ID   A0A452GFK5_9SAUR        Unreviewed;       936 AA.
AC   A0A452GFK5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000000346.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000000346.1}
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   ---------------------------------------------------------------------------
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   AlphaFoldDB; A0A452GFK5; -.
DR   STRING; 38772.ENSGAGP00000000346; -.
DR   Ensembl; ENSGAGT00000000390.1; ENSGAGP00000000346.1; ENSGAGG00000000294.1.
DR   Proteomes; UP000291020; 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:UP000291020};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          185..355
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          445..615
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   936 AA;  107148 MW;  7C43D892B549F20B CRC64;
     MSFEHRRDWS RGGGGGPRPS SSSAGGHEGR GGRGRHPSHL KGRDIGLWYA RKQSQKSKEP
     DRQQRAVVRM DEHREEQIVQ LLNTVQTRNE KEQESVSWWS GEEEGQEVPV EKPTLAKTSV
     KRRPILEKTF LDRDSEYLFQ ENEPDIDLNE KFREELRKKK FDPRYIEMQR FREKLPSYGI
     RRELVTVINN NQVTVISGET GCGKTTQVTQ FILDDYIERG KGSACRIVCT QPRRISAISV
     AERVAAERAE VCGNGKSTGY QIRLQSRLPR KQGSILYCTT GIVLQWLQSD KQLSSVSHVI
     LDEIHERNLQ SDVLMTIIKD LLNVRPDLKV ILMSATLNAE KFSEYFDNCP MIHIPGFTFP
     VMEYLLEDVI EKLRYTPEDT DYRPRRKKGF MQGQISRPEK EEKEEIYKER WPDYLRQLRG
     KYSAGTIDAL EMMDDDKIDL DLIAALIRHI VLEEEDGAIL VFLPGWDNIS TLHDLLMSQV
     MFKSDRFIII PLHSLMPTVN QTQVFKKTPP GVRKIVIATN IAETSITIDD VVYVIDGGKI
     KETHFDTQNN ISTMAAEWVS KANAKQRKGR AGRVQPGHCY HLYNGLRASL LDDYQLPEIL
     RTPLEELCLQ IKILRLGGIA YFLSRLMDPP SREAVVLSIN HLMELNALDR QEELTPLGVH
     LARLPVEPHI GKMILFGALF CCLDPVLTIA ASLSFKDPFV IPLGKEKVAD ARRKELSKNT
     KSDHLTIVNA FAGWEEVRQR GFRSEKDYCW EYFLSSNTLQ MLLNMKGQFA EHLLAAGFVS
     SKNPRDPKSN TNSDNEKLLK AVICAGLYPK VAKIRKSFSK KRKMVKVCTK TDGTVNIHPK
     SVNVEETEFH YNWLVYHLKM RTSSIYLYDC TEVSPYCLLF FGGDISIQKD KDQDTIAVDD
     WIVFESPARI GNLVKVIVHL PLFYAAFHSN IKNNNL
//