ID A0A1L8GCM2_XENLA Unreviewed; 855 AA.
AC A0A1L8GCM2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=[histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B {ECO:0000256|ARBA:ARBA00031786};
DE EC=2.1.1.361 {ECO:0000256|ARBA:ARBA00012187};
DE EC=2.1.1.362 {ECO:0000256|ARBA:ARBA00012188};
DE AltName: Full=[histone H4]-lysine20 N-methyltransferase KMT5B {ECO:0000256|ARBA:ARBA00031835};
GN Name=kmt5b.S {ECO:0000313|RefSeq:XP_018115082.1,
GN ECO:0000313|RefSeq:XP_018115083.1, ECO:0000313|RefSeq:XP_018115084.1,
GN ECO:0000313|RefSeq:XP_018115085.1, ECO:0000313|RefSeq:XP_018115086.1,
GN ECO:0000313|Xenbase:XB-GENE-866439};
GN Synonyms=cgi-85 {ECO:0000313|RefSeq:XP_018115083.1,
GN ECO:0000313|RefSeq:XP_018115084.1, ECO:0000313|RefSeq:XP_018115086.1},
GN cgi85 {ECO:0000313|RefSeq:XP_018115083.1,
GN ECO:0000313|RefSeq:XP_018115084.1, ECO:0000313|RefSeq:XP_018115086.1},
GN kmt5b {ECO:0000313|RefSeq:XP_018115082.1,
GN ECO:0000313|RefSeq:XP_018115083.1, ECO:0000313|RefSeq:XP_018115084.1,
GN ECO:0000313|RefSeq:XP_018115085.1, ECO:0000313|RefSeq:XP_018115086.1},
GN kmt5b-a {ECO:0000313|RefSeq:XP_018115083.1,
GN ECO:0000313|RefSeq:XP_018115084.1, ECO:0000313|RefSeq:XP_018115086.1},
GN suv420h1 {ECO:0000313|RefSeq:XP_018115083.1,
GN ECO:0000313|RefSeq:XP_018115084.1}, suv420h1-a
GN {ECO:0000313|RefSeq:XP_018115082.1, ECO:0000313|RefSeq:XP_018115083.1,
GN ECO:0000313|RefSeq:XP_018115084.1, ECO:0000313|RefSeq:XP_018115085.1,
GN ECO:0000313|RefSeq:XP_018115086.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018115084.1};
RN [1] {ECO:0000313|RefSeq:XP_018115083.1, ECO:0000313|RefSeq:XP_018115084.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018115082.1,
RC ECO:0000313|RefSeq:XP_018115083.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018115082.1,
RC ECO:0000313|RefSeq:XP_018115083.1};
RG RefSeq;
RL Submitted (APR-2022) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC Evidence={ECO:0000256|ARBA:ARBA00023995};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60345;
CC Evidence={ECO:0000256|ARBA:ARBA00023995};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4]
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61992, Rhea:RHEA-
CC COMP:15556, Rhea:RHEA-COMP:15998, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000256|ARBA:ARBA00001543};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61993;
CC Evidence={ECO:0000256|ARBA:ARBA00001543};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-
CC COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; EC=2.1.1.362;
CC Evidence={ECO:0000256|ARBA:ARBA00000167};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC Evidence={ECO:0000256|ARBA:ARBA00000167};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_018115082.1; XM_018259593.1.
DR RefSeq; XP_018115083.1; XM_018259594.2.
DR RefSeq; XP_018115084.1; XM_018259595.2.
DR RefSeq; XP_018115085.1; XM_018259596.2.
DR RefSeq; XP_018115086.1; XM_018259597.2.
DR STRING; 8355.A0A1L8GCM2; -.
DR PaxDb; 8355-A0A1L8GCM2; -.
DR GeneID; 444204; -.
DR AGR; Xenbase:XB-GENE-866439; -.
DR CTD; 444204; -.
DR Xenbase; XB-GENE-866439; kmt5b.S.
DR OMA; NDHAQTK; -.
DR OrthoDB; 5396777at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 444204; Expressed in lung and 19 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140944; F:histone H4K20 monomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0140941; F:histone H4K20me methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR CDD; cd19184; SET_KMT5B; 1.
DR Gene3D; 1.10.10.1700; Histone-lysine N-methyltransferase; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR041938; Hist-Lys_N-MTase_N.
DR InterPro; IPR044424; KMT5B_SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR039977; Suv4-20/Set9.
DR InterPro; IPR025790; Suv4-20_animal.
DR PANTHER; PTHR12977:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE KMT5B-RELATED; 1.
DR PANTHER; PTHR12977; SUPPRESSOR OF VARIEGATION 4-20-RELATED; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 169..284
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 18..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..818
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 97586 MW; 81219B0937AFF9F0 CRC64;
MKWLGESKNM VVNGRRNGNR LSAELRQNQP KLHSPGRENL RTSKNVPDRR SGRFGNVAFE
AQSRYVPSSG MSAKELSEND DLATSLVLDP YLGFQTHKMN ARFRPIKGRQ EELKEVIENF
KKKEHLEKTF KNLVAGDWSR HYFLNKTKMQ EKHFKEHVFI YLRMFATSSG FEILPCNRYS
SERNGAKIVA TKEWKRNDKI ELLVGCIAEL SEAEENMLLR HGENDFSVMY STRKNCAQLW
LGPAAFINHD CRPNCKFVST GRDTACVKAL RDIEPGEEIS CYYGDGFFGE NNEFCECYTC
ERRATGAFKS RVGLNEPGPL INSKYGLRET DKRLNRLKKL GDSGKNSDSQ SVSSNTDADT
SQEKDMSNRK SNGMRKRSKS RTLRRRSMSR IPVSSSSTSS KLPHINNSRV PKRLRKPPKP
FHSKLKIRCH RKKVEQKKAS KKLEVSNLVL KEPKVVLYKN LAIKKDRESQ GAVPVTETTG
CLTRHAAREY KLNSLKGAHS HGEPSPCTYI TRSSLRTRFK SNDMSEAKLQ HNSVDGYRSS
HGTVLQVDKS EPLCQSTCKN ELLQETPRQT IRFHRNNFNT STRNSQQNRY IKQASKVEDS
VSSVYDQSSK DHALPDLGNS HCDLGEGNAL IQTSPDYKSF ESSADEYPLV TSEITKTKKN
NRTAKNKKSR RITRYDAQLI LENSTGIPKL TLRRRHDSNS SKTNEKENEG MSSSKISIKL
SKDHEKDNGL YVAKLNNGFN SGSGSTSTKL KIQLKRDEEN RTAFPNENGM YCNDTLSLLE
TRMKVDGYDH YEEESVEESS TEEDEEEEDE YDDEFEDDFI PLPPAKRLRL IVGKDSIDID
ISSRRREDQS LRLNA
//
