ID A0A9D4L2W0_DREPO Unreviewed; 1024 AA.
AC A0A9D4L2W0;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE RecName: Full=Exosome RNA helicase MTR4 {ECO:0000256|ARBA:ARBA00069430};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=Superkiller viralicidic activity 2-like 2 {ECO:0000256|ARBA:ARBA00082023};
DE AltName: Full=TRAMP-like complex helicase {ECO:0000256|ARBA:ARBA00077324};
GN ORFNames=DPMN_092831 {ECO:0000313|EMBL:KAH3850420.1};
OS Dreissena polymorpha (Zebra mussel) (Mytilus polymorpha).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC Myida; Dreissenoidea; Dreissenidae; Dreissena.
OX NCBI_TaxID=45954 {ECO:0000313|EMBL:KAH3850420.1, ECO:0000313|Proteomes:UP000828390};
RN [1] {ECO:0000313|EMBL:KAH3850420.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Duluth1 {ECO:0000313|EMBL:KAH3850420.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KAH3850420.1};
RA McCartney M.A., Auch B., Kono T., Mallez S., Zhang Y., Obille A.,
RA Becker A., Abrahante J.E., Garbe J., Badalamenti J.P., Herman A.,
RA Mangelson H., Liachko I., Sullivan S., Sone E.D., Koren S.,
RA Silverstein K.A.T., Beckman K.B., Gohl D.M.;
RT "The Genome of the Zebra Mussel, Dreissena polymorpha: A Resource for
RT Invasive Species Research.";
RL bioRxiv 0:0-0(2019).
RN [2] {ECO:0000313|EMBL:KAH3850420.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Duluth1 {ECO:0000313|EMBL:KAH3850420.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KAH3850420.1};
RA McCartney M.A., Auch B., Kono T., Mallez S., Becker A., Gohl D.M.,
RA Silverstein K.A.T., Koren S., Bechman K.B., Herman A., Abrahante J.E.,
RA Garbe J.;
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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:ARBA00049390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00049390};
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
CC Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus,
CC nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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:KAH3850420.1}.
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DR EMBL; JAIWYP010000003; KAH3850420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9D4L2W0; -.
DR Proteomes; UP000828390; Unassembled WGS sequence.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IEA:TreeGrafter.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd18024; DEXHc_Mtr4-like; 1.
DR CDD; cd13154; KOW_Mtr4; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR FunFam; 3.40.50.300:FF:000083; ATP-dependent RNA helicase DOB1; 1.
DR FunFam; 3.40.50.300:FF:000141; ATP-dependent RNA helicase DOB1; 1.
DR FunFam; 2.40.30.300:FF:000001; Mtr4 exosome RNA helicase; 1.
DR FunFam; 1.10.3380.30:FF:000002; superkiller viralicidic activity 2-like 2; 1.
DR FunFam; 1.10.3380.30:FF:000004; Superkiller viralicidic activity 2-like 2; 1.
DR Gene3D; 1.10.3380.30; -; 2.
DR Gene3D; 2.40.30.300; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR025696; Beta-barrel_MTR4.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR050699; RNA-DNA_Helicase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000828390};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 133..289
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 391..563
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 116205 MW; 6826B964D29CEC3F CRC64;
MADAFEEDLF NVFDADTASS RPVPEQDLPE NDRDSTEKDD SQRAEELLQS IAGKRPVVLE
DEEEQSTKKQ KTEAAGRLEV MQRIQVHTVE TVEACLHEVA IPPEADFVPL KRATTEPAKT
YPFILDPFQK EAILCLENNQ SVLVSAHTSA GKTVVAVYAI AMSLRDKQRV IYTTPIKALS
NQKYRELFEE FQDVGLMTGD VTINPTASCL VMTTEILRSM LYRGSEIMRE VGWVVFDEIH
YMRDKERGVV WEETIILLPD NVHYVFLSAT IPNARQFAEW ICHLHQQPCH VVYTDYRPTP
LQHYIFPAGG DGIHLVVDEN GEFREENFNT AMSVLKDAGE AAKGDTKGRK GGFKQQESNC
YKIVKMILER KFAPVIVFSF SKKDCEAYAM QMTKLDFNTE EEKILVQEVF NNAIDALSDE
DKKLPQVEHV LPLLKKGIGI HHGGLLPLLK ETIEILFSEG LIKALFATET FAMGLNMPAR
TVLFTSARKF DGQDFRWVTS GEYIQMSGRA GRRGLDDRGI VILMIDEKMP PAAGKAVLKG
AADPLNSAFH LTYNMVLNLL RVEEINPEFM LERSFYQFQN YAAIPGLIDQ LKVTEERYGK
CAVPNEDQVT SYYKIRQQLD HLGKELQAYI QKPQYLLPFL QPGRLVHVKN GEDDFGWTMV
VNFQKKANQS KSGDDGPVYV CEVLANLTKD SAQSRNSALI KPHRQPGTLG EMQASYCCRI
SAVRLYLPKD LRPLDNRQSV GKSIQEVEKR FPDGLPLLDP VEDMGIKEKS MKDVVKKIEA
FEHRLFSHPL NKDPNLEEWY SLYEKKMKIG NEVKTIKAEL KKKKSLLQMD ELKCRKRVLR
RLGYCTASDV IELKGRVACE ISSGDELMIT ELLFNGVFND LTPQQSAALL SCFVFDESAG
DVTMKLTEQL AGPLRLLQDT ARRIARVSKE AKLEIDEENY VGSFKAQMMD VVHAWCNGCS
FLEICKMTDI FEGSIIRCMR RLEETLRQMV QAAKAIGNTE LENKFNEAIR LMKRDIVFAA
SLYL
//
