ID A0A251S980_HELAN Unreviewed; 1064 AA.
AC A0A251S980;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative zinc finger, ZZ-type, JmjC domain protein {ECO:0000313|EMBL:OTF95394.1};
GN ORFNames=HannXRQ_Chr15g0482601 {ECO:0000313|EMBL:OTF95394.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTF95394.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM007904; OTF95394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251S980; -.
DR InParanoid; A0A251S980; -.
DR OMA; IELEFVW; -.
DR Proteomes; UP000215914; Chromosome 15.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549:SF11; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLASE 2, ISOFORM A; 1.
DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000215914}.
FT DOMAIN 684..1002
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1064 AA; 121597 MW; 4983ACD386D02D98 CRC64;
MATTVTNNDD HELDDSRSDS DAEEQKPRVL KAKNGAKKKS KPKKEVDSSE DEEEDAHMSP
ETGTVTNNDN HELDDSRSDS DAEERKPRVL KAKNGAKKKS KPKKEVDSKV DSSEEEEEEE
HMSPETGAVD NKDLNNVEET EIGCRRSSRS NRNKNPVYNH FLNFDDFKSP RKKRNIKKTE
EGGEEEKKEP KRPRCAAKHK KPDENGVLQY VESVMCHQCQ RNDKGRVVRC QKCGSKRYCV
PCMTTWYPNM SEEDFAKCCP VCLDNCNCKG CLRDVHPKVK NKIDFKPSSD QKVQYSIYIL
HVLLPFLKRL NEEQAKEKTI EAEIQGCALS DVKLTAVNCH LDERMYCDLC KTSIFDLHRS
CPSCNNYDLC LQCCWELRDG NLQGNKEVIN LTNFENPGAG YLHGSEEVKE DEAHEKSHTI
RKTRSSLKDN ISSKEDISPK EDISPKENTS PNENTKPDWK SFADGRIPCP PESMGGCGHG
ILQLTHIKPL DKIPTLLKDT QELLRDHKLE DDMRKMPEEW CTCSDLVNES DAGAMQLRKA
ASREHSNDNY LYCPRAVDIE PGDLKHFQWH WSKGQPVIVS NVLETTLGLS WEPMVMWRAF
RQISNLNHDQ LLDVAALNCL DWCEYDVNVH QFFKWYTEGK YDNEGWPEII KLKDWPPSSL
FEERLPRHGV EFITCLPFKE YTHPRDGYLN LAVKFPKKAL KPDMGPKTYI AYGVAQELGR
GDSVTKLHCD MSDAVNVLTH TATVTPDSEQ TKKINNLKEK HKAQDQKEIF GINVANAKDA
IADNGVESKV EGNTCDADVE RDQTAPSTSN HSNEIPLKNE ECDEAECSND KVQETDVKGK
SHPKRGRKPN KNAEKKLKCV KLEKFDSPHG QRVSNNDTCV DGFDLEGGAL WDIFRREDTP
KLEAYVKKHF REFRHIYCRP LQQVIHPIHD QTFYLTMEHK RKLKEEFGIE PWTFVQKLGD
AVFIPAGCAH QVRNLKSCIK VALDFVSPEN VGDCIQLTED FRVLPKDHRA KEDKLEVKKM
ALYAVEAAIH DLNCPKETIE ESEPEKPKTA KKKPAGRRKK TKKT
//
