ID W5UT56_ICTPU Unreviewed; 1008 AA.
AC W5UT56;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=mov10b.1 {ECO:0000313|EMBL:AHH42823.1};
GN Synonyms=mov10a {ECO:0000313|RefSeq:XP_017335051.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH42823.1};
RN [1] {ECO:0000313|EMBL:AHH42823.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed {ECO:0000313|EMBL:AHH42823.1};
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
RN [2] {ECO:0000313|RefSeq:XP_017335051.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017335051.1};
RG RefSeq;
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 -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005601}.
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DR EMBL; JT418717; AHH42823.1; -; mRNA.
DR RefSeq; XP_017335051.1; XM_017479562.3.
DR STRING; 7998.ENSIPUP00000035122; -.
DR Ensembl; ENSIPUT00000036503; ENSIPUP00000035122; ENSIPUG00000023578.
DR GeneID; 108271790; -.
DR KEGG; ipu:108271790; -.
DR CTD; 566858; -.
DR OMA; NDWDQDQ; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000221080; Chromosome 11.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR CDD; cd18038; DEXXQc_Helz-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR049080; MOV-10-like_beta-barrel.
DR InterPro; IPR026122; MOV-10/SDE3_DEXXQ/H-box.
DR InterPro; IPR049079; Mov-10_helical.
DR InterPro; IPR049077; MOV-10_Ig-like.
DR InterPro; IPR049075; MOV-10_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF537; HELICASE MOV-10; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF21634; MOV-10_beta-barrel; 1.
DR Pfam; PF21635; Mov-10_helical; 1.
DR Pfam; PF21633; MOV-10_Ig-like; 1.
DR Pfam; PF21632; MOV-10_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000313|EMBL:AHH42823.1,
KW ECO:0000313|RefSeq:XP_017335051.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Helicase {ECO:0000313|EMBL:AHH42823.1, ECO:0000313|RefSeq:XP_017335051.1};
KW Hydrolase {ECO:0000313|EMBL:AHH42823.1, ECO:0000313|RefSeq:XP_017335051.1};
KW Nucleotide-binding {ECO:0000313|EMBL:AHH42823.1,
KW ECO:0000313|RefSeq:XP_017335051.1}.
FT DOMAIN 538..720
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 87..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 114671 MW; 7678F2D461229667 CRC64;
MPSLREVCEV GLDFIEFLGE RKSKTDKKEL RDIYNLEFKR EGGPAFSRLV SALVCFNKAS
IRRGEVVLHG KSQIRLYYCD QWRSRTHSNP TVGSRPDHED STAPDSRQGA PYSSPRVNPV
LMPKKRLAQE TLKKLRANRP QLISDKGGIE VTSSPVGRNG KVVLNIELLD TVYVVKFQIV
NKGQKCIHFT FYTALHRIRC FTLVDERRVS RVSPLLLCPG ESYAVEVKYQ ARNYGYFPAT
MYFEFCPESE SSEPPKPFCI VREIEAVVHT QLSTDLGPTS PYRARQKGQN RPKDRVVEEG
VPPESMTHAL KQPVKLKDYK YSAYLKNLVH HWNSDGEKLS PTARQQLHRA RGLLESPMSV
KQYAERFQLI LHLEEIQMEE DIKKYDLYGQ TMKQDKMNKN LLVLRVPGVA ENRPSVLRGD
NLNVYLSEDK AQPITVYKGY VHRVELESVK LGFSKKLIKK FIPKMKFNVE FSFNRFPLKL
QHRAVQLVAE HRLGDVLFPI HNGVKQAALP KLRIYNRDLE TNPEQKAAVQ HILSGQYKPA
PYLIFGPPGT GKTVTLVEAI KQVNKSGPGV HVLACAPSNS ACDLLCERLL GFVDAHRLFR
LYACSRDPRT VPLKLLKYSN WLEMQDSFIL PSKETLMNYT IIVVTLITAG RLVSGGIPVG
HFTHIFIDEA GQVVEPECVV GIAGLLHPEK GQLVLAGDPK QLGAVLRSPL AQQHGLGLSL
LERLMTQISL YQKNQDGRQG YDSCFVTKLL RNYRSHPAIL KIPNELFYDN ELQVFANQME
REAFCKWEHL PKQGFPVIFH GVMGKDEREA NSPSFFNVSE IEVLIGYLKK LLQSHGKKGL
PKLSASDIGI IAPYRKQVDK MQKALKAVRE LHQWKDIKVG SVEEFQGQEK MVIMVSAVRS
SNSYVKMDQD FNIGFLTNEK RFNVAMTRAK ALLIVVGNPV ILSKNPTWQR FFQYCEQEQG
YTGFDYKDFE GEDDVVTRLA SLKIHTSADE IEASAVQQHV HPEWRNEQ
//
