ID A0A0V1AC13_9BILA Unreviewed; 1146 AA.
AC A0A0V1AC13;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peregrin {ECO:0000313|EMBL:KRY22110.1};
GN Name=BRPF1 {ECO:0000313|EMBL:KRY22110.1};
GN ORFNames=T12_9901 {ECO:0000313|EMBL:KRY22110.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY22110.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY22110.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY22110.1};
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:KRY22110.1}.
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DR EMBL; JYDQ01000011; KRY22110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1AC13; -.
DR STRING; 990121.A0A0V1AC13; -.
DR Proteomes; UP000054783; 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.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 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:UP000054783};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 22..53
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 240..290
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 294..427
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 605..675
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1020..1087
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 837..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1146 AA; 129441 MW; F6DD5B75458EC694 CRC64;
MKLDHVTAYR LLSDLKGKGP PFVCPIDNCG NSYRSFSGIR YHFKHAVHET LDKKKTPLVC
KNPKEDVIEH QHDLHSIHEV DISGIDGKFK FPLASAVEKR ISFDSRSTPN SGRHHTPLKR
KDLLFTPKFE KAPKSKLEHL PHAECRPCEE APPKRSRRNF ILSKTYIKCR DVSYKDLIKD
VTYDLDEEDN LWLKLINDKR KSINLAPINK KLMEFVMDRL EKVSYFEVPS IGQGPPVDED
AVCCVCNDGD CENTNVILFC DMCNMPVHQE CYGVPYIPEG QWLCRRCQLS PARSVDCCLC
PNRAGAVKQT NDGRWAHVAC AMWIPEVQFA NLVFLEPIEV DVILLLFDYA ICLNEIPAAR
WKLVCYICKR RNVGACIQCQ VPTCYTAFHV TCGLGANLYM KVEPVVDPSV SAEEQVVRKI
SYCGVHTPNE VSNVSKVVEP VVVNEEAIDV LKESSKVVAR QARKVLAEKR SASYVGLLPV
IPTIRLIQIA NSVRMSADDI FFQRLVNFWM CKRYSRLGVP LLRGVQESFS TLAIYKKDAE
SENTETRKID RPTMLRELRN VSSVLGDFKK REILKKRMLL FEMERMHSVC FPIKLLLLDL
VNRLLAFDVE EVFAQPVSEE IVPGYRSIIS NPMDLGTMRK KVLQFEYMNV NEFMADFNLM
IANCLKFNRQ NRYYLRIGRR MDAFGKKEIA RALEEEKCLR KIASHCSEKD AFINDIKREL
GTCILRKRRS ENGANNDHSI ANAEITGNNN SVCDDQLSEV TFSTKLEENA AHFVSLLDET
ICAGGVNLEN TAADSTADND VSMIDASKHS PQLLLSANAL VNGQDASLDL PSAVVDRQQQ
HTGTGYRQND DHSKANENNS DSSEVKFSDQ EVKKRPGRPR KREASNPGWR PTRQKSLRIA
SALEASTTLN GTDEPSSTAQ TSTLLNSVLL ANSEAANYGL KEEEEEEEDH SIMLSSEMDA
NQILALNVDD VKGEVLSNHA EETSVLKMTN DDIPTSMDLQ HPSDEPVSDE PIADEFVFEM
LDLVWAKRST MPWFPGMIVD PDMPRTGFTG KLADIPSPPE DVLQLKPNDG SYLVMLFNSM
HTWNWLPKRC LKPLGLDISL DKKKVAEARK TLYRQSIAAA YKEAMKYRYL ILGQIVAGNK
QSKSAS
//
