ID A0A2K5MTE9_CERAT Unreviewed; 1096 AA.
AC A0A2K5MTE9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=DHX37 {ECO:0000313|Ensembl:ENSCATP00000028494.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000028494.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000028494.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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DR AlphaFoldDB; A0A2K5MTE9; -.
DR STRING; 9531.ENSCATP00000028494; -.
DR Ensembl; ENSCATT00000052749.1; ENSCATP00000028494.1; ENSCATG00000037537.1.
DR GeneTree; ENSGT00550000074985; -.
DR OMA; KYAYHCA; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000037537; Expressed in skeletal muscle tissue and 11 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0032040; C:small-subunit processome; IEA:Ensembl.
DR GO; GO:0034511; F:U3 snoRNA binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:2000020; P:positive regulation of male gonad development; IEA:Ensembl.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:Ensembl.
DR GO; GO:0042255; P:ribosome assembly; IEA:Ensembl.
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; 3.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
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:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 238..368
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 398..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..512
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 121880 MW; CB3F1A0BDE92CFEE CRC64;
MGKLRRRYNI KGRQQAGPGP SKGSPEPPPV QLELEDKDTL KGVDASNAVA RGSVHIRHTK
PPPSSERLGS TRAEMLQKLS EVQASEAEMR LFYTTSKLGT GDRMYHTKQK PDEVVAPGQE
KISSLSGAHR KHRRQPSTEE EEEEEESELE GESELDEDPA AELAEAGAGT TVAPLPPTPA
PSCQPAPAGM PVPPPPAAAP PLPRALAKPA VFIPVNRSPE MQEERLKLPI LSEEQVIMEA
VAEHPIVIVC GETGSGKTTQ VPQFLYEAGY SSEDSIIGVT EPRRVAAVAM SQRVTSCLAP
AGLRYKVVII DEAHERSVYT DILVGLLSRI VTLRAKRNLP LKLLIMSATL RVEDFTQNPR
LFAKPPPVIK VESRQFPVTV HFNKRTPLED YSGECFRKIC KIHRMLPAGG ILVFLTGQAE
VHALCRRLRK AFPPSRARPQ EKDDDQKDSA QEMRKFKKSR ARAKKARTEV LPQINLDHYS
VLPAGEGDED REAEVDEEEG ALDSDLDLDL GDGGQDGGEQ PDASLPLHVL PLYSLLAPEK
QAQVFKPPPE GTRLCVVATN VAETSLTIPG IKYVVDCGKV KKRYYDRVTG VSSFRVTWVS
QASADQRAGR AGRTEPGHCY RLYSSAVFGD FEQFPPPEIT RRPVEDLILQ MKALNIEKVI
NFPFPTPPSV EALLAAEELL IALGALQPPQ KAERVKQLQK NRLSCPITAL GRTMATFPVA
PRYAKMLALS RQHGCLPYAI TIVASMTVRE LFEELDRPAA SDEELARLKS KRAWVAQMKR
TWAGQGASLK LGDLMVLLGA VGACEYAGCT PQFCEANGLR YKAMMEIRRL RGQLTSAVNA
VCPEAELFVD PKMQPPTESQ VTYLRQIVTA GLGDHLARRV QSEELLEDKW RNAYKTPLLD
DPVFIHPSSV LFKELPEFVV YQEIMETTKM YMKGVSSVEV QWIPALLPSY CQFDKPLEEP
APTYCPERGR VLCHRASVFY RVGWPLPAIE VDFPEGIDRY KHFARFLLEG QVFRKLASYQ
SCLLSSPSTM LKTWARLQPR TESLLRALVA EKADCREALL AAWKKNPQYL LAEYCEWLPQ
AMHPDIEKAW PPTTDH
//
