ID A0A0G4FVT8_VITBC Unreviewed; 1038 AA.
AC A0A0G4FVT8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=R3H domain-containing protein {ECO:0000259|PROSITE:PS51061};
GN ORFNames=Vbra_16365 {ECO:0000313|EMBL:CEM19289.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM19289.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM19289.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-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}.
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DR EMBL; CDMY01000510; CEM19289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4FVT8; -.
DR STRING; 1169540.A0A0G4FVT8; -.
DR VEuPathDB; CryptoDB:Vbra_16365; -.
DR InParanoid; A0A0G4FVT8; -.
DR OMA; WSSQAMY; -.
DR OrthoDB; 170190at2759; -.
DR PhylomeDB; A0A0G4FVT8; -.
DR Proteomes; UP000041254; 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:InterPro.
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 Gene3D; 3.30.1370.50; R3H-like domain; 1.
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; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
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; PF01424; R3H; 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 SMART; SM00393; R3H; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; AN1-like Zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS51061; R3H; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000041254};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 767..833
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT REGION 190..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 348..375
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..859
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 113293 MW; 5BEEDFB1F646361D CRC64;
MTSTASAVSG SNLVESREAF VEKTSELLSL EHAAEVEETT ALLAECTPTE LEEAGIAILK
VEAADVTTGL YGRTVATFQK HSFQQPPPAL PSHRLSSGDI VGLFDSQHPL SSQPALTGVV
HRVKSTGISV VFDDDTDCDV QALVPPVHLA LWASDVTLRR YRAALNALTS YRDGPASALL
DVCFGTTPPR FNKRPSRPSA ERQDGPADDD CCDGSISTCD GTPFKVQLND SQRRAVVHAI
RAVDVACIHG PPGTGKTTTM VEVIRQLVVR NRRVLVCAPS NVAVDNLLER CISIGLKLVV
RLGHPSRIQA TLLPYCLDSL VRASEAAELC SDIRKEMDGH LRQLNRGKAG GREERRRLYG
ELKELRKELR QRERRAVSEV LGKSQVVFAT CTGADDFALR KFATSREDGG PRPFDVVCID
EAAQALEVGC WIPLLLGRKA ILAGDHKQLA PTIKSKEAQR SGLDVTLFQR LQRMWGDQVS
SLLDVQYRMS HVIMEWSSET FYDGKLKADQ SVEHHTIQDL IPHVDEDAVS PMVWIDAGGL
PYMREDDHTA TSGGRDRSSR SNRGEAEVVM RYATHLVVEQ GLDAGKINII TPYNRQVELL
RSMAAENESL SGIPIATVDS FQGREEEVVI ISLVRSNIHK AVGFLSDHRR LNVAVTRAKR
QLVIVGDSAT LEGDPILFSL YTFAQNNGLV RYACEFVNEE DIPQQAAAGP SAPPKRAAQT
SASQPSRSDR PPEARRRPVP PAQPPAGKAP EKPAAAVGPP EPRDEENGEV NAEEARLRRI
LEDVKRRKGE YSFPASLSSY QRRLVHELAE SLGLRHESKG EGDDRFICVM SRDRPSTPQP
SAAPAQPPTE PPAPATDGPP STASSPAAAE DAADEEVSHI PDVASGGPGP TAGSLSSRRR
QQRKNKKKTP ADERPTNADN KVSDEALDEM LAASSRQDWI CALPSCSQST KLIGTTCSYC
RRRFCISHAI AEAHGCGDEA SRQAKQSFRK EQTAESRGGG CVNESFGKND WRRREAQKSL
QAKIADAQAR RKAQHKKS
//
