ID A0A2K5JTB6_COLAP Unreviewed; 1686 AA.
AC A0A2K5JTB6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 {ECO:0008006|Google:ProtNLM};
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:ENSCANP00000032101.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000032101.1}
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 STRING; 336983.ENSCANP00000032101; -.
DR Ensembl; ENSCANT00000055324.1; ENSCANP00000032101.1; ENSCANG00000036013.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0070603; C:SWI/SNF superfamily-type complex; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd18062; DEXHc_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-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 InterPro; IPR030100; BRG1_ATP-bd.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF76; TRANSCRIPTION ACTIVATOR BRG1; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080}.
FT DOMAIN 171..206
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 460..532
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 836..1001
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1154..1316
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1516..1586
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..744
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1625
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1626..1652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1686
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1686 AA; 189511 MW; E1151AC8465CB399 CRC64;
MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPIPTQG
PGGYPQDNMH QMHKPMESMH EKGMSDDPRY NQMKGMGMRS GGHTGMGPPP SPMDQHSQGY
PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGADPQ ALGQQNRGPT PFNQNQLHQL
RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP
GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ
KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PMVPLHQKQS RITPIQKPRG
LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV
VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL
QHAKDFKEYH RSVTGKIQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MWGQGKSRLG
LGSQSWARIF ADPSDHQSDW VVRSRPPTPR INISDHLFLV GQILAACSEE GEAEWKGRDR
VAEDEEGYRK LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE
NAEGQTPAIG PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE
VAPRSDSEES GSEEEEEEEE EEQPQAAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA
KQDVDDEYGV SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN
NNLNGILADE MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV
KVSYKGSPAA RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH
CKLTQVLNTH YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT
GEKVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH
MQAKGVLLTD GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV
QGLDLYRASG KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT
KAEDRGMLLK TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA
HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI
LEHEEQDEEE DEVPDDETVN QMIARHEEEF DLFMRMDLDR RREEARNPKR KPRLMEEDEL
PSWIIKDDAE VERLTCEEEE EKMFGRGSRH RKEVDYSDSL TEKQWLKVYA IEEGTLEEIE
EEVRQKKSSR KRKRDSDAGS STPTTSTRSR DKDDESKKQK KRGRPPAEKL SPNPPNLTKK
MKKIVDAVIK YKDSSSGRQL SEVFIQLPSR KELPEYYELI RKPVDFKKIK ERIRNHKYRS
LNDLEKDVML LCQNAQTFNL EGSLIYEDSI VLQSVFTSVR QKIEKEDDSE GEESEEEEEG
EEEGSESESR SVKVKIKLGR KEKAQDRLKG SRRRPSRGSR AKPVVSDDDS EEEQEEDRSG
SGSEED
//
