKEQK IADDPSSTIV
DDRSESHIEE ETSKADTEEV MTVEAHSEEA MTADVHTEEA STVKMEIEGA RTVEVEPEEI
SPFEKAMTVE VKFEDERKSS VFQLMDSSSD SSDECDQDNN ETKMRPSDFE PSNILLKDLH
MSRLARHPAP LKSTKKSKKK KRQGKTNTSP IDKMKDDEDE LDYLTRQATK SSKCAYQSQS
RCQTSVSMLG SICKFCKLKF CYNHAMPEVH GCGDAVRTFE RMTFKHQMKE TPSKKLTNDK
RKILKKKLQE TVAAKSADRS TKPKKK
//
