SUV3_CHICK
ID SUV3_CHICK Reviewed; 794 AA.
AC Q5ZJT0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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; ORFNames=RCJMB04_16a1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
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; AJ720354; CAG32013.1; -; mRNA.
DR RefSeq; NP_001006498.1; NM_001006498.1.
DR AlphaFoldDB; Q5ZJT0; -.
DR SMR; Q5ZJT0; -.
DR STRING; 9031.ENSGALP00000039978; -.
DR PaxDb; Q5ZJT0; -.
DR GeneID; 423697; -.
DR KEGG; gga:423697; -.
DR CTD; 6832; -.
DR VEuPathDB; HostDB:geneid_423697; -.
DR eggNOG; KOG0953; Eukaryota.
DR InParanoid; Q5ZJT0; -.
DR OrthoDB; 1106167at2759; -.
DR PhylomeDB; Q5ZJT0; -.
DR PRO; PR:Q5ZJT0; -.
DR Proteomes; UP000000539; 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: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..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..794
FT /note="ATP-dependent RNA helicase SUPV3L1, mitochondrial"
FT /id="PRO_0000310548"
FT DOMAIN 182..322
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 341..506
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 678..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 794 AA; 88776 MW; 82A3B5B582B91480 CRC64;
MRRCAWPLLR LSSRVGLALR HGGAVRLRQA AASSSSSSSG GGGLRAPDTS LFVPVPLKPV
EGAAEEDVGA ELTRPLDKGE VLKNLNKFYK RKEIQRLGTE NGLDARLFHQ AFISFRKYIM
ESSSVSADLH IILNDICCGA GHVDDLFPFF LRHAKQIFPM LDCMDDLRKI SDLRLPPNWY
PEARAIQRKI IFHAGPTNSG KTYHAIQRFL SAKSGIYCGP LKLLAHEIFQ KSNAANVPCD
LVTGEERVYA SEDAKQASHI ACTIEMCSTN TPYEVAVIDE IQMIRDPARG WAWTRALLGL
CAEEIHVCGE GAAIDLVTEL MYTTGEEVEV RNYKRLTPLT VLDYALESLD NLQPGDCIVC
FSKNDIYSVS RQIEARGLEC AVIYGSLPPG TKLEQAKKFN DPNDPCKILV ATDAIGMGLN
LCIKRIIFNS IVKPTVNEKG EKEIDSITTS QALQIAGRAG RFGSSFKQGE VTAMHRDDLL
QLKEILSEAV PPVKAAGLHP TPEQIEMFAY HLPDATLSNL IDIFVSLSQV DGLYFVCNID
DFKFLADMIQ HIPLNLRSRY VFCTAPLNRK EPFVCTTLLK FARQFSRNEP LTFDWLCRHT
KWPLAPPKNI KELVHLEAVH DVFDLYLWLS YRFMDMFPDA ALVRDIQKKL DDIIQIGVCN
ITKLIRASQS GAAPGAAEVM SEGFPLSRTK RDARTVSDHR DAKSAEPLSI ALEVPGERRA
KSLRTYRSAT RQEDLKSHGR GSLANRLLRE GLLTQEMLRQ LESEWQDQHR SGRYGLASKR
NDQSSSKEMG KKKK
