ID A0A175YDB2_DAUCS Unreviewed; 958 AA.
AC A0A175YDB2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Histone-lysine N-methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DCAR_029056 {ECO:0000313|EMBL:KZM81443.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM81443.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM81443.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM81443.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM81443.1}.
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DR EMBL; LNRQ01000009; KZM81443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175YDB2; -.
DR STRING; 79200.A0A175YDB2; -.
DR EnsemblPlants; KZM81443; KZM81443; DCAR_029056.
DR Gramene; KZM81443; KZM81443; DCAR_029056.
DR OMA; LAGHAMW; -.
DR Proteomes; UP000077755; Chromosome 9.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:UniProt.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd20142; PWWP_AtATX1-like; 1.
DR CDD; cd10518; SET_SETD1-like; 1.
DR CDD; cd20404; Tudor_Agenet_AtEML-like; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 3.30.160.360; -; 2.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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:SF140; HISTONE-LYSINE N-METHYLTRANSFERASE ATX2; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF05965; FYRC; 2.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00293; PWWP; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 144..207
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 544..595
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 600..648
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 803..921
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 927..943
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
SQ SEQUENCE 958 AA; 108409 MW; DF53850AA106387C CRC64;
MSNVKDIHGM ARDSVKYIPL HEEYMATAPL VNSNGASKKR KIPERNIDKK DVGDVYWPLD
DDWYCGRILG YNLSTERYHV KYNDGVEEHL CLSFERILFY VSPEEIQQRK LCCVQHPDVD
SHDIDNMVSL AASLNHCSRV DPIPGDMIWA KVTGHPMWPA IVLDESACSN LKILNKISGE
RSVLVQFFGT HDFARLSKKQ VTSFIKGLLS ELHRKSKTSD FLRSLIEAKT YLSTEKLPSR
MLSLQSSNAA NFESASGEED CTRDEEIPKN VIFRSCPFDI GGLQIISLGK IVKDSELLYD
RKYICPEGYT AVRKLPSISD PKKCISYTME VLRDGNTLNK PLFRVTSEKG EQFEGPTSSS
CWDKLYRKIR KLHGHDALKA FGEDNKIVRS GPAMFGFSHP KIKELIRLSS TCGSPLDSSK
LTSRRCRDPA IGYRRIHITW KDLDKCNVCY TDEFEGPTSS SCWDKLYRKI RKLHGHDALK
AFGEDNKIVR SGPAMFGFSH PKIKELIRLS STCGSPLDSS KLTSRRCRDP AIGYRRIHIT
WKDLDKCNVC YTDEEYDISP FLQCDNCRMM VHTSCYGELE PADGTLWYCN LCRVGAPESP
PPCCLCPLAG GAMKPTTDGR WAHLACAISI PETCLLDVRK MEPIDGLNRI NKCSNSSCYV
AYHPLCARAA GYFLEFYEED GLRLCSEKED EKDQCIRLRS YCKRHRRPSD KCIVVQESMG
TCQRPDYIPS PNPSGCARTG RKQPQSHEPA SLKHLYLENV PYLVGGIRQH EFLSKVVSSQ
CNISSNISSM VEKYSHMKET FRRRLTFGKS GIHGYGIFAK QPHRAGDMVI EYTGEVVRVN
VADRREHLTY DSLVGAGTCM FKIDDDRVID ATKAGNIARL INHSCEPNCY SRIITVNGDQ
HVIIYAKRDL NQWEELTINY RLSSVDEQLA CSCGVSRCRG IVNDIKAVEQ VAKPCIPQ
//
