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Database: UniProt
Entry: G1PL21_MYOLU
LinkDB: G1PL21_MYOLU
Original site: G1PL21_MYOLU 
ID   G1PL21_MYOLU            Unreviewed;       787 AA.
AC   G1PL21;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
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:ENSMLUP00000011532.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000011532.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000011532.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000011532.2}
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; AAPE02056546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02056547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006107356.1; XM_006107294.2.
DR   RefSeq; XP_014304754.1; XM_014449268.1.
DR   RefSeq; XP_014304755.1; XM_014449269.1.
DR   AlphaFoldDB; G1PL21; -.
DR   STRING; 59463.ENSMLUP00000011532; -.
DR   Ensembl; ENSMLUT00000012673.2; ENSMLUP00000011532.2; ENSMLUG00000012664.2.
DR   GeneID; 102426686; -.
DR   KEGG; mlf:102426686; -.
DR   CTD; 6832; -.
DR   eggNOG; KOG0953; Eukaryota.
DR   GeneTree; ENSGT00390000003100; -.
DR   HOGENOM; CLU_010647_3_2_1; -.
DR   InParanoid; G1PL21; -.
DR   OMA; QPANWYT; -.
DR   OrthoDB; 161833at2759; -.
DR   TreeFam; TF106432; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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:UP000001074};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          354..522
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          37..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   787 AA;  87852 MW;  F7C46F2682D79A04 CRC64;
     MSFPRCALLW ARLPAGRRAG HRAAVCSALR AHGGPVPGPL GRTPAVASAS SSASGGSKAP
     NTSLFVPLTV KPQGPSADGD VGAELTRPLD KNEVKKILDQ FYKRKEIQKL GADYGLDARL
     FHQAFISFRN YILQSHSLDV DIHIILNDIC FSAAHVDDLF PFFLRHAKQI FPVLECKDDL
     RKISDLRIPP NWYPEARAIQ RKIVFHSGPT NSGKTYHAIQ KYLSAKSGVY CGPLKLLAHE
     IFEKSNAEGV PCDLVTGEER VSVEPNGKQA AHVACTVEMC SVTTPYEVAV IDEIQMIKDP
     ARGWAWTRAL LGLCAEEVHL CGEAAAIDLV TELLYTTGEE VEVRNYTRLT PISVLDHALE
     SLDNLRPGDC IVCFSKNDIY SVSRQIEIRG LESAVIYGSL PPGTKLAQAK KFNDPDDPCK
     ILVATDAIGM GLNLSIRRII FYSLIKPSIN EKGEKELEPI TTSQALQIAG RAGRFSSKYK
     EGEVTTMNRE DLRLLKEILN KPVDPIKAAG LHPTAEQIEM FAYHLPDTTL SNLIDIFVDF
     SQVDGQYFVC NLDDFKFSAE LIQHIPLSLR VRYVFCTAPI NKKQPFVCSS LLQFARQYSR
     NEPLTFAWLR RYIKWPLHPP NNIKDLMDLE AVHDVLDLYL WLSYRFIDMF PDASLVRDLQ
     KELDGIIQEG VHNITKLIKI SEAQRLLNLE NVSADSRSRL PGTLKSQARR MRGTKTLGYK
     AVEPPSPSAE EKSLASRLVQ QGLLTADMLK QLEKEWLTQR TEHGKDRTAP GTSSKGSRRK
     KKEPDSD
//
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