ID A0A067GUU7_CITSI Unreviewed; 1724 AA.
AC A0A067GUU7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=CISIN_1g000127mg {ECO:0000313|EMBL:KDO82475.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO82475.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO82475.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK784875; KDO82475.1; -; Genomic_DNA.
DR Proteomes; UP000027120; Unassembled WGS sequence.
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; cd15519; PHD1_Lid2p_like; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_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; PTHR47162:SF12; BINDING PROTEIN, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR47162; OS02G0192300 PROTEIN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 751..801
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1045..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1675..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1675..1689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1724 AA; 193409 MW; 5C9E3D83A420EA7B CRC64;
MILSDDSPPH LGNDNLSDFG IDREQACKSQ TINETKSDCL SKIAGRPTSD YIVLDDDIGE
FLVEGRSSAS VWRMVSQTLV HACRKIYEQT GVCKFRCRHD VFKIWSSYFV SVSEEATESS
DSLSKFCCLS GPVNIPHLIR SNDELETSCK ALVKWLDQDR FGLDVEFVQE IVEQLPRVRV
CAEYTFLDKR RDWSTSQTVR SGFLRVRRKS NTYEKAADRH VFEGCQRPRG QVLENPVMKS
YFPPGKPLSS KLPIELIGDV IQSWELLWRF SEVLGLEEPL SFKELEEELR NGSAFTLRSS
STSTVAQEIG QAFIAEEMES LREAAHVRLA SNTSSGHANV GLANVLCSLL ILLLGELQSK
VAVLGDTSFD GTESKSRRRR KKDAENLMFA KKIMLDLLPV NVLTWPELAR RYLLTVSSIE
GNLDTVDFLN HESCKALNCF QGDSGTIRSS RPGVAGMEAD ALLLAEATKR IFGSLKNTSG
PLSVHYNDSD AVGAHETVKV NNSGIPGWAQ VLEPVRKLPT NVGARIRKCI YDALDKDPPE
WARKRLEHSI SKEVYKGNAS GPTKKAVLSV LADVCGEDQP QKPTRKRKNR CFTSVPDVIM
KQCRKVLRCA AAADEERVFC NLLGRTLLNT SDNDDEGLLG FPAMVSRPLD FRTIDLRLAF
GAYGGSHEAF LEDVREVWHH ICTAYSDQSD LLQLAGKLCQ NFEVLYKKEV LTLVQKFADY
PSLECLNSEA KKEMEDILES ASEIPKAPWD EGVCKVCGID KDDDNVLLCD TCDSGYHTYC
LTPPLTRVPE GNWYCPPCLS GNCKNKYMSQ VPHVSSRIPK RRHQGEFTCR ILEEVFHLAA
TMEMRDYWDY SDKERIFLLK FLCDELLNST NIREHLERCA SVSVDLQQKI RSLSLEWRNL
KFREEILAGK VARDKASVLS GTGKCGTEGV ATLYPHYGKL MRQPSGGGGY FSSFASDLAL
SEDGLQLNES RKLSFWFNSK GISMRQPSCS RNQIGEAPYT ESQVHQESEK DNIRVDDLQY
DVPHSASQPQ KQDTAGEYAT WRNKGQDLEN GHTSGPLQPN CEASQSHFSS DHTNGNQVAE
HLCVMPINPE NIVPGHHSIV QHDMNEPHAH DLKGSVLKNE IAVLQDSIAG LESQQLAVSL
RKELLGRDSA GRLYWAFFRP NTSPWLLVDG TTVLEQERIL KEHGDSLANS PFEEEYNGIS
TSSSWFSYQS DTEIEELIQW LSDSDPRDKE LAESILRWTK IGYKDLKIAG NHIEDESVPS
SSKRRKSEAT VKSSGLVTKA LTVLEEKHGP CLEPEVLKMS MKLDTNSELT CKERMYRCEC
LEPVLPTRFH CRRCHLSFSA RNELEEHNDA KCILSATSSQ NSKEDDERTK GAGTIRTETL
QAECMETAGK GMSQSLKHGT AMGSFEIPKE FACPFNFEEI STKFITKNSI KELVQEIGLI
GSNGVPAFVP STSPYLCDPS LKLVEMCKNE INRGNKSTNL ENLFQYSIAG DMVSGLEHDN
ISNNSSRRCT VSHNDDDVLK CRRLNPNFMN EKRDQSFNLR SLKPGIGNSS IVRDTSLMPL
MGRGIEILRQ LKINLLDMDA AVPEEALRSS KACWEKRSAW RAFVKSAKSI FEMVQATIVF
EDMIKTDYLR NGWWYWSSLS GAANIATVSA LALRLYTLDA AIVYEKHSDS IEIQEHISQP
DKETSPCKDS KSNPKPSKAI LKTQSSDLTE FSKTRSKSGK KRKD
//
