ID H3A4E9_LATCH Unreviewed; 1677 AA.
AC H3A4E9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=SET domain containing 1A, histone lysine methyltransferase {ECO:0008006|Google:ProtNLM};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000004520.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000004520.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AFYH01127754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01127755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01127756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01127757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01127758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01127759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01127760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01127761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000004520; -.
DR Ensembl; ENSLACT00000004559.1; ENSLACP00000004520.1; ENSLACG00000004022.1.
DR eggNOG; KOG1080; Eukaryota.
DR GeneTree; ENSGT00940000162290; -.
DR HOGENOM; CLU_001226_0_0_1; -.
DR InParanoid; H3A4E9; -.
DR OMA; WARTREI; -.
DR TreeFam; TF106436; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0042800; F:histone H3K4 methyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd19169; SET_SETD1; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR037841; SET_SETD1A/B.
DR PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR PANTHER; PTHR45814:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1538..1655
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1661..1677
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..425
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..805
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..862
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1677 AA; 186092 MW; 70456D3777FE4E22 CRC64;
RQGTPGYSSY METGYKSRRQ ENSYQDSFSR RTNHHYSHNT PHYRGNDPHF PASYNQQYES
GPLFPHHHHH QDGNSFQPYQ NVAETPSSTP FSMHMEQAFE QPSGDKDYRL LATQPEAFAV
ANSDYFAQEE EAVAPSPGVA PAGDERSRSP EPMQASPARS GSPEPDSTNE SVPFAHHSSL
DSRIEMLLKE QRSKFSFLNS ESEQEEEKEE EEEEKGAAQN QPATPPPPLP VSFEDILLPH
DTGQRRIAPT ENGQDGTVVI GTRLLFQCNG RGFGKGAMVY INYLHVNSWC PPINLLQVLC
VYKVPRLEVV KTSHHSSGED MEISDDEVAD QSHAEQQFSV IPPALGGMPL NVPAYAPHHQ
LPHPQSSFQL QPPPGISHAM GHLSGAEVGP HPPPPPPPPP PPPPQVPEFP LPHPHHLQPE
PPPPHIYDFV NSMELMNRLG NQWGGMPMSF QMQTQMLSRL HQMRQSGKGQ GSFEDPFATF
PPGQDSTAVA AGAFGNPPHP YSHYPLDQDN PHFDRDHRFP PHPHHPHLHQ RPFDYGAPTW
SYAEEKDPHS ATVGSVLSTL VQEMKNIMQR DLNRKMVENI AFGTFDEWWE RKEQKAKPFQ
NAAKLQAKEE EKEKAKPKEP GLVSLVDWAK SGGAGGLEGF GFGTGLRGAL RLPSFKVKRK
ELSELSECSE QKRPRPSTPA EEDEDEADRE KESSESVRPG SKTSKREEAK SRSSGKRRKS
LDLDSEGEET SEESNSEKAD GRENESDSKK RPSLVRQGAG GQVEERVNLT EKKRPFLKAN
ETDAWLEEEE DLETSEKEEE SEDEAVSETS SKAEAETDEE SDTTSDSESS SSSSSSEEEE
EEEELAAGSA EETADETADT MDESTMDGSL AEAEERECRA QKEAVGAKPQ VREPDVTKDQ
LRVMEPEEFK VEPQVMDSKV KVEAQTTELE EGRVQELVKS ALCSRIPPPP SMVLSVQHLT
ETPPEKPPEA GMARSELEGR LPKTEERRAG DVGSAETAAK KEEPIALLPP LKKRRKTVSF
SVVPEEEGPA EKKGEASLEA AASAAAAPRA QPDTPVTSTV KLESETESPH ASPSKSEVPL
NYAVSTPDTL PTPAVATSFK TELPMVPEAK SPDALEEMGA PTVKPPVPAT PTRKLPTKAD
SPLTPLGKPH PAISVSRLLS KPEAPVIPKT RTPPKNEAPV TPLSKLPLRP ELTIGKPLEA
SEPLVTPVPK LPSKNKGRVP QEQDSEGTET SDEAEGQPVA SELTPPDQLR VAAPKKVPSK
AAGDEIIHMD ILAGQVGAVL EAPEEVIAGT DASETLAKPE LLVGELQPQL SVPASPAKSE
KPEQAKAKKK KHKEKQKAKK EAAIAEPGEV PHSDEERRKE RRRSLRSRQC AHVEPRFETR
SEFEQMTVLY DIWNCGIDSE DMHYLKLTYE KLLQEDSATD WLNDTHWVHH TNILSRSKKK
KKSQDGLREH KTGSARSEGY YHISKKEKDK YLNLCPVTPR ALETVDTQGV DGLLFRGCST
RGCWRTAFLF ELLFSLLLTD EVRIASAIVF NNINFRKKKL RFGRSRIHEW GLFAMEPIAA
DEMVIEYVGQ NIRQVVADMR EKRYVQEGIG SSYLFRVDHD TIIDATKCGN LARFINHCCT
PNCYAKVITL ESQKKIVIYS KQPIGVNEEI TYDYKFPIEE NKIPCLCGME NCRGVLN
//
