ID A0A0A0A7H6_CHAVO Unreviewed; 1988 AA.
AC A0A0A0A7H6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Histone-lysine N-methyltransferase SETD1B {ECO:0000313|EMBL:KGL89413.1};
DE Flags: Fragment;
GN ORFNames=N301_08431 {ECO:0000313|EMBL:KGL89413.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL89413.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL89413.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL89413.1};
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 speckle {ECO:0000256|ARBA:ARBA00004324}.
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DR EMBL; KL870823; KGL89413.1; -; Genomic_DNA.
DR STRING; 50402.A0A0A0A7H6; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd12549; RRM_Set1B; 1.
DR CDD; cd19169; SET_SETD1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR034468; Set1B_RRM.
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:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1B; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KGL89413.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGL89413.1}.
FT DOMAIN 86..174
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 1849..1966
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1972..1988
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 224..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1651..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1794..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1007
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1068
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL89413.1"
FT NON_TER 1988
FT /evidence="ECO:0000313|EMBL:KGL89413.1"
SQ SEQUENCE 1988 AA; 220786 MW; 90B37D3C6BEF3210 CRC64;
WINGMENSTQ ASTSVEKRNH HWRSYKLIID PALKKGQHKL YRYDGQHFSM PNSGIAPVDC
VRDPRIGRIW TKTKELELSV PKFKIDEFYV GPVPPKQVTF AKLNDNIREN FLTDMCKKYG
EVEEVEILYN PKNKKHLGIA KVIFATVKGA REAVQHLHNT SVMGNIIHVE LDTKGETRMR
FYELLVNGLY TPQTLPVGTE QDVSPTANET LQLTDSLKRL KDSNLSSAGS SVTPNSSTPF
SHDTAYSSCR QDTPNSYSQF TPQSQGTPHT PRLGTPFSQD STYSSRQTTP VYHFGQDSGY
KPRRHETKFT DAYNRRPGHH YVHNSAGVYR GTEHQFSTFK SHQQDPVQFS HTPPLSHSSS
SSYKSAFSPY QAPAVFPQSD EQQFPQTSRE TEYRRPAPPP AEMVVESSAA TNIDFVPVKE
KQEEPPPLPD SNSVPEPSTA SFSQTPERSE TPGTPTMESE MQHNSLDSRI EMLLKEQRTK
LPFLNEHDSD NEIRMEGSPI SSSSSQLSPI PMYGSNSQPG YRGQTPSSRP SSTGLEDISP
TPLPDSDDDE PIPGTAALSQ NSRGASEASM TPIDQLSRTS KIETSEAKEM VPGDQTPTSE
KMDEGQHSSG EDMEISDDET NPAPITSAEC AKTIVVNSSV SNTAVMAPSI PPLPPPGFPP
LPPPPPPQPG FPMPPPLPPP PPPTHPAVTV PPPPLPAPPG VPPPHILPPL PPFHPGMFPV
MQVDMISVLG NQWGGMPMSF QMQTQMLSRM MQAQNTYQYP PFMTGRMQFV NLPPYRPFSM
GAALGRGQQW PPLPKFDPSV PPPGYEPKKE DPHKATVDGV LLVIVKELKA IMKRDLNRKM
VEVVAFRAFD DWWDKKERLA KASLTPVKSG GELEEKPKPK DRIASCLLEN WNKGEGLGYE
GIGLGIGLRG AIRLPSFKVK RKEPPEAASA GDQKRIRPST SVDDEDEESE RDRDASDTTS
DLSKKDAEAV GLRRRPARPL ELDSEGEEGD ETSGKEEESS SEKEEEQEEE GGLVKAAPGK
EEEEDEDEED EDEEDEDDDE EDDEDEDDEE ETGIDTSDKE EEQDSEEDVA SPSSSKAEVE
SSDESEDSSE FESSSDSDDE DEDEDEEEEE EEEEEEEEEV AEDQDREPMV AETEHEPAGH
ELPDDERETI LELYPVDDYM DTTGLGLAEP ALAVKDEGME EIKAGEGECG DVPEASIAAE
TLKHLVMERD QETKLALSPI CRPEEESEPT TMLEPEVQEG PKPESQDEEA ALCISTPVGV
FGEPLPNKSS FFSKSDDSSL EARVKTKLPS AAEEDDRLPR TPGREVMIHS DTDTLLLPAH
KVPSSMLPLP STPGKEESLV PPEKFPEQLM VTKTSVEEEI PRTPGRDILA KSSHPLVKSQ
STDTVPATPG SDAPLTGSSL TLSSPQVPGS PFSYPSQSPG INSGIPRTPG RDFNFTPTFP
EAGATIPCLL SGKKQSEDEL DEKPFKEPLG ASLTISMNSV PSPIPFASPP QADFHTDMGL
PPDEPIPVAA LPCMHGDGRM PIEECKAEVK SVLLSPEVPT GASILPPPPP PSVLPKRRPG
RPKRSPPSVL SLDVYSGKTI EPPPVPVALV ESAVGKELLS GHPDAFYGLK DPEAVTLDFR
NDGFHEKMAA ETVAEKLPFK ELENQWNEDF KEEEAHAKPK RQWRRQKKTP EDLPVIPSPE
YSPPRPQFRP RSEFEEMTIL YDIWNGGIDE EDIKFMCITY DRLLQQDNGM DWLNDTLWVF
HPYILSRCFS TPKKKKRDDG MREHVTGCAR SEGYYKIDKK DKLKYLNNSR AFAEEPPADT
QGMSIPAQPH ASTRAGSERR SEQRRLLSSF TGSCDSDLLK FNQLKFRKKK LKFCKSHIHD
WGLFAMEPIA ADEMVIEYVG QNIRQVIADM REKRYEDEGI GSSYMFRVDH DTIIDATKCG
NFARFINHSC NPNCYAKVIT VESQKKIVIY SKQHINVNEE ITYDYKFPIE DVKIPCLCGS
ENCRGTLN
//
