ID A0A3M6VF82_9STRA Unreviewed; 886 AA.
AC A0A3M6VF82;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DD237_004195 {ECO:0000313|EMBL:RQM09770.1}, DD238_002662
GN {ECO:0000313|EMBL:RMX65364.1};
OS Peronospora effusa.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Peronospora.
OX NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX65364.1, ECO:0000313|Proteomes:UP000282087};
RN [1] {ECO:0000313|Proteomes:UP000282087, ECO:0000313|Proteomes:UP000286097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R13 {ECO:0000313|EMBL:RQM09770.1,
RC ECO:0000313|Proteomes:UP000286097}, and R14
RC {ECO:0000313|EMBL:RMX65364.1, ECO:0000313|Proteomes:UP000282087};
RA Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA Reyes Chin-Wo S., Mou B., Michelmore R.;
RT "Comparative genomics of downy mildews reveals potential adaptations to
RT biotrophy.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RMX65364.1}.
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DR EMBL; QLLG01000252; RMX65364.1; -; Genomic_DNA.
DR EMBL; QKXF01000669; RQM09770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M6VF82; -.
DR STRING; 542832.A0A3M6VF82; -.
DR VEuPathDB; FungiDB:DD237_004195; -.
DR Proteomes; UP000282087; Unassembled WGS sequence.
DR Proteomes; UP000286097; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000282087};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 216..400
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 617..657
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 718..872
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 886 AA; 99921 MW; 8927B3BADF8F850E CRC64;
MVSGIVRIAT MEHLQIGRLE RKMELLLHPL MKRGLVKLAG VCETPPVSSH MFASFYLTVF
IYVSVKAFDV FIEGDQNFSL SDQVYSLLQI VQGADSSSLD AIATRPTSEA KDPSLQVNPQ
DLDTLFSECV GASSLHNSVD GLNEDPSEHL TQYLHSIELR DHQKQALRWM LWREDQMKDD
VGEQESNDPM WEKRQFRSKS FYYVNPFEKS ASLTRPEPPA PCLGGILADD MGMGKTMMML
SLIAYQKHMG EERLTNDNIP TQAKREATGK TLVICPLSLL HQWKNEALER FLPNTLSVYV
YYGDDRGTCT KLTMAPFSKN DIVLTTYGVL SAEFGKNGPV ATTKWNRIIL DEAHSIKNRA
TGYFKTCSAL KATHRWCLTG TPIQNTLDDV FALLCFLEYQ PWCRVAWWKR VITKPYEDGD
DVNALGRLKV ILTPILLRRT KQSRDKLGNM IVHLPPKHVD LVKLEFSPDE RTFYQAVYDK
SRAEFNGFVA SGTAMTSYVA IFALLLRLRQ ACDHPLLALG KKFEHALKRD DKKAGVNTTA
QTRLAFQPQQ NESPEAYYQR IAAQLQTDMQ ASNCERLLDN GHDVSDDKEG NSTGGLTASY
IQNVIAQVED GLEAHECPIC LDPPRNAVLT PCAHILCVQC LRESLLNDPE NGCPVCRAVV
DMAKVFKLPP PSASMTKDES SFEMNTPAVA SVADDDDDGT GFESTKLQQL LRDLNAIRLE
NKNVESPEQK RKVVVFSQWT SMLDMVSLLL SRHGFSHCTF NGGLNQEARE RVLTKFAKDP
HIEVLVISLK AGGVGLNLTC ASVVILLDPW WNPGVEEQAI DRVHRLGQTQ DVIVKRYVVM
DTVEDMILQL QERKEQLAKH VLVIAKTHDE RRSERLHLDD LRRFFR
//
