ID A0A2K5HWD3_COLAP Unreviewed; 872 AA.
AC A0A2K5HWD3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000008606.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000008606.1}
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. DDX10/DBP4
CC subfamily. {ECO:0000256|ARBA:ARBA00038084}.
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DR RefSeq; XP_011782070.1; XM_011926680.1.
DR AlphaFoldDB; A0A2K5HWD3; -.
DR STRING; 336983.ENSCANP00000008606; -.
DR Ensembl; ENSCANT00000031471.1; ENSCANP00000008606.1; ENSCANG00000027716.1.
DR GeneID; 105500988; -.
DR KEGG; cang:105500988; -.
DR CTD; 1662; -.
DR OMA; FLWRQKQ; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17941; DEADc_DDX10; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR24031:SF54; ATP-DEPENDENT RNA HELICASE DDX10-RELATED; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 69..97
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 100..274
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 287..448
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..97
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 20..40
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 872 AA; 100644 MW; 8444DA6F9C443B34 CRC64;
MGKTADPPGS GARPDPVRSF NRWKKKHSHR QNKKKQLRKQ LKKPEWQVER ESISRLMQNY
DKINVNEITR FSDFPLSKKT LKGLQEAQYR LVTEIQKQTI GLALQGKDVL GAAKTGSGKT
LAFLVPVLEA LYRLQWTSMD GLGVLIISPT RELAYQTFEV LRKVGKNHDF SAGLIIGGKD
LKHEAERINN INILVCTPGR LLQHMDETVS FHATDLQMLV LDEADRILDM GFADTMNAII
ENLPKKRQTL LFSATQTKSV KDLARLSLKD PEYVWVHEKA KYSTPATLEQ NYIVCELQQK
ISVLYSFLRS HLKKKSIVFF SSCKEVQYLY RVFCRLRPGI SILALHGRQQ QMRRMEVYNE
FVRKRAAVLF ATDIAARGLD FPAVNWVLQF DCPEDANTYI HRAGRTARYK EDGEALLILL
PSEKAMVQQL LQKKVPVKEI KINPEKLIDV QKKLESFLAQ DRDLKERAQR CFVSYIRSVY
LMKDKEVFDV SKLPIPEYAL SLGLAVAPRI RFLQKMQKQP TKELVMSQAD KVIEPRAPSL
TNDEVEEFRA YFNEKMSILQ KDGKRLEGTE HRLDNDTGDE EQDEEEDDEE EMEEKLAKAK
GSQAPSLPNT SEAQKIKEVP TQFLDRDEEE EDADFLKVKR HNVFGLDLKE EKTLQKKEPS
KSSVKKKVTK VAEAKKVMKR NFKVNKKITF TDEGELVQQW PQMQKSAIKD AEEDDDTGGI
NLDKAKERLQ EEDKFDKEEY RKKIKAKHRE KRLKEREARR EANKRQAKAK DEEEAFLDWS
DDDDDGFDPS TLPDPDKYRS SEDSDSEDME NKISDTKKKQ GMKKRNNSEV EDVGPSSRNR
KKAKWDTLEP LDTGLSLAED EELVLHLLRS QS
//
