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Database: UniProt
Entry: H2NJ34_PONAB
LinkDB: H2NJ34_PONAB
Original site: H2NJ34_PONAB 
ID   H2NJ34_PONAB            Unreviewed;      1156 AA.
AC   H2NJ34; A0A2J8XIY5;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 62.
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:ENSPPYP00000005819.3};
GN   ORFNames=CR201_G0000739 {ECO:0000313|EMBL:PNJ81961.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000005819.3, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000005819.3, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ81961.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ81961.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000005819.3}
RP   IDENTIFICATION.
RG   Ensembl;
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000256|ARBA:ARBA00008792}.
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DR   EMBL; NDHI03003364; PNJ81961.1; -; Genomic_DNA.
DR   STRING; 9601.ENSPPYP00000005819; -.
DR   Ensembl; ENSPPYT00000006042.3; ENSPPYP00000005819.3; ENSPPYG00000005106.3.
DR   eggNOG; KOG0926; Eukaryota.
DR   GeneTree; ENSGT00550000074985; -.
DR   HOGENOM; CLU_001832_0_0_1; -.
DR   OMA; KYAYHCA; -.
DR   TreeFam; TF105654; -.
DR   Proteomes; UP000001595; Chromosome 12.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; 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; PF00270; DEAD; 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:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595}.
FT   DOMAIN          261..428
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          547..715
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..182
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..221
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..576
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1156 AA;  129459 MW;  19CE1326ACEBCD18 CRC64;
     MGKLRRRYNI KGRQQAGPGP SKGPPEPPPV QLELEDKDTL KGVDASNALV LPGKKKKKTK
     APPLSKKEKK PLTKKEKKVL QKILEQKEKK SQRAEMLQKL SEVQASEAEM RLFYTTSKLG
     TGDRMYHTKE KPDEVVAPGQ EKISSLSGAH RKRRRWPSAE EEEEEEESES ELEEESELAE
     DPAAEPAEAG MGTTVAPLPP APAPSSQPVL AGMSVPPPPA AAPPLPRALA KPAVFIPVNR
     SPEMQEERLK LPILSEEQVI MEAVAEHPIV IVCGETGSGK TTQVPQFLYE AGYSSEDSII
     GVTEPRRVAA MAMSQRVAKE MNLSQRVVSY QIRYEGNVTE ETRIKFMTDG VLLKEIQKDF
     LLLRYKVVII DEAHERSVYT DILIGLLSRI VTLRAKRNLP LKLLIMSATL RVEDFTQNSR
     LFAKPPPVIK VESRQFPVTV HFNKRTPLED YSGECFRKVC KIHRMLPAGG ILVFLTGQAE
     VHALCRRLRK AFPPSRARPQ EKDDDQKDSA EEMRKFKKSR ARAKKARAEV LPQINLDHYS
     VLPAGEGDED REAEVDEEEG ALDSDLDLDL GDGGQDEGEQ PDASLPLHVL PLYSLLAPEK
     QAQVFKPPPE GTRLCVVATN VAETSLTIPG IKYVVDCGKV KKRYYDRVTG VSSFHVTWVS
     QASADQRAGR AGRTEPGHCY RLYSSAVFGD FEQFPPPEIT RRPVEDLILQ MKALNIEKVI
     NFPFPTPPSM EALLAAEELL IALGALQPPQ KAERVKQLQK NRLSCPITAL GRTMATFPVA
     PRYAKMLALS RQHGCLPYAI TIVASMTVRE LFEELDRPAA SDEELARLKS KRARVAQMKR
     TWAGQGASLK LGDLMVLLGA VGACEYAGCT PQFCEANGLR YKAMMEIRRL RGQLTTAVNA
     VCPEAELFVD PKMQPPTESQ VTYLRQIVTA GLGDHLARRV QSEELLEDKW RNAYKTPLLD
     DPVFIHPSSV LFKELPEFVV YQEIVETTKM YMKGVSSVEV QWIPALLPSY CQFDKPLEEP
     APTYCHERGR VLCHRASVFY RVGWPLPAIE VDFPEGIDRY KHFARFLLEG QVFRKLSSYQ
     SCLLSSPGTM LKTWARLQPR TESLLRALVA EKADCHEALL AAWKKNPKYL LAEYCEWLPQ
     AVHPDIEKAW PPTTVH
//
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