ID A0A0D2TG17_GOSRA Unreviewed; 1084 AA.
AC A0A0D2TG17;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Histone-lysine N-methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B456_012G003100 {ECO:0000313|EMBL:KJB74703.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB74703.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB74703.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM001751; KJB74703.1; -; Genomic_DNA.
DR RefSeq; XP_012460028.1; XM_012604574.1.
DR AlphaFoldDB; A0A0D2TG17; -.
DR STRING; 29730.A0A0D2TG17; -.
DR EnsemblPlants; KJB74703; KJB74703; B456_012G003100.
DR GeneID; 105780319; -.
DR Gramene; KJB74703; KJB74703; B456_012G003100.
DR KEGG; gra:105780319; -.
DR eggNOG; KOG1080; Eukaryota.
DR OrthoDB; 304343at2759; -.
DR Proteomes; UP000032304; Chromosome 12.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048188; C:Set1C/COMPASS complex; 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:0006325; P:chromatin organization; 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 CDD; cd15663; ePHD_ATX3_4_5_like; 1.
DR CDD; cd15495; PHD_ATX3_4_5_like; 1.
DR CDD; cd15517; PHD_TCF19_like; 1.
DR CDD; cd20143; PWWP_AtATX3-like; 1.
DR CDD; cd10518; SET_SETD1-like; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR041955; ATX3/4/5_ePHD.
DR InterPro; IPR042011; ATX3/4/5_PHD.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR025780; Hist-Lys_N-MeTrfase_ATX.
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:SF132; PHD FINGER PROTEIN RHINOCEROS; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00628; PHD; 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; SM00249; PHD; 3.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS51566; SAM_MT43_TRX_MLL; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT TRANSMEM 41..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 269..338
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 460..516
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 655..706
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 709..824
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 942..1059
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1068..1084
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 13..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1084 AA; 122900 MW; 42EBCF06190EC7BE CRC64;
MIIKRNLKSQ MPSLKRCKLG DSVGEDEDSS GTTRKKRKIN YYYPLTLLGH VAAGIIPVSL
HYIIASGELE KGFAASWNTE VSCSPDEVES KSKRSDSSKP KNRTVEIARP PLVRTSRGRV
QVLPSRFNDS VIESWKKESK TSLHDHSFDE DEDDDDFECK KDKFSFKSSK NCKQNMKNQR
NKENNGYKGR KYTTLCEEDD REAGYGRSSG IGKYSSFRSS LTSVHEQLVG EYEKNANGVL
IVDLTTQGQA SRENGEKEDG LYGPEDFYSG DIVWARPGKR EPCWPAIVID PMTQAPELVL
RSCIAEAACV MFFGHSGNEN QRDYAWVRRG MIFPFADFLD RFHEQPELAG CKPSDFQLAM
EEALLAEEGF TEKLMDDINI AAGNPAYDES ILRWGQEATG SNQDLGYCLP NQGLFGKCKD
ARFCESCGMT LPFKMGKKMK ASTPGGQFLC KTCARLTKSK HYCGICKKIW NQSNSGSWVR
CDGCKVWVHA ECDKISSRHF KDLGATDYYC PACKAKFNFE LSNPEKWQPK AKSKNNNSQL
LLPNKVTIVC CGVEGIYYPS LHLVVCKCGS CGSEKQALSE WERHTGSRER NWRVSVKVKG
SLLPLEQWML QLAEYHANAT SSAKPPKRPS LRERKQKLLA FLQEKYEPVR AKWTTERCAV
CRWVEDCDYN KIIICNRCQI AVHQECYGAR NVRDFTSWVC KACETPEVTR ECCLCPVKGG
ALKPTDIETL WVHVTCAWFQ PEVSFASDEK MEPALGILSI PSDSFVKICV ICKQIHGSCT
KCCKCSTYYH AMCASRAGYC MELHCLEKNG RQITKKVSYC AYHRAPNPDT VLIIQTPLGV
FSAKKKSGSR LISSKRVKIE EVPTVETTDV EPFSAARCRV FKRSNNNRKR TEEEAVAHRL
MRPCHHPLST IQSLNAFRMV EEPTGFSSFR DRLYHLQRTE NDRVCFGRSG IHGWGLFARR
NIQEGEMVLE YRGEQVRRSI ADLREARYRI EGKDCYLFKI SEEVVVDATD KGNIARLINH
SCMPNCYARI MSVGDDESRI VLIAKTNVSA GDELTYDYLF DPDEPEEFKV PCLCKAPNCR
KFMN
//
