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Database: UniProt
Entry: A0A2K5YD71_MANLE
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Original site: A0A2K5YD71_MANLE 
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}.
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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
//
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