ID A0A4U6WG26_SETVI Unreviewed; 1486 AA.
AC A0A4U6WG26;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SEVIR_1G340100v2 {ECO:0000313|EMBL:TKW41781.1};
OS Setaria viridis (Green bristlegrass) (Setaria italica subsp. viridis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4556 {ECO:0000313|EMBL:TKW41781.1, ECO:0000313|Proteomes:UP000298652};
RN [1] {ECO:0000313|EMBL:TKW41781.1, ECO:0000313|Proteomes:UP000298652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. A10 {ECO:0000313|Proteomes:UP000298652};
RA Huang P., Jenkins J., Grimwood J., Barry K., Healey A., Mamidi S.,
RA Sreedasyam A., Shu S., Feldman M., Wu J., Yu Y., Chen C., Johnson J.,
RA Rokhsar D., Baxter I., Schmutz J., Brutnell T., Kellogg E.;
RT "WGS assembly of Setaria viridis.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM016552; TKW41781.1; -; Genomic_DNA.
DR EnsemblPlants; TKW41781; TKW41781; SEVIR_1G340100v2.
DR Gramene; TKW41781; TKW41781; SEVIR_1G340100v2.
DR Proteomes; UP000298652; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 2.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
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:SF107; PHD FINGER FAMILY PROTEIN; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 2.
DR SMART; SM00249; PHD; 4.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51805; EPHD; 2.
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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000298652};
KW Transferase {ECO:0000256|ARBA:ARBA00022603};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 285..336
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 347..471
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 1157..1266
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 64..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1486 AA; 163825 MW; 432F1C95F44084AB CRC64;
MSGEMARAEV SPEGAAPGFG ADLYAQATKA LALRTPFEGE EAASRVPTLP ARLVSWAGPG
DARKKHKKIQ LPPPDDAAVE PPPPAAAKVG LWEQFEAYFR PVTLADVEML KPKLPFGYSK
LDSCMLIPFL GTGEELMNQG ETYDVAVFET SSYLGVGGAE VVSNRERGDQ SGHLLSQKEK
RDQNVDPDIH DVVVQQMVSD KDISRRSRVS IQPGGRPFEV DQAVSNGIVS AQCAEEEGSS
LNWLLGATGR FVLTSERPNK KRKLLGVAAG LEQLVLLPRL GAEKSSTCDV CCLGESSMDS
NRIVNCSNCK VSVHQKCYGL RVVPDGQWLC AWCTYLESNK DSGSTQPTPC VLCPKEKGAL
KPVKVEPTQS ADVSHLKFAH LFCSLWAPEV FVEDMESMEP VTNLDNVQEN RMKLTCSICK
IKHGACVRCS HGTCRAAFHP ICARESKHQM EIWGKSRHSN VELRAFCSKH SSVGYTSSVE
NSNHASEQSP TESGPNNTNL ITGKIPKLRF TRKNKDKFMN CETSASSSGN LIRVETTEQD
ALANTVRNAN AQPIRSRETG TGHPSVGGDR MRSPGDIAVV LRKLIDSGKV SVGDIASEVG
ISSESLEAAL VGETTTFSHG LMLKIINWLQ NSVHMHAVQG NACKRNSVVL QDDNSDGFDT
TDTIDMKISS VPDDDKDVFV DVSDSAVTEP TLRRTKSNSK ILEEDNATCA TGVTILQNGN
KNMVKDGADL ECSPAKEFAK ESTREFSPIG SKGVSKEEKG KLILNNTSGN NEFGTSMEIP
NENRGVLLGR KNDNLTEAGL GSGLKEGVSS PDHCFSQGDH ARDGENSIEN GFRTPRHCDS
NCSHGQPFFN FDDSHSYIHP FIKKKISHHW DITFNQNKEA LNHHEEPSCP SHEKIPVDSS
EEHEDATDTA ASDQVLKASS LEILEHAPDD EVEGEIVYLQ ARLLDNAVVL KHRYEKLIAK
VVQNISRELD AFSRRKWDLI FVNQFLRDVR EAKKRGRKEK RHKEAQAVLA AAAAAAASSS
RNSTMRKDAK EDAAPANQES SPKLVAGSSR VGQRTKDSSK SSNSKLPPDN KFGSFHMPIS
SNENALHCDV CMRTETLLNR IFICSRCKQA AVHIDCYRNL ENSIGPWKCE LCEDQDISLE
TPTTSDKLDC NGKKSPFARC GMCHGTSGAF RKTADGQWVH AFCAEWLLDT KYVRGQENPV
EGMESLVEGK DTCCLCLRKV GMCLRCSSGD CHITFHPTCA RNSGFYMNTK GFGTTSQHKA
YCGKHSAQQK EEDAQRYGLE ELRSMKRMRV ELEKLRLLCE RVIKREKVKR ETVLCDHDIL
AKTKDTVIFS YLACGASSES ATTSVNNRSY SGTAQRSDDV TVDSTLSRKK TIRFSLNSRD
AERNTADSSR TLISFKRKLS ERGLHAGKQL PQRPAITSQK LDDGEKKTND KKIEMFQKEL
VMTSDQASTQ NQRLPKGYVY VPRDSLSKER PWNRNTQPHT PQEPGG
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