ID   SET1B_XENTR             Reviewed;        1956 AA.
AC   Q08D57;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD1B;
DE            EC=2.1.1.43;
DE   AltName: Full=SET domain-containing protein 1B;
GN   Name=setd1b;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone methyltransferase that specifically methylates
CC       'Lys-4' of histone H3, when part of the SET1 histone
CC       methyltransferase (HMT) complex, but not if the neighboring 'Lys-
CC       9' residue is already methylated. H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       activation (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + histone L-lysine =
CC       S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity).
CC   -!- SIMILARITY: Contains 1 post-SET domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SIMILARITY: Contains 1 SET domain.
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DR   EMBL; BC123932; AAI23933.1; -; mRNA.
DR   RefSeq; NP_001072649.1; -.
DR   UniGene; Str.52478; -.
DR   GeneID; 780106; -.
DR   KEGG; xtr:780106; -.
DR   Xenbase; XB-FEAT-5842343; setd1b.
DR   HOVERGEN; Q08D57; -.
DR   BRENDA; 2.1.1.43; 279072.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; a_b_plait_nuc_bd.
DR   InterPro; IPR015722; MLL.
DR   InterPro; IPR003616; Post-SET_Zn_bd.
DR   InterPro; IPR000504; RRM_RNP1.
DR   InterPro; IPR001214; SET.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   PANTHER; PTHR22884:SF10; MLL; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Activator; Chromatin regulator; Methyltransferase; Nucleus;
KW   RNA-binding; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1   1956       Histone-lysine N-methyltransferase
FT                                SETD1B.
FT                                /FTId=PRO_0000316998.
FT   DOMAIN      111    199       RRM.
FT   DOMAIN     1816   1938       SET.
FT   DOMAIN     1940   1956       Post-SET.
FT   COMPBIAS    657    722       Pro-rich.
FT   COMPBIAS    987   1223       Glu-rich.
SQ   SEQUENCE   1956 AA;  218069 MW;  9AFF263E87E53DCD CRC64;
     MSFKEAKPGE RGKNPEDHGR KQTASWINGM EAGNQPSTSG EKKSHHWRSY KLIIDPALRK
     GQHKLYRYDG LSFSMPNSGV PPVDSVRDPR IGRIWTKTKE LDLPVPKLKI DEFYVGPVPP
     KQVTFAKLND NIRENFLGDM CKKYGEVEEV EILYNPKNKK HLGIAKVIFA SVKGARDAVK
     HLHNTSVMGN IIHVELDTKG ETRMRFYDLL VNGFYTPQTL PVGSDLDASP TVNETPQVVE
     SVKRTKETAI GPSVTPNSST PFSHDTAYSS SRQGTPNSYS QFTPQSQGTP HTPRLGTPFS
     QDSSYSSRQT TPAFHYGQDS GFKPRRHENK FTDAYNRRPG HHYVHSSGSY RGTEHTFNVT
     RPQPEPVQVP RTPPLSHSSG NYKSAFSPYQ GNTVFPQTDE SQYPQTSRDM EYRRTGPQTS
     DSYSDAGCNS ASLELKPVKE KPEEPPPPEP DSTTEQKASF SQTPERCETP GTPTLEAELQ
     HNSLDTRIAM LLKEQRTQLH LIAGDQNSDN EIRMEGSPIS SSSSQLSPIP PYSSGSRYQD
     VTPSSRPSST GLEDISPTPL PDSDDDDEPI PGTASLCQNS RSASPIDQIN QSGRKTESLD
     KKELVAGDET PTSEKMDEGH PSSGEDMEIS DDEVTPSPIT SAECAITSSS VISSVIPIPP
     PGFPPLPPPP PPQPGFPMPP PLPPPPPPTH PSVTVPPPPL PAPPGVPPHH ILHHPPPYHH
     FPVMQGEMMN VLGNHWGGMT MSFQMQTQML SRMMQGQGSY PYHHFMGGSM QFGNQHPYRP
     FAISAHLTRG QPWPPFPKFD PSVPPPGYEH KKEDPHKATV DGVLQVIVKE LKAIMKRDLN
     RKMVEVVAFR AFDEWWDKKE RLAKQSLTPV KSGESKEEDK QKTKEHITSS LLESWNKGEG
     LGFEGIGLGI GLRGAIRLPS FKVKRKEPPD AALAGDQKRI RPSHSVDDED EESERDRDIS
     STASDLSKKD ADAVNNRRRP ARPLDSEGEE EVESEGDDGE TSDKEDSSSE KEDQDDGSVS
     ALSSKKQLYG DKEGDDEDDD TQSSGKEEDL VSEEEDTTSV ASSRAEMDSS DESEESSEYE
     SSSDSDEKEE EDDEEEELVF GDDQSEDQDL GQEYEVETDR EEDFFRENLS ECSSLPKAGD
     VELEDEMQKV EEDVARQTTQ ETLHLRKKNL DVPLVESKEC KQDTLDKVEK LFAVPMQEEV
     FKEHEKAPSP MNEEEEYIEL QLEPVPLVPE GAAPAAQEPV IIRPLTPTGA FGETGPVLKL
     EEPKLQVNLT QFATEDEELY PRTPGRDTAA HSDTEVTFQP GLKVAPSSLP FLPSHNKEEE
     CLLPPEKHAG HLTVTKMLSE EDLPRTPGRD IVVKSSHLGK SQSTETVPAT PGSDAPLTGS
     SLTLTSPHIP GSPFSYLSQS PGIINSGIPR TPGRDFNFTP TFPESNSIFP CHPSGKKPSV
     DEPDEKSFKE PTSASLTMNS VPSPIPFASP PRGLPHMDIR LGADDLESSD TPAYLSDKLL
     SEESECEFTK VHLTSTDESA PSPPLPPAEK RKGDRSKKPL SAHEFETEKN YETSSAVAMS
     EGALGKQMFI GQPDAVSGIK DPAAVPLDFR NDSLSENTVH EPIIQKVPLK ELENQWNEVL
     KEEEDITKHK KSRNSRHNNR YDEFSTVPSP EFSPPRAMFK PRSEFEEMTI LYDIWNGGID
     DEDIKYMCIT YDRLLQQDNG MDWLNDTLWV YHPSTSVYSP KKKKRDDGLR EHVTGCARSE
     GYYKIDKKDK LKYLINNRSL TEELPIDTQG KSIPAQPQAS TRAGSERRSE QRRLLSSFTG
     SCDSDLLKFN QLKFRKKKLR FCKSHIHDWG LFAMEPIIAD EMVIEYVGQN IRQVIADMRE
     KRYEDEGIGS SYMFRVDHDT IIDATKCGNF ARFINHSCNP NCYAKVITVE SQKKIVIYSK
     QYINVNEEIT YDYKFPIEDV KIPCLCGAEN CRGTLN
//