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Database: UniProt
Entry: A0A5P1EKX1_ASPOF
LinkDB: A0A5P1EKX1_ASPOF
Original site: A0A5P1EKX1_ASPOF 
ID   A0A5P1EKX1_ASPOF        Unreviewed;      1356 AA.
AC   A0A5P1EKX1;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A4U43_C07F37130 {ECO:0000313|EMBL:ONK65439.1};
OS   Asparagus officinalis (Garden asparagus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC   Asparagoideae; Asparagus.
OX   NCBI_TaxID=4686 {ECO:0000313|EMBL:ONK65439.1, ECO:0000313|Proteomes:UP000243459};
RN   [1] {ECO:0000313|Proteomes:UP000243459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DH0086 {ECO:0000313|Proteomes:UP000243459};
RX   PubMed=29093472; DOI=10.1038/s41467-017-01064-8;
RA   Harkess A., Zhou J., Xu C., Bowers J.E., Van der Hulst R., Ayyampalayam S.,
RA   Mercati F., Riccardi P., McKain M.R., Kakrana A., Tang H., Ray J.,
RA   Groenendijk J., Arikit S., Mathioni S.M., Nakano M., Shan H.,
RA   Telgmann-Rauber A., Kanno A., Yue Z., Chen H., Li W., Chen Y., Xu X.,
RA   Zhang Y., Luo S., Chen H., Gao J., Mao Z., Pires J.C., Luo M., Kudrna D.,
RA   Wing R.A., Meyers B.C., Yi K., Kong H., Lavrijsen P., Sunseri F.,
RA   Falavigna A., Ye Y., Leebens-Mack J.H., Chen G.;
RT   "The asparagus genome sheds light on the origin and evolution of a young Y
RT   chromosome.";
RL   Nat. Commun. 8:1279-1279(2017).
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DR   EMBL; CM007387; ONK65439.1; -; Genomic_DNA.
DR   EnsemblPlants; ONK65439; ONK65439; A4U43_C07F37130.
DR   Gramene; ONK65439; ONK65439; A4U43_C07F37130.
DR   OMA; WCKDLES; -.
DR   OrthoDB; 1058151at2759; -.
DR   Proteomes; UP000243459; Chromosome 7.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15571; ePHD; 2.
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; 2.
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; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243459};
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          146..197
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          210..331
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          951..1000
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1020..1131
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          56..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1247..1297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1247..1270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1274..1288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1356 AA;  149734 MW;  01E09F687304A373 CRC64;
     MEVYFRPITE ADIESLRPRG LLDSLDSCFS IPVLDSSLEL EKKDAIFSGS EVGVSSEVVK
     EEEEEEKPME IDSVGGLSTA ETSTLPIPEV KEEDANEDES SSMNWVLGSK HRAILTTLRP
     TKKRKLLGSD AGLDQLLILP HSEQGSARCH VCCLGESGGK SNKIISCSSC GALVHKKCYG
     ILEAVVEKWV CSWCKHVEET WDDKRGNEGL RPCILCPKEG GALKPVGGDL NNEGKKKFAH
     LFCSLWTPHV YVEDTKTMEP VVNIVDVTEM KTKMVCNVCK VKHGVCVRCS SGTCRTAFHP
     YCAREARHLM EIWGKFGCDN VELRAFCSKH STSQDVDSVL RTRNVTRTAG DDFLGAKPPS
     ATVLPNKPLK LRLSCKVKEE NVTQAEVASS ISSEVIKNEA TTEEDGSSMN LSAENGDMQS
     SKNIDFEVNE AENSLSDSPT LIPFVKKLIA QGEYVVGDIA SAIGISPDSL ETALMGEISS
     FPSDLRPKIA KWFQGNAYVS AGIRHLKFWN GSAISSGSLA ARVDCPKVAN ASGLDTPDNI
     IVPDPENADA HSVKSMLSHK RAKNSNGVLK KDKLVVTSEE KIQPDSNEEL VDEIGQDTVV
     HTNDGAKDPA GNISPIVDQS QCKDQDRLKT LIEDACSLPS SGPLVLPPEV EGNLATVEKN
     ELSETQHKPE CATESVLSEK LDEDQANEID VPQDGAVKKI RIDGSCSSYI HPYIQERLME
     VQKSVLPELE RREYKLNGQV KDRILSSNAS DSCNQDLLSP VCKHVDHVPD HGQFDHLAQV
     NKIGMLELSP EDEVEGEMLY LQNKLLDSAS AIKHGFDDLL GRVVQQLPHE LEVLKKHRWD
     MVLVNQFLRD VKELKKRGRK ERRHQEAQAV LAAAAAVAAS SSRNPLPRKD GSDEIGFLPQ
     SPQNVSGLPG RSGQPLPRSR LKEATRSAII KVSPDKHSGG LQSPEFPKDN ALSCDICRRP
     ETLLNRIFVC SSCKVAVHLD CYRKFKDPVG PWKCELCEEM LHSGSPRNQT VENRDRSCLV
     IECGLCGGGY GAFRKATNGQ WVHAFCAEWM LESTFRRGQQ NLVDGMDVIS KATDVLTCSI
     CQQKFGICSK CSYGHCQVTF HPSCARAAGF YMNVKAVGGR LHHKAYCEKH SVEQRQKADT
     QHGAEELKGI KQIRFELEKV RILCERIVKR EKIKRELVLC SHDILASRRD YVAYSALMRS
     SLCPPGISSE SATTSIDNRS YSGIIQRSED VTVDSTISGK RIKRSLDVDR KTDESSTSRP
     SFKRKAPDRT SYSGKQLPHR TQSVSFRNST DDGEKRFKAK KQAETFHKEI VMTSLQASMQ
     NQRLPKGFVY VPVGCLSKEK PVVDDPESHE PEEPGG
//
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