ID A0A5D2T757_GOSMU Unreviewed; 1060 AA.
AC A0A5D2T757;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Histone-lysine N-methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=E1A91_D10G147000v1 {ECO:0000313|EMBL:TYI61067.1};
OS Gossypium mustelinum (Cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=34275 {ECO:0000313|EMBL:TYI61067.1, ECO:0000313|Proteomes:UP000323597};
RN [1] {ECO:0000313|EMBL:TYI61067.1, ECO:0000313|Proteomes:UP000323597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1408120.09 {ECO:0000313|EMBL:TYI61067.1};
RA Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M.,
RA Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R.,
RA Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G.,
RA Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D.,
RA Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.;
RT "WGS assembly of Gossypium mustelinum.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Polycomblike family.
CC {ECO:0000256|ARBA:ARBA00008084}.
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DR EMBL; CM017658; TYI61067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D2T757; -.
DR Proteomes; UP000323597; Chromosome d10.
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:0010468; P:regulation of gene expression; 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; cd15662; ePHD_ATX1_2_like; 1.
DR CDD; cd15494; PHD_ATX1_2_like; 1.
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; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR041956; ATX1/2_ePHD.
DR InterPro; IPR042010; ATX1/2_PHD.
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; IPR002999; Tudor.
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; 1.
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; 2.
DR SMART; SM00293; PWWP; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
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 3: Inferred from homology;
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:UP000323597};
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 283..346
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 592..643
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 648..773
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 899..1014
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1020..1036
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
SQ SEQUENCE 1060 AA; 119744 MW; C7E2042BF80B9954 CRC64;
MAFPEKGDEE DADTPIRYVS LDRVYSSASV CVSATNSSNV MSKKVKARKL IVDNDHPLKT
HNPPVVHVYS RRLKRPRQCV SFYDSLLEGE SQKTAVKSEI DESLRKKRRI GSNELANLGV
DSSVLCQSDR PRLRDCRNNC SVNNNVNSNS VKKRKHNSTL NSQRSFTASA TAKKWVRLSF
DGVDPKAFIG LQCKVFWPLD ADWYLGRVVG YNLETNRHHV EYVDGDEEDL ILSNERLKFH
VSHEEMERLN LSFCVDSTKD DDHDYDEMVA LAASRDDCQE LEPGDIIWAK LTGHAMWPAI
VVDESLLGDR KGLSKISGGR SVPVQFFGTH DFARIKLKQV VSFLKGLLSS FHRKCKKPRF
SRGLEEARLF LCEQKLPRRM LQLQNGIVVD GGEASSEDEG GKDSIDDHLK KDQGIQITLG
GHGGSSYVIG GLQIINLGKV VKDSEYFQDD GIIWPEGYTA VRKFTSVKDP SVCTLYRMEV
LRDPQSKNHP LFRVTSDEEK FEGPDPSACW NMIYERIRKR QNDSSDCKAG KGRLFEPGAD
MFGFSNPEVT KLIQGLSKSR LSSKFSAFKL ASGRFRDLPA GYRPVRVDWK DLDKCSVCHM
DEEYENNLFL QCDKCRMMVH ARCYGELEPL DGILWLCNLC RPGAPESPPS CCLCPVIGGA
MKPTTDGRWA HLACAIWIPE TCLSDVKRME PIDGLNRISK DRWKLLCSIC GVSYGACIQC
SNPTCRVAYH PLCARAAGLC VELEDEDRLF LLSVDEDDED QCIRLLSFCK KHRQPSNDRV
ASDERFGRIA RRCSDYTPPL NPSGCARTEP YSHFGRRGRK EPEALAAASL KRLFVENQPY
LVGGCCQHGM SGSTVPNNRV SGIKFSLSLN KLKAPQLDAP NNILSVAEKY DYMKQTFRKR
LAFGIHGFGI FAKHPHRAGD MVIEYTGELV RPSIADRREH FIYNSLVGAG TYLFRIDNER
VIDATRAGSI AHLINHSCEP NCYSRVISVH GNEHIIIFAK RDIKRWEELT YDYRFFSIDE
RLACYCGFPR CRGVVNDTEA EEQVSKILVN RGELIQWTGE
//
