ID A0A077Z877_TRITR Unreviewed; 1096 AA.
AC A0A077Z877;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=TTRE_0000317501 {ECO:0000313|EMBL:CDW54905.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW54905.1};
RN [1] {ECO:0000313|EMBL:CDW54905.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW54905.1}
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}.
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DR EMBL; HG805923; CDW54905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077Z877; -.
DR STRING; 36087.A0A077Z877; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR CDD; cd17982; DEXHc_DHX37; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
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; 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:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
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 Helicase {ECO:0000313|EMBL:CDW54905.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 232..399
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 427..663
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 21..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 123332 MW; A37268B2CA360848 CRC64;
MEEEPVYVLP HDTANAFVLP PRKKKAKKEG NDKIKESKQK AAISKKKQKK LKKLLEKRKK
KAECADIFER LKRCQIEPSE MLLMTSVAKM QQKDPKRLPI VPEAPVCKSI AGSRKGMLSR
EQAFERSTPY FETDSSSGSD EEDADDKVPE ISNGNNPSLI QSDPLQSASC SNEPAKEKLF
ESTIPKPETA CTTAVDSKVI SCPAVHVPVF RSDEIEKGRL KLPVVAEEQA IIEAIKENQV
VIVCGETGSG KSTQVPQFLY EAGFTTAGKM IGVTEPRRVA AINISHRVAD EMNLSRDVVS
YQIRFEGNVT EKTKIKFMTD GVLLKEIQKD FLLSSYSAIL IDEAHERSMY SDVLIGLLSR
IILIRERRQD KLHLVIMSAT LRVEDFLMPK LFKQTPTVIK VDSRQYPVTA YFSRHTMHDY
LQAAYRKVCQ VHRLLPRGSI LVFVSGQKEV HTLLSWLKKR FPLNAKASEP KPDKKSLGKR
KKKLVNLDDY KEDSLHIFEE VDLNDQDAPD LDIFDVEELE CPDIPTASLE PDEPLFCLPL
YSLMPSGKQA RVFQEPPAGY RCCVIATNVA ETSVTIPNVR YVIDTGKEKV RLYDPVTGIS
KFVVQWISKA SASQRAGRAG RLGPGHCYRL YSSAVYNDFE KYSRPEILTE PLDDLVLQMK
AMCILKVCNF PFPTALDVDS LRCAEERLVK LGLLENALDS NGRQVARITK LGRTVALLPL
APRYGKMVAL ACQQGLLAYA ICLVSALSVR EPLLNPSTIE CKDIEKKKEK IAECLRSRRA
LAGQGHSLLL GDLMVLLKAS LAAEQELTVS FCEKHGFRYK AMVEICKMRR QLTKIVNALC
TEADLAIGTQ LKPPTDEQAE LLRQLVLTGL CENVARRADD CFAQTGCKPS RLAYRSAAVE
DPLWIHPTSV LFRAQPEWLV YQEIVDSNGK KCMLNVMAIE SEWLVALARG CCSMGEPLKE
PAPFYSETKD QIVCHVDCTY GLAAWPLPRQ EVAHPVDIMY YRYFASEFLE GRVISKLAKY
RSSLITPPSI LFKPWARLQS KTGSLLGVLV SNEVTSKEAL IRFWKEKPNF LCNEYLEWVA
QSKHNDVLFD WPPLEK
//
