ID S4R967_PETMA Unreviewed; 1211 AA.
AC S4R967;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=SET domain bifurcated histone lysine methyltransferase 1b {ECO:0000313|Ensembl:ENSPMAP00000001748.1};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000001748.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000001748.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; S4R967; -.
DR STRING; 7757.ENSPMAP00000001748; -.
DR Ensembl; ENSPMAT00000001757.1; ENSPMAP00000001748.1; ENSPMAG00000001573.1.
DR GeneTree; ENSGT00940000157471; -.
DR HOGENOM; CLU_003279_1_0_1; -.
DR OMA; IRAVTNC; -.
DR Proteomes; UP000245300; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0140938; F:histone H3 methyltransferase activity; IEA:UniProt.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd01395; HMT_MBD; 1.
DR CDD; cd20382; Tudor_SETDB1_rpt1; 1.
DR CDD; cd21181; Tudor_SETDB1_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 3.
DR Gene3D; 2.170.270.10; SET domain; 2.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR040880; DUF5604.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR047232; SETDB1/2-like_MBD.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR041292; Tudor_4.
DR InterPro; IPR041291; TUDOR_5.
DR PANTHER; PTHR46024; HISTONE-LYSINE N-METHYLTRANSFERASE EGGLESS; 1.
DR PANTHER; PTHR46024:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETDB1; 1.
DR Pfam; PF18300; DUF5604; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF18358; Tudor_4; 1.
DR Pfam; PF18359; Tudor_5; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000245300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 556..627
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 689..762
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 765..1186
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1195..1211
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 380..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 136889 MW; B370D5D61F952B33 CRC64;
EDLVVSVEEM ELLVEKHLAE YADFHKQCTT FQEVQLLLAQ REEKVANIDH IYSGFKMTVD
HIQGQVRELY IKLGLNFDEV ESLADAAIEI ATTTGKEPSN DVIEILDDED ENAEANSETD
SLKEVQCCLS TLKLNIPLFL MLVERRPLFC KSIALNSTTP WQMIGHSSHV GDEILLGMRV
LGKKRTKTWH RGILVAIVSS ASGFKYKVKF DSKGKSLLSG NHIAYDRHPE SESLVVGSRV
VAKYKDGSSV WLYAGIVAET PHRTNKYRFL IFFDDGYASY VTLLELYEVC RQLTNSWEDV
DDRASREFME DYIKSYPNRP MVLLKPGQNI KTEWEGTWWK SRIEEVDGSL VKIVFLIDER
CEWIYRGSTR LEPMHTLKHY HTEKKPGQRM RPTTAAGRNK GGPVVQYPQQ EPQQHTKPQT
PPFSPVPPKS QQLCSSHSES SLNSANRKQV AKKSTTFRQV TTSTRITDSD ITWPATNYSY
MPRINKLIQM TLGTTCATFT TNYLKCPVAH LILGRLLQSL ATYPIYKAPK EKLLYVPHAC
SQSCLRSLRP ANLDKYKGRN PLLVPLLYDF RRLSARRKIN RKAPFHMMYR APCGRSLRCM
MEVQRYLFET YANFLFLEQF CFDPYVMAER RISTVKPLYC VRDITNGVED VPVSCVNEID
SEPPPDAAYS KVRIPEHGVF INTSPEFLVC CSCTDGCQDK SKCACQQLTV DATGCSPGGQ
TNTDAGYHNK RLEECLPTGI YECNKQCKCN VRMCQNRLVQ HGLQVRLQLF KTQNKGWGIR
CLDDISKGSY VCIYAGKILT DDTADKEGLE MGDEYFANLD YIESVERHKD GYESEALASS
ESSGVNVKGG DDEEGSDDSE SFCSNDHPEY RSPRVHRDTK RERHTHKARD TPKDTQKGTH
TTTSQPVSSP APPTPPVNSE TAKHKVASWL SANQLDALTV QDSDSRSSFK NVEDLTKDSS
KMADCRTETT FCSTVSIWCY KSNFKIKQCI ANSLLKVTDS HLIETYRAVD PKDDLLSRPR
GHHSCRLMSH HEIMILSSSS ECEFQKGSTN AVPTLNSDDV QTISSGTDSD LADRPLKRQV
AVKRGFAFKT TARGVAVKST GMRRTGEGGN QPEKKSTREF FDGEDSCYII DAKLIGNLGR
YLNHSCSPNL FVQNVFVDTH DLRFPWVAFF ASKRIRAGTE LTWDYSYEVG SVPGKELLCY
CGSTECRGRL L
//
