ID A0A2K6A8C6_MANLE Unreviewed; 520 AA.
AC A0A2K6A8C6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=SP140 nuclear body protein like {ECO:0000313|Ensembl:ENSMLEP00000036288.1};
GN Name=SP140L {ECO:0000313|Ensembl:ENSMLEP00000036288.1};
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:ENSMLEP00000036288.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000036288.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K6A8C6; -.
DR Ensembl; ENSMLET00000059889.1; ENSMLEP00000036288.1; ENSMLEG00000042246.1.
DR GeneTree; ENSGT00940000164523; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05501; Bromo_SP100C_like; 1.
DR CDD; cd15626; PHD_SP110_140; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.10.390.10; SAND domain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR004865; HSR_dom.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR InterPro; IPR043563; Sp110/Sp140/Sp140L-like.
DR InterPro; IPR030411; Sp140_Bromo.
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; PTHR46386; NUCLEAR BODY PROTEIN SP140; 1.
DR PANTHER; PTHR46386:SF8; NUCLEAR BODY PROTEIN SP140; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF03172; HSR; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63763; SAND domain-like; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51414; HSR; 1.
DR PROSITE; PS50864; SAND; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 8..124
FT /note="HSR"
FT /evidence="ECO:0000259|PROSITE:PS51414"
FT DOMAIN 255..314
FT /note="SAND"
FT /evidence="ECO:0000259|PROSITE:PS50864"
FT DOMAIN 343..389
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 448..482
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 130..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 60222 MW; BA1D56F9BD21CDED CRC64;
MAGGGSDLST RIFTEDQDVD EGLLYDTIFK HFKRHKLEIS NAIKKTFPFL EGLRDRELIT
DKMFEDSQDS CRNLVPVQRV VYNVLSELEK TFNLPVLEAL FSEVNMQEYP DLIHIRKSFN
NAIQDKLSFQ ESDRKEREER PDIQLSLEQE EVPESPEAKM ENGQACGKMD TVGIGNNSTL
EKPKRKRKKK KGHSWTRIKS GTQKKIQQHD NSKPGGQLVP NEEKAKVNLQ GLSKISGSKR
SKPGTRFTQS DRAPQKRVRS RGSFLKCIQT EDGNWFTPGE FETKGGYARA KNWKLSVRCG
GRPLQRLIEE GSLPNPPKIH YRNQKRILKS HNNSSVDPCM RNLDECEVCR DGGELFCCDT
CSRVFHEDCH IAPVETERTP WSCIFCRMKE SSGSQQCCQE SEVLERQMCP QEQLKCEFLL
LKVYCCSESS FFAKIPYYYY IREACQGLKE PMWLDKIKKR LNEHSYPQVE GFIRDMRLIF
QNHRASYKYN DFGQMGLRLE AEFEKDFKEV FAIQETNGNS
//