ID A0A2K5IIZ1_COLAP Unreviewed; 1215 AA.
AC A0A2K5IIZ1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
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:ENSCANP00000016634.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000016634.1}
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A2K5IIZ1; -.
DR STRING; 336983.ENSCANP00000016634; -.
DR Ensembl; ENSCANT00000039575.1; ENSCANP00000016634.1; ENSCANG00000031479.1.
DR OMA; DPMVAPE; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd17971; DEXHc_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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044762; DHX8/Prp22_DEXHc.
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; 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 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080}.
FT DOMAIN 260..331
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 570..733
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 751..931
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 87..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..221
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 138736 MW; 9FEF5B37288C922A CRC64;
MAVAVAMAGA IIGSEPGPAE ELAKLEYLSL VSKVCTELDN HLGINDKDLG EPREVQTLET
FPELSVKPGA IISDSLISNL LRLIQTMRPP AKPSTSKDPV AKPKTEKEKL KELFPVLCQP
DNPSVRTMLD EDDVKVAVDV LKELEALMPS AAVQEKQRDT EHRDRTKKKK RSRSRDRDRD
RDRDRERNRD RDHKRRHRSR SRSRSRTRER NKAKSRYRSR SRSQSPPKDR KDRDKYGERN
LDRWRDKHVD RPPPEEPTIG DIYNGKVTSI MQFGCFVQLE GLRKRWEGLV HISELRREGR
VANVADVVSK GQRVKVKVLS FTGTKTSLSM KDVDQESGED LNPNRRRNLV GETNEETSMR
NPDRPTHLSL VSAPEVEDDS LERKRLTRIS DPEKWEIKQM IAANVLSKEE FPDFDEETGI
LPKVDDEEDE DLEIELVEEE PPFLRGHTKQ SMDMSPIKIV KNPDGSLSQA AMMQSALAKE
RRELKQAQRE AEMDSIPMGL NKHWVDPLPD AEGRQIAANM RGIGMMPNDI PEWKKHAFGG
NKASYGKKTQ MSILEQRESL PIYKLKEQLV QAVHDNQILI VIGETGSGKT TQITQYLAEA
GYTSRGKIGC TQPRRVAAMS VAKRVSEEFG CCLGQEVGYT IRFEDCTSPE TVIKYMTDGM
LLRECLIDPD LTQYAIIMLD EAHERTIHTD VLFGLLKKTV QKRQDMKLIV TSATLDAVKF
SQYFYEAPIF TIPGRTYPVE ILYTKEPETD YLDASLITVM QIHLTEPPGD ILVFLTGQEE
IDTACEILYE RMKSLGPDVP ELIILPVYSA LPSEMQTRIF DPAPPGSRKV VIATNIAETS
LTIDGIYYVV DPGFVKQKVY NSKTGIDQLV VTPISQAQAK QRAGRAGRTG PGKCYRLYTE
RAYRDEMLTT NVPEIQRTNL ASTVLSLKAM GINDLLSFDF MDAPPMETLI TAMEQLYTLG
ALDDEGLLTR LGRRMAEFPL EPMLCKMLIM SVHLGCSEEM LTIVSMLSVQ NVFYRPKDKQ
ALADQKKAKF HQTEGDHLTL LAVYNSWKNN KFSNPWCYEN FIQARSLRRA QDIRKQMLGI
MDRHKLDVVS CGKSTVRVQK AICSGFFRNA AKKDPQEGYR TLIDQQVVYI HPSSALFNRQ
PEWVVYHELV LTTKEYMREV TTIDPRWLVE FAPAFFKVSD PTKLSKQKKQ QRLEPLYNRY
EEPNAWRISR AFRRR
//
