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Database: UniProt
Entry: G3UJN7_LOXAF
LinkDB: G3UJN7_LOXAF
Original site: G3UJN7_LOXAF 
ID   G3UJN7_LOXAF            Unreviewed;       994 AA.
AC   G3UJN7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=DHX36 {ECO:0000313|Ensembl:ENSLAFP00000028046.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000028046.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000028046.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000028046.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000028046.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000028046.1};
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};
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DR   AlphaFoldDB; G3UJN7; -.
DR   Ensembl; ENSLAFT00000033499.1; ENSLAFP00000028046.1; ENSLAFG00000015342.3.
DR   GeneTree; ENSGT00940000156903; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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   CDD; cd17981; DEXHc_DHX36; 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; 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:SF237; ATP-DEPENDENT DNA_RNA HELICASE DHX36; 1.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 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; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          203..373
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          463..633
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   994 AA;  113313 MW;  75BCB521CD4A034A CRC64;
     MSSDYSQSWG RDGCPRSSGG GFGGGRGGGH GGSRGRGRHP GHLKGRQIGL WYARLQGQKN
     KEAERQERAV VHMDEHREER IVQLLNSVQA KNDKDSEAQI SWFAPEDHGQ NTEVPAENKP
     SSEKKLEDQE KKLINQEKKP FRSRDRSYMD RDSEYLLQEN EPDITLDRQL LEDLQRKKTE
     PRYIEMQHFR EKLPSHGMQK ELVSLIANHQ VTVISGETGC GKTTQVTQFI LDDYIKQGKG
     SACRIVCTQP RRISAISVAE RVAAERAEPC GNGNSTGYQI RLQSRLPRKQ GSILYCTTGI
     ILQWLQSDPH LSSVSHMVLD EIHERNLQSD VLMTVIKDLL TSRPDLKVIL MSATLNAEKF
     SEYFGHCPMI HIPGFTFPVV EYLLEDIIEK IRYVPEQKEP RSQFRRGFMQ GRVSRQEKEG
     KEAIYEERWP DYVRELRGRY SARTVDVLEM MDDDKVDLNL IAALIRHIVL EEEDGAILVF
     LPGWDNISSL HDLLMSQVMF KSDKFLIIPL HSLMPTVNQT QVFKKTPPGV RKIVIATNIA
     ETSITIDDVV YVIDGGKIKE THFDTQNNIS TMSAEWVSKA NAKQRKGRAG RVQPGHCYHL
     YNGLRASLLD DYQLPEILRT PLEELCLQIK ILRLGGIAYF LRRLMDPPSN EAVLLSIKHL
     IELNALDKQE ELTPLGVHLA RLPVEPHIGK MILFGALFCC LDPVLTIAAS LSFKDPFVIP
     LGKEKIADAR RKELAKGSRS DHLTVVNAFK GWEEARRRGF RYEKDYCWEY FLSSNTLQML
     HSMKAQFAEH LLGAGFVGGR NPKDPDSNIN SDNEKIIKAV ICAGLYPKVA KIRPNLGKKR
     KMVKVYTKSD GLVAIHPKSV NVEQTDFHYN WLIYHLKMRT SSIYLYDCTE VSPYCLLFFG
     GDISIQKDDD QETIAVDEWI VFQSPARIAH LVKELRKELD VLLQEKIESP HPVDWNDTKC
     RDCAVLSAII DLIKTQEKAM PRNFPPRYQD GCYS
//
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