ID A0A0V0WBY8_9BILA Unreviewed; 1125 AA.
AC A0A0V0WBY8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peregrin {ECO:0000313|EMBL:KRX73097.1};
GN Name=BRPF1 {ECO:0000313|EMBL:KRX73097.1};
GN ORFNames=T06_8624 {ECO:0000313|EMBL:KRX73097.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX73097.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX73097.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX73097.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX73097.1}.
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DR EMBL; JYDK01000186; KRX73097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WBY8; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15572; PHD_BRPF; 1.
DR CDD; cd05839; PWWP_BRPF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR013087; Znf_C2H2_type.
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; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 237..287
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 291..412
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 590..660
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1001..1068
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 824..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..873
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 127153 MW; B38DAE53E8BD6D11 CRC64;
MKLDHVTAYR LLSELKGKGP PFVCPIDKCS NSYRSISGIR YHFKHAVHET LDKKKTPLVC
KNPKEDVIEY QHDLHSIHEV DISGIDGKFK FQLASAVEKR ISFDSRSTPN SGRHHTPLKR
KDLLFTPKFE KAPKKHLPHA ECRPCEEAPP KRSRRNFILS KTYIKCRDVS YKDLIKDVTY
DLDEEDNLWL KLINDKRKSI NLAPINKKLM EFVMDRLEKV SYFEVPSIGQ GPPVDEDAVC
CVCNDGDCEN TNVILFCDMC NMPVHQECYG VPYIPEGQWL CRRCQLSPAR SVDCCLCPNR
AGAVKQTNDG RWAHVACAMW IPEVQFANLV FLEPIECLNE IPAARWKLVC YICKRRNVGA
CIQCQVPTCY TAFHVTCGLG ANLYMKVEPV VDPSVSAEEQ VVRKISYCGV HTPNEVSNVS
KVVEPVVVNE EAIDVLKESS KVVARQARKV LAEKRSASYV GLLPVIPTIR LIQIANSVRM
SADDIFFQRL VNFWMCKRYS RLGVPLLRGV QESFSTLAIY KKDAESENTE TRKIDRPTML
RELRNVSSVL GDFKKREILK KRMLLFEMER MHSVCFPIKL LLLDLVNRLL AFDVEEVFAQ
PVSEEIVPGY RSIISNPMDL GTMRKKVLQF EYMNVNEFMA DFNLMIANCL KFNRQNRYYL
RIGRRMDAFG KKEIARALEE EKCLRKIVSH CSEKDSFIRD IKRELGICIL RKRRSENDAN
NDHSIANAEI TGNNNSVCDD QLSEVTFSTK LEENATHFVS LLDETIRAGG VNLENTAVDS
TADNDVSMID ASKHSPQLLL SANALVNGQD ASLDLPSAVV DRQQQHTGTG YGQNDDHSKA
NENNSDSSGV KFSGQEVKRR RGRPRKRVAS NRGWRQTRQK SLRIASALEA STTLNGTDEP
SSTAQTSTPL NSVLLANSEA ANYGLKEEED HSVMLSSEMD ANQILALNVD DVKGEDLSNH
AEETSVLKMT NDDIPTSMDL QHPSDEPVSD EPIADEFVFE MLDLVWAKRS TMPWFPGMIV
DPDMPRTGFT GKLADIPSPP EDVLQLKPND GSYLVMLFNS MHTWNWLPKR CLKPLGLDIS
LDKKKVAEAR KTLYRQSIAA AYKEAMKYLI LGQIVAGNKQ SKSAS
//
