ID A0A0V0U360_9BILA Unreviewed; 1538 AA.
AC A0A0V0U360;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:KRX45711.1};
GN ORFNames=T05_1917 {ECO:0000313|EMBL:KRX45711.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX45711.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX45711.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX45711.1};
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 CRELD family.
CC {ECO:0000256|ARBA:ARBA00005897}.
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|ARBA:ARBA00008708}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:KRX45711.1}.
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; JYDJ01000071; KRX45711.1; -; Genomic_DNA.
DR Proteomes; UP000055048; 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:0005509; F:calcium ion binding; IEA:InterPro.
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 GO; GO:0032367; P:intracellular cholesterol transport; IEA:InterPro.
DR CDD; cd17913; DEXQc_Suv3; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00064; FU; 1.
DR CDD; cd00916; Npc2_like; 2.
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; 2.60.40.770; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR021852; DUF3456.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR003172; ML_dom.
DR InterPro; IPR033916; ML_Npc2-like.
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; PF11938; DUF3456; 1.
DR Pfam; PF02221; E1_DerP2_DerF2; 2.
DR Pfam; PF07645; EGF_CA; 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; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00261; FU; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00737; ML; 2.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KRX45711.1};
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:UP000055048};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 667..857
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1324..1369
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1423..1462
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 1359..1368
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1538 AA; 172090 MW; B23EE1DB40809EE5 CRC64;
MLSLTSNWRQ NGFAEPLCRR RPEEHFPTSM TMLAATRTKF TLIVCFAFGF FYFAQPKSVE
FNNCKSIFTV NDVAVDPCDA EGSTCPLIRG SKASITIRFV PDREVKQLKA RVHGILMKLG
KVPFLLPNSD ACKNSNLTCP LVAGEEYTYQ QSIHVLRSYP KMNLLIKWEL IEPGDEPKNG
SVPIIAVMYK LLSYACLLAA AVAININFRD CGSVAGSVQN VTLDPCDNPN YCSLKRGTSP
KVGILFTPSK CKVKLDCSIL RPMYTIAGQE TTAVHVVVHG IIKGLPVPFP VPNPDGCKDS
GLQCPLSSNN TVHYEDVFDV KSEYPTIGLL VRWELVDQNK KDLFTVARRT VNNENFDEIG
QLYLTQVVRD MTSVKAVLLG LRNTGRLLQL RHLSGSKKSF EDLVVPLTVK SASTANDVDV
GVEFGGILAK DALASVLSQF ARRPAVRKLG AEHGLTGKFF LQALASFRRY CQESAVLPVD
LHIMLADILQ NSRHVDDLFP LFLRHARQVF PHLECIEELK NISDLRLPQN WYPEARSIQR
RVIFHAGPTN SGKTYQALQR YLAAKSGVYC GPLKLLASEV FHKSNAAGVP CDLITGEERC
LANGQTCSEH ISCTVEMLDT RVHYEVAVID EIQMMRDLQR GWAWTRALLG VCADEIHVCG
ESAAVDFVKE LLVSLGDEFE VHTYERKTPL KVLDSPLGSL DSIQPYDCIV AFNRNDLFKV
TRQVEASGRS VAMIYGSLPP GTKLAQARKF NDPDDPCDVL VATDAIGMGL NLSIRRVIFY
SLVKVTLNES GEKELEPIST SQALQIAGRA GRFGTFHESG EVTTLRMEDL PALKAILTKP
TEPISAAGLF PTLEQIEMFS YYLPKATLSN LLDIFVSLSA VDESRFFMCN VDDLKFLADM
IEHVPLTLKV RYIFCMAPIS RKKPFVCGMF LRYARKFSRG EPLTSDWLAR TVGWPFSAPT
KIVDLIHLED VFDVLDTYLW LGYRFTDMFP ETEQVRAMQR ELDVLIRESL QNVKQLLKTV
QVAGLFDQQG LNGFDSKSPT TANAAAVAKD SPAKMKQATT TAATAVRKGG VIQSLIKQGL
LTPGMVEQIR KEIQADQEEL FIPTHYFPIT TDLMLFSYLF ECSCGREVNT FAFTISALYF
ANTIAANNLS QRVSFSWRRI RTNKTILTTN RHQQNRLACC CPIDVLLVVD LASRATDVPH
GDRCDTCRFL ARSFEKGFND TNKSHFEGGN TAWENENLGK YSTSETRFIE IMELICSKKS
KDVKEESKIK NLESKCHAMA EEHEETLETW YYHNQKKYPD LFDWFCIRTV KVCCPDNTFG
ASCAPCPGDP KRPCFGNGIC EVMNNIGSGS RFGSGKCKCH RGYQGKLCRH CDSNFFKVHS
NETYILCQPC HESCKGGCSG EGPRECNSCR VGWIMDEDTG CKDIDECESS PCTDQFEICE
NTPGSYKCVC AEAFRREDGV CIPDPDVPRP KPVFFGLLAQ QVLRYASYFG LLLSFLLILL
RPKTPLIVLF TLIMNDKKYS AGRIENSKTF EEETHDEL
//
