SUV3_CAEBR
ID SUV3_CAEBR Reviewed; 721 AA.
AC Q61SU7; A8X130;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=ATP-dependent RNA helicase SUV3 homolog, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN ORFNames=CBG06022;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: ATPase and DNA/RNA helicase able to unwind DNA/DNA, DNA/RNA
CC and RNA/RNA duplexes in the 5'-3' direction. {ECO:0000250}.
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=3.6.4.13;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; HE600909; CAP26340.3; -; Genomic_DNA.
DR AlphaFoldDB; Q61SU7; -.
DR SMR; Q61SU7; -.
DR STRING; 6238.CBG06022; -.
DR EnsemblMetazoa; CBG06022.1; CBG06022.1; WBGene00028368.
DR WormBase; CBG06022; CBP37585; WBGene00028368; -.
DR eggNOG; KOG0953; Eukaryota.
DR HOGENOM; CLU_010647_3_2_1; -.
DR InParanoid; Q61SU7; -.
DR OMA; AKTVFPH; -.
DR OrthoDB; 1106167at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0045025; C:mitochondrial degradosome; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR CDD; cd17913; DEXQc_Suv3; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022192; SUV3_C.
DR InterPro; IPR041082; Suv3_C_1.
DR InterPro; IPR044774; Suv3_DEXQc.
DR InterPro; IPR041453; Suv3_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12513; SUV3_C; 1.
DR Pfam; PF18147; Suv3_C_1; 1.
DR Pfam; PF18114; Suv3_N; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Helicase; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Nucleus; Reference proteome; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..721
FT /note="ATP-dependent RNA helicase SUV3 homolog,
FT mitochondrial"
FT /id="PRO_0000310550"
FT DOMAIN 181..319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 343..499
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 655..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 692..720
FT /evidence="ECO:0000255"
FT COMPBIAS 662..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 721 AA; 81220 MW; BDE8424DD7A1ADA4 CRC64;
MQRATGVLRI LGSFSQRCSP SSSATPSRFQ TMNSRRKRNS IRKAAAIEDL VEPRKVKHVT
QAAAGMEEWI GSLNNAAIHM ALDEFMRRPM VRQLAKENGI NDKLFIRAFK SFREYCTPED
LSSVDPGLLI LMSDISKGGK DCEMLYPFFL DHSKQVFPHL EAMDDLRIIS DLTRPHNWYP
EARSIIRKIF FHAGPTNSGK TYHALKRFGE AKSAVFCGPL KLLATEVFNR TNALGIPCDL
VTGEERRFAK DNHHPSQHLS STVEMLSTQM RVEVVVIDEI QMLRDEQRGW AWTRALLGAA
ADEIHLCGEP AAINIVKKLL EPIGETVEVR YYDRKSPLTI ADRAIESYSN IEPGDCIVCF
SKRAVFFNSK KLEENGIKPA VIYGDLPPGT KLAQAAKFND PDDECNVLVA TDAIGMGLNL
NIRRVIFNSC TRQTELLPTY AALQIAGRAG RFGTAYANGV ATTMRKEDLG TLKTILAEKV
EPITNVGIAP TYDQIETFSF HLPQASFVRL LDLFVSVCSV SDHFFICTVY DMRELAVLID
QVPLPLKVRY TFCTSPLNTD DKRTAAVFVK MARRFATGQA LTYEWLMDML EWPPKPASTL
SELSLLEQNY EVLDQYMWLS MRFPDMLPDE PRVRDASKIL DKMIQDGVEG FMSLLAVGPG
DNSDSREKRL SRPSEEKLAK SASEKPTRKS SILEALLKRT DISEEDLDQL REELNKKKKK
P
