ID A0A559M8B8_9HELO Unreviewed; 1180 AA.
AC A0A559M8B8;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Peregrin {ECO:0000313|EMBL:TVY89205.1};
GN Name=Brpf1 {ECO:0000313|EMBL:TVY89205.1};
GN ORFNames=LAWI1_G006602 {ECO:0000313|EMBL:TVY89205.1};
OS Lachnellula willkommii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Lachnaceae; Lachnellula.
OX NCBI_TaxID=215461 {ECO:0000313|EMBL:TVY89205.1, ECO:0000313|Proteomes:UP000315522};
RN [1] {ECO:0000313|EMBL:TVY89205.1, ECO:0000313|Proteomes:UP000315522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 172.35 {ECO:0000313|EMBL:TVY89205.1,
RC ECO:0000313|Proteomes:UP000315522};
RA Giroux E., Bilodeau G.;
RT "Genome sequencing and assembly of the regulated plant pathogen Lachnellula
RT willkommii and related sister species for the development of diagnostic
RT species identification markers.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:TVY89205.1}.
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DR EMBL; QGML01001363; TVY89205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A559M8B8; -.
DR Proteomes; UP000315522; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15670; ePHD_BRPF; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
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; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000315522};
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 448..498
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 502..621
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 794..825
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1180 AA; 129153 MW; A09546BA13EAFF5C CRC64;
MTPAPATPRR PASSRVRSSR PRASTTAPRS DKPAPVASSE PPKKKLRYIP GGPGGGGRYV
DDQGIEIPVG GTGPGGYNYV GPRGRIGREN AAMGLVPQVF PRRDRSTRTR TVLPRSQQPP
MRFSSAAQAA AVVQSDGYKP REERAWEEFH PNLDIEGALR AFTINEVQGI PESRPVTPGP
PSAEGSIPSA TVAETPNGVE GFKAKSEGIP TPAASLNGES TLKIAIPGTP GGGKRRPGRP
PKDPVAFYSA KAAKMGVPFI GTPKTPKIVA PVQNINAKEK LTLPQPSYRK TDTLARFEDK
ALGLVRYVDK SMANVGYQET DVFIRPEHKL IKVSDTSMEE DLDLGPGHKS EGDGIIALGS
GGVGRVEYDM DEQDDKWLEE YNAERKAINF EPITREIFEI TITKVEKEWH ALEKRIPKPN
PKPPQTHRPR SSSAAAVNGE PQPGEEQDSK CAICDDGDCE NTNAIVFCDG CDLAVHQECY
GVPFIPEGQW LCRKCQLIGR GIPTCIFCPN TDGAFKQTNA SKWSHLICAM WIPEVSLGNH
TFMEPVMDVE KVPKTRWRLT CYLCNQRMGA CIQCGNKNCY QAFHVTCARR AHLFLKMKNN
HGTLAVLDGN AVLKAFCDKH CPSDYTKEND VARATREARA FYKKSMRGRL WADSQASALT
MAANHRHAVT EHQPDESQLT GAKVAQSLSE GKKKGNQPAK PIWKLPSGAP VIPQVVFNSV
ESSLQRFNIR KRKEYAADAC RYWTLKREAR RGAALLKRLQ LQMETFSSME ITRRNFAGMG
HAGRPRLNRR IEFAQSLIQD MERLKALAED VMKREREKLR SVELEEEVVD TVYFPVAKMF
PPMIDKAIML DIKMVFTDGL LKLKKKVNDR FYTTAMGFAH DICNIFHSGV VTQPSPDAEI
VLSSEIKKPV VTDIKERKKL GKRIVKAIQP QLQMAVRAEA DISGKSADDL LKELDQLLDA
SVQPTGDTIS VSVGDSHSLA DAEAKHERDV DMADGVEHST HENESANGSQ KQLNNGSEDV
EMQDADAPGE VDEGIGSTEE TDKALIEVDG NVSPTKVEHV NGVKNSNKPD TNGTAKPHQP
PTPPLSNGDA STDPADPLVN GGIFWYLKGF HPEGTSIIQE LGSGKDAVSQ LSEDLSDMDD
EALKGLGIDV DEGGDGIVAA VAGIPKPKAK AKARKKKSRR
//
