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Database: UniProt
Entry: A0A0S3SGR1_PHAAN
LinkDB: A0A0S3SGR1_PHAAN
Original site: A0A0S3SGR1_PHAAN 
ID   A0A0S3SGR1_PHAAN        Unreviewed;      1617 AA.
AC   A0A0S3SGR1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=Vigan.07G069200 {ECO:0000313|EMBL:BAT92034.1};
GN   ORFNames=VIGAN_07069200 {ECO:0000313|EMBL:BAT92034.1};
OS   Vigna angularis var. angularis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT92034.1, ECO:0000313|Proteomes:UP000291084};
RN   [1] {ECO:0000313|EMBL:BAT92034.1, ECO:0000313|Proteomes:UP000291084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX   PubMed=26616024; DOI=10.1038/srep16780;
RA   Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA   Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA   Tomooka N.;
RT   "The power of single molecule real-time sequencing technology in the de
RT   novo assembly of a eukaryotic genome.";
RL   Sci. Rep. 5:16780-16780(2015).
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DR   EMBL; AP015040; BAT92034.1; -; Genomic_DNA.
DR   Proteomes; UP000291084; Chromosome 7.
DR   GO; GO:0000785; C:chromatin; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15532; PHD2_CHD_II; 1.
DR   CDD; cd15489; PHD_SF; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR018501; DDT_dom.
DR   InterPro; IPR047365; Tudor_AtPTM-like.
DR   InterPro; IPR028942; WHIM1_dom.
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; PTHR46508:SF10; DNA-BINDING AND ZINC-FINGER PROTEIN; 1.
DR   PANTHER; PTHR46508; PHD FINGER FAMILY PROTEIN; 1.
DR   Pfam; PF02791; DDT; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF21743; PTM_DIR17_Tudor; 1.
DR   Pfam; PF15612; WHIM1; 1.
DR   SMART; SM00571; DDT; 1.
DR   SMART; SM00249; PHD; 4.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   PROSITE; PS50827; DDT; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          176..236
FT                   /note="DDT"
FT                   /evidence="ECO:0000259|PROSITE:PS50827"
FT   DOMAIN          380..427
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1219..1242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1364..1385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1617 AA;  181282 MW;  0239021B71C798A3 CRC64;
     MEPPVVRSRG RPRKRRREED GTVAGDPKTF PEAKKAPPVA LVGRYVLKEF RGNTVLLGKV
     VRYESGLYRV VYESGGFEDL DSIAIRRILL LDSYFDDDLI RRKGELEESV LPKIAEVRER
     GSSELHGDLL VESEEERDET DDESCSEARD LSSDSETPIP SAPTLPPSSG TIGVPESCVL
     NLLSVYGFLR SFSIRLFLSP FTLDEFVGAL NCKVSNTLLD AIHISLMRVL RRHLENISPD
     GSRRATKCLR CIDWSLLDAL TWPVFTFQYL AIYGYTKGPE WKGFYNEIFH GEYYLLSASR
     KLMILQILCD DVLASEEFKA EMNMREESEV GIDYDNEDSL PTEIGPRRVH PRYSKTTACK
     DSETKKYVSE LNAEDVDGNG DECRLCGMDG TLLCCDGCPA VYHSRCIGVM KMHIPDGEWY
     CPECKINMIG PSIARGTSLK GAEVFGKDLY GQVFMGTCDH LLVLDVNRDE FCLKYYNQND
     IPEVLQVLTA SEQLRPIYNG ICMAMLEYWK IPENFLSICV TSVPKVNLTN SNTDVLLSPM
     IEEKNQAVSS VKAEYSLTFS NGICSDNLEP SLDASLVTSC GPAPGSRYNT RTTVNLKLCE
     ETAMNSTFSI VNHQFNPKFE NSVNKSTAVS PAKCTFVNNQ FNNYGHTNDS RLPMNLSLQS
     KGDQSGFGKC KGSLTKDFMY TGFSYKPQSY INCYMHGDFA ASAAANLAVL SSEDSRSEGH
     VSDNLGKATS GNTYLLAKAF SQTASRFFWP SSEKKLIEVP RERCGWCLSC KALISSKKGC
     MLNHAALSAT KNAMKILSGL APVRIGEGII PSIATYVIYM EESLRGLIVG PFISECYRRH
     WRKQVERATS FSDIKPLLLK LEENIRTIAF CGDWVKLMDD WLAEFSTIQS AAVTLGTTQK
     GATCGRRKKQ LSINKVTAGA CPQNFVWWHG GKFSKSVFQK AVLPKTMARK AARQGGSRKI
     SGILYADGSE IPKRSRQVVW RAAVQISRNA TQLALQVRYL DFHIRWNDLI RPEHNLLDVK
     GQDTEASAFR NANIHEKRIV EGKILYRVAF GSQKHLPSRV MKHVEVERGP EGKEKFWFSE
     KRIPLYLVKE YEMRNGKMLS DKEYMYITSQ LHKRQLKATY KDIFFYLTCK RDKLNMLSCS
     VCQLGVLIGN ALKCSACQGY CHTGCSVSST VSTCEEVEFL ATCKQCHHAK LLTQKESCNE
     SPTSPLLLEG QEQSTSAVLK GSGPKCDGQE LMSSRTKNSR SDTKRFASDF SLETKGRSRN
     CSWGIIWKKK NNEDTGFDFR LKNILLKGGS GLPQLEPVCR LCQKPYNSDL MYICCETCKH
     WYHAEAVELE ESRLFDVLGF KCCKCRRIKS PVCPFSDLSY RTQEDKRSSR ASKKDYFGGD
     SDSGTPIDRS TCEPATPICP AVDFSRQDND PLLFSLSSVE LLAEPELDAN CVGNTVSGPG
     LPKISKRERE NNGSFRGNLH AEFSTSNEML SKSVKDLSPS VEDASANCSL LKDPEIVNYH
     EFVDFEPHTY FSLTELLHSD ENIQSEEADA SRVFSGCLKN SSCVPEGCGT VNLASNCEPT
     NLLQGNVYSC QQCSQKEPLP DLHCEICRIW IHRQCSPWVE SPSRLASWRC GDCREWR
//
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