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Database: UniProt
Entry: I3LWS4_ICTTR
LinkDB: I3LWS4_ICTTR
Original site: I3LWS4_ICTTR 
ID   I3LWS4_ICTTR            Unreviewed;       780 AA.
AC   I3LWS4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=ATP-dependent RNA helicase SUPV3L1, mitochondrial {ECO:0000256|ARBA:ARBA00021960};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   AltName: Full=Suppressor of var1 3-like protein 1 {ECO:0000256|ARBA:ARBA00031873};
GN   Name=SUPV3L1 {ECO:0000313|Ensembl:ENSSTOP00000000454.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000000454.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000000454.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC       {ECO:0000256|ARBA:ARBA00004436}.
CC   -!- SIMILARITY: Belongs to the helicase family.
CC       {ECO:0000256|ARBA:ARBA00008708}.
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DR   EMBL; AGTP01042546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01042547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3LWS4; -.
DR   STRING; 43179.ENSSTOP00000000454; -.
DR   Ensembl; ENSSTOT00000000503.3; ENSSTOP00000000454.3; ENSSTOG00000000503.3.
DR   eggNOG; KOG0953; Eukaryota.
DR   GeneTree; ENSGT00390000003100; -.
DR   HOGENOM; CLU_010647_3_2_1; -.
DR   InParanoid; I3LWS4; -.
DR   TreeFam; TF106432; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0045025; C:mitochondrial degradosome; IEA:Ensembl.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0034458; F:3'-5' RNA helicase activity; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:Ensembl.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0006310; P:DNA recombination; IEA:Ensembl.
DR   GO; GO:0035946; P:mitochondrial mRNA surveillance; IEA:Ensembl.
DR   GO; GO:0035945; P:mitochondrial ncRNA surveillance; IEA:Ensembl.
DR   GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IEA:Ensembl.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; IEA:Ensembl.
DR   CDD; cd17913; DEXQc_Suv3; 1.
DR   CDD; cd18805; SF2_C_suv3; 1.
DR   Gene3D; 1.10.1740.140; -; 1.
DR   Gene3D; 1.20.272.40; -; 1.
DR   Gene3D; 1.20.58.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00023271};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          352..520
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          698..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..780
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   780 AA;  87163 MW;  F8BFC65F4FCF4A81 CRC64;
     MSFPRCALLW ARLPAGRQAG HRAAVCSALR AHCGPSPAVL GRVPALAASS ASGGSKAPNT
     SLFVPLTVKP QGPSADGDVG AELTRPLDKN EVKKILDKFY KRKEIQKLGA DYGLDARLFH
     QAFISFRNYI MQSHSLDVDI HIVLNDICFS AAHVDDLFPF FLRHAKQIFP VLECKDDLRK
     ISDLRLPPNW YSEARAIRRK IIFHSGPTNS GKTYHAIQKY LSAKSGVYCG PLKLLAHEIF
     EKSNAAGVPC DLVTGEERVT VEADGKQAAH VACTVEMCSV TTPYEVAVID EIQMIRDPAR
     GWAWTRALLG LCAEEIHLCG ESAAIDLVTE LMYTTGEEVE VRNYKRLTPI SVLDHALESL
     DNLRPGDCVV CFSKNDIYSV SRQIEIRGLE SAVIYGSLPP GTKLAQAKKF NDPSDPCKIL
     VATDAIGMGL NLSIRRIIFY SLIKPSINEK GEKELEPITT SQALQIAGRA GRFSSQYKEG
     EVTTMNREDL GLLKEILNRP VDPIRAAGLH PTAEQIEMFA YHLPDTTLSN LIDIFVDFSQ
     VDGQYFVCNM DDFKFSAELI QHIPLSLRVR YVFCTAPINK KQPFVCSSLL QFARQYSRNE
     PLTFAWLRRY IKWPLQPPKN IKDLMDLEAV HDVLDLYLWL SYRFMDMFPD TSLVRDLQKE
     LDGVIQDGVH NITKLIKISE TRKLLYLESS LAESQSRLSG TLKSQARRAR GTKTAGSKAA
     EPLGASAGEL SLASRLVQQG LLTPDMLKQL EKEWMTQQTE HGQERTGTRR KKKEHNSDFL
//
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