ID A0A158QPY1_HAEPC Unreviewed; 1550 AA.
AC A0A158QPY1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Bromo domain-containing protein {ECO:0000313|WBParaSite:HPLM_0001355601-mRNA-1};
GN ORFNames=HPLM_LOCUS13548 {ECO:0000313|EMBL:VDO49624.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001355601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001355601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO49624.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO49624.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; UZAF01018250; VDO49624.1; -; Genomic_DNA.
DR STRING; 6290.A0A158QPY1; -.
DR WBParaSite; HPLM_0001355601-mRNA-1; HPLM_0001355601-mRNA-1; HPLM_0001355601.
DR OMA; KSSLRIX; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; Unassembled WGS sequence.
DR GO; GO:0016586; C:RSC-type complex; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 6.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR037382; Rsc/polybromo.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16062:SF19; PROTEIN POLYBROMO-1; 1.
DR PANTHER; PTHR16062; SWI/SNF-RELATED; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF00439; Bromodomain; 4.
DR Pfam; PF00505; HMG_box; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 2.
DR SMART; SM00297; BROMO; 4.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF47370; Bromodomain; 5.
DR SUPFAM; SSF47095; HMG-box; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 4.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000268014};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 59..121
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 163..217
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 452..514
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 567..637
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 836..956
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1015..1133
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1172..1243
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1254..1284
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DNA_BIND 1172..1243
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1487..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1550 AA; 177998 MW; E77C7149D895BBC5 CRC64;
MSAKRKRLED TAENSPPEGT PTPKRRKGRI SAKERERISE ENRKAQGVYN VLRQHTDSEN
RQLAEKFIRT PSRRAEPDYY KQVKSPIDFT RIQQKLKTEE YQTFEEFCED VELLVDNTRT
YYKVWSISPA PSSRASSNGS SDEVETEMVE DILCALLELT DSTGRLISPP FRVLQSKEEF
PVYYEKIRHP MDLKTIAEKA RAGLYKRMSQ VEADVRLQIF SGKGSEIYKD AVALMTFFKE
KRDLVLEKGV HPKRRDKVRR AVDGLLIQAA LPPVAELSED SEEDEDTEES DDPLWKLYWT
VRNLNGNCQF NSLFSAIILI ILMKYLVFEN ACEYNMESSD IFIAAQKLQN LTIRKARELQ
PSLDLSASSN FIFIPTIQSL ASTPPPEKKR YRSPKKMRPI STGMTAEHVS LPGRPGRKSM
DELMLRYRQK LMTFWDLIYN HKIGIYWPAG AFMELPSSRE YPDYYQVIEH PIDMKIIRDK
IENNRYESSV QLIEEFTILF NNARQYNEAN SQIARDAAVL LSMVTTAHAT DKDAPYESPM
ALKQKLPAHE QQMWKLYTLV RDATDADGRK LAGAFIKLPT KEEYPDYYEV IRKPMDLQRI
QHRLQAHGYG RWIDLVADLS LMLENACKYN EPESTIYKDA VALQRLVLEK KRELGAAEDC
MPRVQMEIRT MFTNIFSILF LFFLDSEGRC RCDSFAELPD LLKARGFPRD EWPFSLDQIK
RNIDKVLLPC EYSIFSRLHD FPLIRRRFDG QGIFDFFDLF ERARELSRSD SKLFEDATEL
QLAFIRERDA QCKGVLVSTA FIAIENVMTS HDSIILRELF LQEGEVDLDS LNFDGVEYIT
PSYAYITRTD DNSRAPPHIM RIERIFKTDT GEMMVRGKWV YRPHETLHLA NRKFIENEVF
ITPFIDTVLA ERLCGKCMVV PVKVAMHNVV EGINPTDLFV CECRYLGKPR YFAKLKSWPF
PGEEDSLKLT SRSRPLSPVR VTSNFMNVDG VIPARAEADA DGRTYLHAMR THSGKYHDVG
QFVLVFNPQK PTCDVMRVDK LWREKDGSEW FSGGWLARPS EIQHDCGRTF YVREVFAVDQ
PDQTRRIEDI QSHCAVLTPK EFVKERPTEI PECDVFVCES RVPGVSFAKG EPSSLFTKPS
EKVCNSILIS SVFLSTFSGL MSNWLAAQPK LTAKSKSGYI LFSAEIRKRI MHENPDSGFG
EVSKIVGIEW KKLSDDQKRQ YEVRAEYIAS ERAKQEAARA ATEKTLQPGQ IRIYQCKWIN
CDSQFDSENG LYEHIVQHHT SQIIMDSEQQ YVCMWVTCVR NRKDGKPFPS LPRLHRHMKE
KHLATAMKSV YANQIGKNFF KLSTQSTPNG ETVFDHPVSD GSLQFNSNIL ATNAATTSTS
YCSNAFASRS SSYAFMLTRT HGNSLHNICL GSPLTVLCTF QPSSSMAVPT ITDAGRTVVK
SQGVDPVFVA PPSSVHARRV LHSETYLRYI ESLSSNRQRT VSKWDTSLST NPRNAQPNAA
RPPPTHWIRE SRGRPIAREE DVVRALWRLR DELLESTCNM SVERDVGGIL
//
