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Database: UniProt
Entry: A0A0V1MUW9_9BILA
LinkDB: A0A0V1MUW9_9BILA
Original site: A0A0V1MUW9_9BILA 
ID   A0A0V1MUW9_9BILA        Unreviewed;       753 AA.
AC   A0A0V1MUW9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=Supv3l1 {ECO:0000313|EMBL:KRZ75363.1};
GN   ORFNames=T10_10501 {ECO:0000313|EMBL:KRZ75363.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ75363.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ75363.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ75363.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the helicase family.
CC       {ECO:0000256|ARBA:ARBA00008708}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ75363.1}.
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DR   EMBL; JYDO01000039; KRZ75363.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1MUW9; -.
DR   STRING; 268474.A0A0V1MUW9; -.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KRZ75363.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          297..487
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   753 AA;  84059 MW;  C0611907A569A8FA CRC64;
     MASVKAVVTG LRNIGRLPQL RHLSGSKKSF EDLVVPLTVK SASTVNDVDV GVEFGGILAK
     DALASVLSKF ARRPAVRKLG AEHGLTGKFL LQALASFRRY CQESAVLPVD LHIMLADILQ
     NSRHVDDLFP LFLRHARQVF PHLECIEELK NISDLRLPQN WYPEARSIQR RVIFHAGPTN
     SGKTYQALQR YLAAKSGVYC GPLKLLASEV FHKSNAAGVP CDLITGEERC LANGQTCSEH
     ISCTVEMLDT RIHYEVAVID EIQMMRDLQR GWAWTRALLG VCADEIHVCG ELAAVDLVKE
     LLVSVGDDFE LHTYERKTPL KILDSPLGSL DSIQPYDCIV AFNRNDLFKV TRQVEASGRS
     VAMIYGSLPP GTKLAQARKF NDPDDPCDVL VATDAIGMGL NLSIRRVIFY SLVKVTLNES
     GEKELEPIST SQALQIAGRA GRFGTFHESG EVTTLRMEDL PALKAILTKP TEPIHAAGLF
     PTLEQIEMFA YYLPKATLSN LLDIFVSLSA VDENRFFMCN VDDLKFLADM IEHVPLTLKV
     RYVFCMAPIS RKKPFVCGMF LRYARKFSRG EPLTSDWLAR TIGWPFSAPT KIVDLVHLED
     VFDVLDTYLW LGYRFTDMFP ETEQVRAMQK ELDVLIRESL QNVKQLLKTV QVAGLFEQQG
     LNFDSRNPTT ATNAAAAVTK DSSTKMKQAT TTTTVRKGGV IQSLIKQGLL TPGMVEQIRK
     EIQTDQEEFV KKQNNPKNIK KNLGLLCKHD LSE
//
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