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Database: UniProt
Entry: A0A158NDX0_ATTCE
LinkDB: A0A158NDX0_ATTCE
Original site: A0A158NDX0_ATTCE 
ID   A0A158NDX0_ATTCE        Unreviewed;      1196 AA.
AC   A0A158NDX0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=105618808 {ECO:0000313|EnsemblMetazoa:XP_012055728.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012055728.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012055728.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; ADTU01013059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012055728.1; XM_012200338.1.
DR   AlphaFoldDB; A0A158NDX0; -.
DR   STRING; 12957.A0A158NDX0; -.
DR   EnsemblMetazoa; XM_012200338.1; XP_012055728.1; LOC105618808.
DR   GeneID; 105618808; -.
DR   KEGG; acep:105618808; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   InParanoid; A0A158NDX0; -.
DR   OMA; DPMVAPE; -.
DR   OrthoDB; 5488182at2759; -.
DR   Proteomes; UP000005205; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   CDD; cd17971; DEXHc_DHX8; 1.
DR   CDD; cd21691; GH2-like_DHX8; 1.
DR   CDD; cd05684; S1_DHX8_helicase; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR044762; DHX8/Prp22_DEXHc.
DR   InterPro; IPR049588; DHX8_GH2-like.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049621; S1_DHX8_helicase.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 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   Pfam; PF00575; S1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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.
DR   PROSITE; PS50126; S1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005205}.
FT   DOMAIN          243..314
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          550..713
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          731..911
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          126..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..217
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1196 AA;  136444 MW;  B2739580C91CC010 CRC64;
     MEEVNQLEHL SLVSKICTEL ENHLGLNDKD LAEFIIHLAE NNKTFLSFKK VLIENGAEFS
     DSFIANLLRI IQHMKPVKSS TEKPSKNKQD ELAIKFPALA LPNDDPRSET NDEDIVNDVM
     ASLEAFAPSN KKHSANIEKS NGKIDNGEKK NKRERKSRSR SRDKRRHRSL NQKERRRRSR
     TRSRSRTRYR SRDRARRRRS GSRERKRSSS RNHKDTRHSR RRDADRSRSR SVEETLSVEP
     EVGKIYAGKV ANIVPFGCFV QLEGLRRRWE GLVHISQLRR EGRVANASDV VSRGQKVLVK
     VLSVGGQKVS LSMKDVDQET GRDLNPVVPI AKADEDEKHL RNPDRPTSLL ELQGNYDEDE
     TYSRKRVQRL SSPEKWEIKQ MLAASCIDRS ELPEFDTETG ILPREDDEEE DVEIELVEEE
     PPFLHGHGRA LGDLSPVRIV KNPDGSLAQA AMMQSALAKE RREQKMLQRE QEMDSVPTGL
     NKNWIDPLPE AESRTLAANM RGIGLQTQDL PEWKKHVIGG KKSSFGKKTN LTLLEQRQSL
     PIYKLRDDLV KAVTDNQILI VIGETGSGKT TQITQYLAET GFTARGKIGC TQPRRVATMS
     VAKRVAEEFG CCLGQEVGYT IRFEDCTGPE TSIKYMTDGM LLRECLMDLD LKTYSVIMLD
     EAHERTIHTD VLFGLLKQAV GRRPDLKLIV TSATLDAVKF SQYFFEAPIF TIPGRTFEVE
     VMYTKEPETD YLDAALITVM QIHLREPPGD ILLFLTGQEE IDTACEILYE RMKSLGPDVP
     ELIILPVYSA LPSEMQTRIF EPAPPGSRKV VIATNIAETS LTIDGIYYVV DPGFVKQKVY
     NSKTGMDSLI VTPISQAAAK QRSGRAGRTG PGKCYRLYTE RAYRDEMLPT PVPEIQRTNL
     ATTVLQLKTM GINDLLHFDF MDAPPVESLI MALESLHSLS ALDNEGLLTR LGRRMAEFPL
     EPNLSKMLIM SVHLQCSDEI LTIVSMLSVQ NVFYRPKDKQ ALADQKKAKF NQPEGDHLTL
     LAVYNSWKNN KLSNAWCYEN FVQIRTLKRA QDVRKQLLGI MDRHKLDVVS AGKNTVRIQK
     AVCSGFFRNA AKKDPQEGYR TLVDSQVVYI HPSSALFNRQ PEWVIYHELV QTTKEYMREV
     TTIDPKWLVE FAPAFFKFSD PTKLSKFKKN QRLEPLYNKY EEPNAWRISR VRRRRN
//
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