ID A0A2K5YD71_MANLE Unreviewed; 899 AA.
AC A0A2K5YD71;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Chromodomain helicase DNA binding protein 1 like {ECO:0000313|Ensembl:ENSMLEP00000013475.1};
GN Name=CHD1L {ECO:0000313|Ensembl:ENSMLEP00000013475.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000013475.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000013475.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K5YD71; -.
DR Ensembl; ENSMLET00000036916.1; ENSMLEP00000013475.1; ENSMLEG00000030900.1.
DR GeneTree; ENSGT00940000159402; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd18006; DEXHc_CHD1L; 1.
DR CDD; cd03331; Macro_Poa1p-like_SNF2; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 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 InterPro; IPR031053; ALC1.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
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 PANTHER; PTHR47157; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1-LIKE; 1.
DR PANTHER; PTHR47157:SF1; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1-LIKE; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT DOMAIN 60..224
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 352..514
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 706..899
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT REGION 629..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..710
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 101327 MW; 2994EA3B8B76C56E CRC64;
MERAGAASRG GQAPGFLLRL HTEGRAEAAR ARVQEQDLRQ WGLTGIHLRS YQLEGVNWLA
QRFHCQNGCI LGDEMGLGKT CQTIALLIYL AGRLNDEGPF LILCPLSVLS NWKEEMQRFA
PGLSCVTYAG DKEERACLQQ DLKQESHFHV LLTTYEVFIP WVFSHRFPWS VLVVDEAHRL
KNQSSLLHKT LSEFSVVFSL LLTGTPIQNS LQELYSLLSF VEPDLFSKEE VGDFVQRYQD
IEKESESASE LHKLLQPFLL RRVKADVATE LPKKTEVVIY HGMSALQKKY YKAILMKDLD
AFENETAKKV KLQNILSQLR KCVDHPYLFD GVEPEPFEVG DHLIEASGKL HLLDKLLAFL
YSGGHRVLLF SQMTQMLDIL QDYMDYRGYS YERVDGSVRG EERHLAIKNF GQQPIFVFLL
STRAGGVGMN LTAADTVIFV DSDFNPQNDL QAAARAHRIG QNKSVKVIRL IGRDTVEEIV
SRKAASKLQL TNMIIEGGHF TLGAQKPSAD ADLQLSEILK FGLDKLLASE GSTMDEIDLE
SILGETKDGQ WVSDALPAAE GGIREQEEGK NHMYLFEGKD YSKEPSKEDR KSFEQLVNLQ
KTLLEKTSQE GRSLRNKGSV LIPGLVEGST KRKQVLSPEE LEDRQKKRQE AAAKRRRLIE
EKKRQKEEAE HKKKMAWWES NHYQSFCLPS EESEPEDLEN GEDESSAELD YQDPDATSLK
YVSGDVTHPQ AGAEDALIVH CVDDSGHWGR GGLFTALEKR SAEPRKIYEL AGKMKDLSLG
GVLLFPVDDK ESRNKGQDLL ALIVAQHRDR SNVLSGIKMA ALEEGLKKIF LAAKKKKASV
HLPRIGHATK GFNWYGTERL IRKHLAARGI PTYIYYFPRS KSSVLHSQSS SSSSRQLVP
//