ID A0A077Z4L8_TRITR Unreviewed; 1195 AA.
AC A0A077Z4L8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=TTRE_0000189501 {ECO:0000313|EMBL:CDW53630.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW53630.1};
RN [1] {ECO:0000313|EMBL:CDW53630.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW53630.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) 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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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; HG805861; CDW53630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077Z4L8; -.
DR STRING; 36087.A0A077Z4L8; -.
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:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.30.160.20; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF119; ATP-DEPENDENT RNA HELICASE A; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 3..71
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 147..220
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 364..532
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 610..806
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 112..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1195 AA; 133546 MW; C07D5A58083F11A5 CRC64;
MAEVKAILNQ WAAKRSIKPQ YDMRAVLGDN GLQFHCDLTL TGFDHVSYGC STNKKAAMTT
AARDFCAFLL RTKNMDISMF PANIREDIEA DSSSSAAPNT TTTSTELVAN ISEVPKEPAS
TDSPVGANSS KKTTDIQEDC GGWTLENSKQ CLNQFMQTYK LTNFAYEYKL SGPSHRLEFV
AEASLPVPDL NMTISASGKG FSKKQASACC AMSLVHQLYN LGVIRKFEEA TPKKKLEVPI
YDVFVPPPLE QDISDYLTTE GINYVEATSG SLESVSLITE DNDDSSMPVV DHLVNSVRWS
PPIMNFNPWT GKQIEDGNWS TMTLEQISAY LFAQRFSRET SESYKLMLKA RNELPVFSSK
EKILDAVNNN SATLVVGETG CGKTTQVCQY ILDSMLDNGK GACCNIIVTQ PRRISAITVA
ERVATERGEK LGQSVGYSVR FDSHFPSPYG SIMFCTPFKG VLLRRMENGL QGVSHIIVDE
VHERDVDTDF LLIILRDLLA IYPDLRVILM SATVDTSLFE QYFNGCATVH IEGRLFSVTR
YFLEDAVQMT NFVIDEAMED SFVEDKIISE SANVENLNLI VSDSYPESVR KTVAMMPEND
SNFELIQAII VQQIAQGVKG SILVFLPGWN IIITLQRFLE TRLADGSLTY ASYLGGIKCV
LLPLHSQLPK ENQFQVFEAV PPGFTKVCAH FCLQLFQCHP RILLQIILAT NIAESSVTIS
DVVMVIDSCK VKLKKYTSYN NMIHYVTTWA SKSNLQQRCG RAGRCQPGVC FHLCSKARFE
RLDQYSEPEM LRSPLHETVL AVKLLGLGSS VNFLSKAMQP PPLDSVCEAE MVLRDIGALT
KDSQLTALGR ILAHLPIDPV FGKTIVLGTI FSIGDIMCSI AALSSFIEPY IIPLHQKRLS
ESQKAFTGSR FSDHTALLEI YQCFVAARHN IIISAPFNYG IQSEKDFCRS YRVNAPLLRT
IFEATHQLKT LLQNFGFLPE LLQMHRICTR LGLIETTLLG KRCPMMALFQ MTSLLIAAYY
PNVCWHYGKR RVLTLENTTA LIHKHSVNCE SQNVQFPSPF FVFSEKMRTG TVACRQLSMV
THLQLLLFGA KSVELCDDLV VLDNWLKLRM SPVVAAKIVA LRRCVNRLVG LAKCHLTNEK
ECGDELQNVQ DSTCRAVAAE EGIVMVLYSI HRITMFRKNL CYSRGYVNTI QHCSY
//