ID A0A093PNT6_9PASS Unreviewed; 1380 AA.
AC A0A093PNT6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Histone-lysine N-methyltransferase NSD2 {ECO:0000313|EMBL:KFW78493.1};
GN ORFNames=N305_04561 {ECO:0000313|EMBL:KFW78493.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW78493.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW78493.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW78493.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KL670101; KFW78493.1; -; Genomic_DNA.
DR STRING; 328815.ENSMVIP00005001863; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd21991; HMG-box_NSD2; 1.
DR CDD; cd15651; PHD2_NSD2; 1.
DR CDD; cd15654; PHD3_NSD2; 1.
DR CDD; cd15657; PHD4_NSD2; 1.
DR CDD; cd15660; PHD5_NSD2; 1.
DR CDD; cd20165; PWWP_NSD2_rpt2; 1.
DR CDD; cd19211; SET_NSD2; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR041306; C5HCH.
DR InterPro; IPR047443; HMG-box_NSD2.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR047439; PHD2_NSD2.
DR InterPro; IPR047441; PHD3_NSD2.
DR InterPro; IPR047442; PHD5_NSD2.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR047435; PWWP_NSD2_rpt2.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR047437; SET_NSD2.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22884:SF293; HISTONE-LYSINE N-METHYLTRANSFERASE NSD2; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF17982; C5HCH; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00855; PWWP; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00293; PWWP; 2.
DR SMART; SM00184; RING; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 2.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KFW78493.1};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFW78493.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 223..288
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 457..506
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 671..717
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 732..778
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 846..890
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 895..957
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1026..1076
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1078..1195
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1202..1218
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DNA_BIND 457..506
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 143..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 156216 MW; A9A4790B02E52BC5 CRC64;
MDFSIKRSSQ LLAQKIKYIK MKQVPEILGN TNGKPQNCEV NRECSVYLGK AQLSATLQEG
VMQKYNGHET LPFIPAEKLK DLTSRVFNGE SGAQDAKLRF EPQEIKGVGT PPNTTPIKNG
SPEIKLKITK TYMNGKPLFE SSICGDNGAD VSQSEENEQK PTNKERRNRK RSIKYDSLLE
QGLVEAALVS KTSSPTEKKA PAKRDPTQST TKEEKVHLLK YNVGDLVWSK VSGFPSGIEN
FFPTVSFNSE HFLKGQKKSF RQYHVQFFGD VPERAWIFEK SLVPFKEKDQ FEQLCQESAR
QALTKAEKIK MLKPVSGKLR PQWEMGVKQA SEAAGMTVEE RKAKYTFIYV RDRPHLNPRV
AKEVGITVEP PEEMDESSYS NEETTPNLRS MKESGIPNKR RRRTSKLSAT DDTQESSQLE
DKNTTPQKSS EQAESKRGIG SPLNRKKTPA STPRSRKGDA VSQFLVFCQK HRDEVVAEHP
DASSEEIEEL LESQWNMLSE KQKARYNTKF AIVTSPKSEE DSGNLHGNKR NQKKRTKEPT
EDFEVQEAPR KRLRMDKQNN RKRETSNDKT AKTNSSKVTE TSSSQKNQSA TKNLSDACKP
LKKRNRASAA ESSTLAFSKS SSPSASLTEN EISDGQGDER SESPYESADE TQTEVSISSK
KSERGAGTKK EYVCQLCEKT GDLLLCEGLC YRAFHVSCLG LSGRPAGKFI CSECTSGNYI
LFIILPLGVH TCFVCKERKA DVKRCVVSHC GKFYHEACVK KFHLTVFENR GFRCPLHSCL
SCHVSNPSHP RISKGKMMRC VRCPVAYHAG DVCIAAGCAV IASNSIVCTN HFTAMKGKSH
HAHVNVSWCF VCSKGGSLLC CESCPAAFHP DCLNIEMPDG SWYCNDCRAG KKLHFQDIIW
VKLGNYRWWP AEVCHPKNVP PNIQKMKHEI GEFPVFFFGS KDYYWTHQAR VFPYMEGDRG
SRYQGIKGIG KVFKNALQEA EARFREIKLQ REAKETQESE RKPPPYKHIK VNKPCGKVQI
YTADISEIPK CNCKPTDENP CGFDSECLNR MLMYECHPQV CPAGERCQNQ CFTKRQYPET
KIIKTDGKGW GLVAKRDIKK GEFVNEYVGE LIDEEECMAR IKYAHENDIT HFYMLTIDKD
RIIDAGPKGN YSRFMNHSCQ PNCETLKWTV NGDTRVGLFA VCDIPAGTEL TFNYNLDCLG
NEKTVCKCGA PNCSGFLGDR PKASNTSRDS DKEKGKKTKK RTRRRRMKNE GKKESEDDCF
RCGDGGQLVL CDRKSCTKAY HLSCLGLVKR PFGKWECPWH HCDVCGKPSV SFCHFCPNSF
CKEHQDRTVL NSMLNGQLCC SEHVLGVDSV ETRKTEKPRR KLNKLKPRRK RNRWMRAECK
//
