ID A0A2K5IM63_COLAP Unreviewed; 1980 AA.
AC A0A2K5IM63;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
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:ENSCANP00000017808.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000017808.1}
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=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR Ensembl; ENSCANT00000040757.1; ENSCANP00000017808.1; ENSCANG00000032302.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd18057; DEXHc_CHD5; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR028727; DEXHc_CHD5.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF6; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 5; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 417..464
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 498..555
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 593..626
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 713..897
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1029..1194
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1598..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..411
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1980 AA; 224732 MW; DD4A9E3A2B37A6F9 CRC64;
WLGSLGGEQQ EPLSPGPGES EEEDGGLEGF DDFFPVEPVS LPKKKKPKKL KENKCKGKRK
KKEGSNDELS ENEEDLEEKS ESEGSDYSPN KKKKKKLKDK KEKKAKRKKK DEDEDDNDDG
CLKEPKSSGQ LMAEWGLDDV DYLFSEEDYH TLTNYKAFSQ FLRPLIAKKN PKIPMSKMMT
VLGAKWREFS ANNPFKGSSA AAAAAAVAAA VETVTISPPL AVSPPQVPQP VLIRKAKTKE
GKGPGVRKKI KGSKDGKKKG KGKKMAGLKF RFGGISNKRK KGSSSTHTPT YPSTIYYAST
LCLSGLGRCS WLCSGGADEA FHDCFSPTLV DDGDGYETDH QDYCEVCQQG GEIILCDTCP
RAYHLVCLDP ELEKAPEGKV PPPGLLPQEK EGIQWEPKDD DDEEEEGGCE EEEDDHMEFC
RVCKDGGELL CCDACPSSYH LHCLNPPLPE IPNGEWLCPR CTCPPLKGKV QRILHWRWTE
PPAPFMVGLP GPDVEPSLPP PKPLEGIPER EFFVKWAGLS YWHCSWVKEL QLELYHTVMY
RNYQRKNDMD EPPPFDYGSG DEDGKSEKRK NKDPLYAKME ERFYRYGIKP EWMMIHRILN
HSFDKKGDVH YLIKWKDLPY DQCTWEIDDI DIPYYDTLKQ AYWGHRELML GEDTRLPKRL
LKKGKKLRDD KQEKPPDTPI VDPTVKFDKQ PWYIDSTGGT LHPYQLEGLN WLRFSWAQGT
DTILADEMGL GKTVQTIVFL YSLYKEGHSK GPYLVSAPLS TIINWEREFE MWAPDFYVVT
YTGDKESRSV IRENEFSFED NAIRSGKKVF RMKKEVQIKF HVLLTSYELI TIDQAILGSI
EWACLVVDEA HRLKNNQSKF FRVLNSYKID YKLLLTGTPL QNNLEELFHL LNFLTPERFN
NLEGFLEEFA DISKEDQIKK LHDLLGPHML RRLKADVFKN MPAKTELIVR VELSQMQKKY
YKFILTRNFE ALNSKGGGNQ VSLLNIMMDL KKCCNHPYLF PVAAVEAPVL PNGSYDGSSL
VKSSGKLMLL QKMLKKLRDE GHRVLIFSQM TKMLDLLEDF LEYEGYKYER IDGGITGGLR
QEAIDRFNAP GAQQFCFLLS TRAGGLGINL ATADTVIIYD SDWNPHNDIQ AFSRAHRIGQ
NKKVMIYRFV TRASVEERIT QVAKRKMMLT HLVVRPGLGS KSGSMTKQEL DDILKFGTEE
LFKDDVEGMM SQGQRPVTPI PDVQSSKGGN LAASAKKKHG STPPGDNKDV EDSSVIHYDD
AAISKLLDRN QDATDDTELQ NMNEYLSSFK VAQYVVREED GVEEVEREII KQEENVDPDY
WEKLLRHHYE QQQEDLARNL GKGKRIRKQV NYNDASQEDQ EWQDELSDNQ SEYSIGSEDE
DEDFEERPEG QSGRRQSRRQ LKSDRDKPLP PLLARVGGNI EVLGFNARQR KAFLNAIMRW
GMPPQDAFNS HWLVRDLRGK SEKEFRAYVS LFMRHLCEPG ADGAETFADG VPREGLSRQH
VLTRIGVMSL VRKKVQEFEH VNGKYSTPDL IPEGPEGKKP GEVISSDPNT PVPASPAHLP
PAPLGLPDKM EAQLGYMDEK DPGMQKPKKP LEVQALPAAL DRVEGEDKHE SPASKERARE
ERPEDTEKAP PSPEQLPREE VLPEKEKILD KLELSLIHSR GDGSELRPDD TKAEEKEPIE
TQQNGDKEED DEGKKEDKKG KFKFMFNIAD GGFTELHTLW QNEERAAVSS GKIYDIWHRR
HDYWLLAGIV THGYARWQDI QNDPRYMILN EPFKSEIHKG NYLEMKNKFL ARRFKLLEQA
LVIEEQLRRA AYLNMTQDPN HPAMALNARL AEVECLAESH QHLSKESLAG NKPANAVLHK
VLNQLEELLS DMKADVTRLP SMLSRIPPVA ARLQMSERSI LSRLTNRAGD PTIQQGAFGS
SQMYSNSFGP NFRGPGPGGI VNYNQMPLGP YPCPAPAVLL VADITSCLTP SLPAQDQEGG
//
