ID A0A0S3SCG0_PHAAN Unreviewed; 1730 AA.
AC A0A0S3SCG0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Vigan.06G172800 {ECO:0000313|EMBL:BAT90474.1};
GN ORFNames=VIGAN_06172800 {ECO:0000313|EMBL:BAT90474.1};
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:BAT90474.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT90474.1, 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; AP015039; BAT90474.1; -; Genomic_DNA.
DR Proteomes; UP000291084; Chromosome 6.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd20401; Tudor_AtPTM-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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; PHD FINGER FAMILY PROTEIN; 1.
DR PANTHER; PTHR46508:SF1; 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; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
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 195..255
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 418..465
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1197..1227
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1730 AA; 192676 MW; AF5E91C9E76E2B9F CRC64;
MEAPVARPRG RPRKRRRNDE ENENEAKKLA SMGTRPPVAL LGRFVLKNFP RNGVFLGKVV
YYESGLYRVC YEDGDSEDLD SGEVRSILVK EGGINGDLAG RKEKLEELVS KNGGKIGIGS
QKGPVESIKE ESKAGVCELN DGGLMIEKDE EDDDEDVNSL SDSGTGLGMD SGSEAETLPP
PPELPVSSGT IGVPEQCVSL VFSVYGFLRS FSIRLFLQPF TLDEFIGALN YQVTNSLFDA
IHLSLMRVLR QHLEFRSSEG SERASRCLRC NEWSLLDPVT WPVFLIQYLV VSGRTYSHEW
KTFYQEVSTV EYYVLPVSRK LMILQILCDD VLESEDILNE MNIRRESEVG IDDDGEDILP
TEVGLRRVEP RYTFTSASED KEATKLVSAS NAVNQPGSVI SYSRGTESTE DGDVDRNGDE
CRLCGMDGIL LCCDGCPSAY HSRCIGVLKN HIPEGPWYCP ECKINMLGPT IAKGTSLRGA
EIFGKDLYGQ LFMGTCEHLL VLNIGNAESC LRYYNQNDIP KVLQVLYASL QYRPIYHDIC
MAVLQYWSVP ESLLFHSVSS GANVNSANIK EETKPSPFLL PPVGEGNLMK EEYPLTSAST
AYCDNLVPSL DASSVSTPSS ALQCNGNGSS SEYPVVTTKL PESSRIESIL SADSASVSVS
HHSNIKHGNF DGRPTEVDPG KCSSVHGQFS YYGHANHTGF PINISFQTKE NTQASFEKCE
RNVTNGFAYM GFSYKPFSYM NYYIHGEFAA SAAAKFALLS SEESRSEGHV SDNQRKLASG
NTYLQAKAFS LTASRFFWPS SEKKPVEVPR ERCGWCISCK APASSKRGCM LNHAALSATK
SATKVLAGFS PIKSAEGVLP SIATYIMYME ECLRGLVVGP FLSSIYRRQW RTRVEQASTF
SAIKPLLLEL EENIRSISFC GDWVKLMDDW LVEFSMVQSA TSTLGTAQKR APSGRRYKKR
SAIDEATTEG RPENFVWWRG GKFTKFIFQK AILPKSMVRK AAREGGSRKI SAISYADGIE
IPKRSRQLVW RAAVQMSRNA SQLALQVRYL DFYLRWSDLI RPEQNIQDGK GQETEASAFR
NANICDTKLV EGKNCYGIVF GSQKHLPSRV MKNVFEIEQD PKGKEKYWFS EARIPLYLVK
EYEEGKGNMA YNEEQHLNTA SGLHRKRLKT ICKDIFFYLT CKRDNLDVES CSVCQMGVLI
RDATKCNACQ GYCHEGCSTS QIVSANEVEY LTTCNQCYHA RLLAQKENSN ESPTSPLLLR
GRENNSGTVL KRSRPRTLDQ VPKSSKTKAN NPMKQVTSAT SLKKTKAKRS EQEPTTGIND
NHLDMQQVAS VETSAAKRHR KNCSWGIIWK KKHNEDSDDF MLRNILLKGS SNIPGLKPVC
HLCRKPYTSD LMYICCETCQ NWYHAEAVEL EESKLSSVLS FKCCKCRRIK SPVCPYSDLK
PKKQEGKRSR TKAKKEHSGA DTDSGAISDM RESEAATPVF PVYDDTPTYS AEDPSYVFPD
EDPTPVFPVE DDPLFFSLTS VELVTEPKIE GDMEWNGVSV PGLQKLPVRR NVKNEGDDVS
FEGGVPLDAE FSTYDGETGN LSNPAEESIP LEYTSGVDLD NKLPNDSENV NYDDYMDFEP
HTYFSVTELL QSDDGGQFEG VDMSEDLSGY MENSSTTTLI PESCDASLAD KSAPTTYTGH
SCMQCSQMEP APDLCCEICG ILIHSQCSPW VELPSLGSWR CGHCREYGNN
//