ID W5LWP0_LEPOC Unreviewed; 1628 AA.
AC W5LWP0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=PHD and ring finger domains 1 {ECO:0000313|Ensembl:ENSLOCP00000000547.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000000547.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000000547.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01008072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000000547; -.
DR Ensembl; ENSLOCT00000000548.1; ENSLOCP00000000547.1; ENSLOCG00000000493.1.
DR eggNOG; KOG0825; Eukaryota.
DR GeneTree; ENSGT00950000183205; -.
DR HOGENOM; CLU_003222_0_0_1; -.
DR InParanoid; W5LWP0; -.
DR OMA; VPGYLMS; -.
DR Proteomes; UP000018468; Linkage group LG27.
DR Bgee; ENSLOCG00000000493; Expressed in muscle tissue and 13 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16635; mRING-HC-C3HC3D_PHRF1; 1.
DR CDD; cd15536; PHD_PHRF1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR047157; PHRF1-like.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12618; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR12618:SF20; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 102..143
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 179..229
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..376
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1122
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1628 AA; 179498 MW; 7E3D2848B7792E9C CRC64;
MDDDDSQNQM INRNASLGKG KRQAVFVLTD EDEPSDEEGE DSEEEETDSE EEDDEENGAN
ADEDEAGDSD EPEDNEKELE GAIGGSSSGL GYVSSDEDAD KCPICLNTFQ DQAVGTPENC
EHFFCLDCIL EWSRNANSCP VDRLVYKNIC LRSCYGGKIQ RKIPIQTTAK TSEQEVDEQT
NCEVCGRSDR EDRLLLCDGC DAGYHMECLV PPLDAVPVEE WFCPECAVNN PSQAQEEDVN
EDEVAVLMAD VVPSTSRLRA TTGQTRAIAR TRQSERVRAN VNRNRISQAR NMQHVPRHLM
ESSLLEETID AVVAGLNTAV YVRPLTPRAG TTRRRRTVKR RGTKSKKPRS KTAGGTRTKG
TKRRRRRLKK QRSRRKVQLP KEPTARARIA KSLGMGKPIR GSSIPSVYRP VDPSLGAMRA
DIGAASLSVY GDPFDLDPFD DGNEATEQPS SPLSPFEVKR RGLSQSALKS HQPVARPVSI
ELRRRALSIP EAEVITEAAP VPDLLGSILS GQSLLMMDSA DVVINRDGSL KAIKPDFILL
YSSYLDTEVS ATWSTCSKTS AFSSSGDNEL PSSSSPCNIP EGSASFCLFA SNGSLSPPVS
PKPQVQLGSQ SHNVRSATSG SSSIRLLTSA VPQPNPLASL TAPGGSLRNG NSGPCSLNYR
GSNSDPCSRS TIVPARKVPL RPVRVDVSEL PRIPKIKRED MGISQPRDGN SSGIPDSCMN
NLTGNGGRQQ TVGQRDVRSN QNRTDRSEGQ RQSQGGSSSS SSYSCSSGSS ETRPSSTVSF
RISASGNSWH GRRLAHGGVF GTSLKPTGDE PWEIHSKAVQ PEKREKAVKS EIYDPFDPTG
SDSSSSESAS DIFLNTSSET EKMSHSIQDS TSREQELPSS SWNFLEVKTE RVHGDTDEKE
DVEPNFEQRS KILITEPLSD GEHGASAGGG IDTTHKTLEL KKRLPQKDAH SRSNSPASTH
SEKKIKLETK SEAKDHKSRS NSRSELYPHS SSDGKQSSKP EARLASDECC RSSSSETTKE
KSAIVKYREK NPLRSRERRW SHSHSGSSSP EISERWARKK RRSRSRSKDR RQSCSSSSER
AKKKNHKKER SCERYESKGS GSRQKDKKYR RSRSRSKERR KDRSRSRSTS RSKEARRSRS
KERQRQRSRS REKKSETCGK MSQSIERKGE RGSQKLGKIS VETLKESKDL KEKPAFIAPV
KDEPGVPKLV NESTPKGERK KIDECDLESK MDVVLEAKVK MEPTWPKEFG CSSCEDEFLG
SVKDEVFSAQ PISVDEHYKP KLVGTSENLP GAAFHETEPN KKENEEHSAD KVNIDYILHT
TDLIKHEVVE PIKVSAPAVD TVTAIKKDDA TIKPEVVPSP VTATSKSRAP VKRVTWNLQD
SDGPSAEKTG SKVSLFKPQQ SSKDGLCKAP ESRQALNQST LLFISCLMCV CNQTVSADFF
LKFLHLQDFA EPAPLDTSVH VGSLPYAPVV SESTAQYIMQ GNLATAGSAT SLTCPSSSDL
KAGVSEPGAQ VPSAQKDEPR APESVSDVDK SKNEKYIKKL HMQERAVEEV KLAIKPFYQK
RDITKEEYKD ILRKAVQKVC HSKSGEINPV KVANLVRAYV DKYKHARKHR KEAEGSRKDT
AMTKDPPS
//
