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Database: UniProt
Entry: A0A2K6TIG0_SAIBB
LinkDB: A0A2K6TIG0_SAIBB
Original site: A0A2K6TIG0_SAIBB 
ID   A0A2K6TIG0_SAIBB        Unreviewed;       493 AA.
AC   A0A2K6TIG0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000019411.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000019411.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU365068}.
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DR   AlphaFoldDB; A0A2K6TIG0; -.
DR   STRING; 39432.ENSSBOP00000019411; -.
DR   Ensembl; ENSSBOT00000036231.1; ENSSBOP00000019411.1; ENSSBOG00000026304.1.
DR   GeneTree; ENSGT00680000100037; -.
DR   Proteomes; UP000233220; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24031:SF301; ATP-DEPENDENT RNA HELICASE DDX18; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU365068};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU365068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW   RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          235..400
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          31..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  56211 MW;  D35B7F6F1FE70905 CRC64;
     MSHLPMKLLR RKIEKRNLKL RQRNLKLQQR NLKLQETENG DVSEETMGGR KVKKSKHSMN
     VGLSEAQNGD VSQEAVENTK VKKSPQKSIE LTNGEAAMQS PNSESKKKKK KKKRKMVNDA
     GPDRKKAKTE NKGESEEESA ESPKETENNV EKPDNDEDDS EVPSLPLGLT GKCPGSFLDI
     ASLKYASQRV IARRQTMLFS ATQTRKVEDL ARISLKKEPL YVGVDDDKAN ATVDGLEQGY
     VVCPSEKRFL LLFTFLKKNR KKKLMVFFSS CMSVKYHYEL LNYIDLPVLQ KQNKRTTTFF
     QFCNADSGTL LCTDVAARGL DIPEVDWIVQ YDPPDDPKEY IHRVGRTARG LNGRGHALLI
     LRPEELGFLR YLKQSKVPLS EFDFSWSKIS DIQSQLEKLI EKNYFLHKSS QEAYKSYIRA
     YDSHSLKQIF NVNNLNLPQV ALSFGFKVPP FVDLNILFLM NNEGKQKKRG GGGGFGYQKP
     RNKKSSDSRQ FSH
//
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