SUV3_DANRE
ID SUV3_DANRE Reviewed; 763 AA.
AC A4IG62;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=ATP-dependent RNA helicase SUPV3L1, mitochondrial;
DE EC=3.6.4.13;
DE AltName: Full=Suppressor of var1 3-like protein 1;
DE Short=SUV3-like protein 1;
DE Flags: Precursor;
GN Name=supv3l1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Major helicase player in mitochondrial RNA metabolism.
CC Component of the mitochondrial degradosome (mtEXO) complex, that
CC degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality
CC in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate
CC helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA
CC heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA
CC surveillance system in mitochondria; regulates the stability of mature
CC mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation
CC of non coding processing intermediates. Also implicated in
CC recombination and chromatin maintenance pathways. May protect cells
CC from apoptosis. Associates with mitochondrial DNA (By similarity).
CC {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: Nucleus {ECO:0000250}. Mitochondrion matrix
CC {ECO:0000250}. Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; BC134945; AAI34946.1; -; mRNA.
DR RefSeq; NP_001077033.1; NM_001083564.1.
DR AlphaFoldDB; A4IG62; -.
DR SMR; A4IG62; -.
DR STRING; 7955.ENSDARP00000099447; -.
DR PaxDb; A4IG62; -.
DR PeptideAtlas; A4IG62; -.
DR PRIDE; A4IG62; -.
DR Ensembl; ENSDART00000189730; ENSDARP00000147822; ENSDARG00000111098.
DR GeneID; 570852; -.
DR KEGG; dre:570852; -.
DR CTD; 6832; -.
DR ZFIN; ZDB-GENE-030131-2838; supv3l1.
DR eggNOG; KOG0953; Eukaryota.
DR InParanoid; A4IG62; -.
DR OrthoDB; 1106167at2759; -.
DR PRO; PR:A4IG62; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0045025; C:mitochondrial degradosome; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; ISS:UniProtKB.
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:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
DR GO; GO:0001889; P:liver development; IMP:ZFIN.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0035946; P:mitochondrial mRNA surveillance; ISS:UniProtKB.
DR GO; GO:0035945; P:mitochondrial ncRNA surveillance; ISS:UniProtKB.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:2000827; P:mitochondrial RNA surveillance; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
DR CDD; cd17913; DEXQc_Suv3; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Mitochondrion nucleoid;
KW Nucleotide-binding; Nucleus; Reference proteome; Transit peptide.
FT TRANSIT 1..65
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 66..763
FT /note="ATP-dependent RNA helicase SUPV3L1, mitochondrial"
FT /id="PRO_0000310549"
FT DOMAIN 192..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 354..519
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 39..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 763 AA; 86255 MW; A430A5753A264809 CRC64;
MSVNRCIYLL SRSHIRYRVC ASTNLSTVST LSTTQHSTRR TFDKLSTRHS SSGSSRPLDT
SLFIPLPVKT DEDAEGSVGA ELTKPLDKNE LLKVLNRFYK RKEMQKLASD QGLDARLFHQ
AFVSFRKYVL EMNSLNADLH IILNDICCGA GHIDDIFPYF MRHAKQIFPM LDCIDDLRKI
SDLRVPANWY PEARAIQRKI VFHAGPTNSG KTYHAIKRYL EAKSGVYCGP LKLLAHEIYE
KSNAAGVPCD LVTGEERIFV DPEGKPSGHI ASTIEMCSVT TPYEVAVIDE IQMIKDPARG
WAWTRALLGL CAEEIHVCGE AAAVDFITEL MFTTGEEVEV HNYKRLTPFS ISNHAVESLD
NLKPGDCIVC FSKNDIYSIS RQIEIRGLEC AVIYGSLPPG TKLAQAKKFN DPDDPCKILV
ATDAIGMGLN LSIRRIIFNS LVKHSLNEKG EKEVDTISTS QALQIAGRAG RFSSVFKEGE
VTTMHRDDLP VLKEILGKPV DPIATAGLHP TAEQIEMFAY HLPQATLSNL IDIFVSLSQV
DGLYFVCNID DFKFLADMIQ HIPLNLRSRY VFCTAPINKK QPFVCTSFLK FARQFSRDEP
LTFNWVCRQV NWPLSPPKNI KDLVHLEAVH DVLDLYLWLS YRFMDMFPDS NQIREIQKEL
DENIQIGVRN ITRLIRAIDS QPTDTESNSS STVPESETSQ RKGRVLRSQN QRKELPRKSS
LSSRLLRDGL LTKELLSQLQ KEWAREQNED NSIPVNNGKR KKK
