ID A0A091WTX7_OPIHO Unreviewed; 1913 AA.
AC A0A091WTX7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Histone-lysine N-methyltransferase SETD1B {ECO:0000313|EMBL:KFR04891.1};
DE Flags: Fragment;
GN ORFNames=N306_02052 {ECO:0000313|EMBL:KFR04891.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR04891.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR04891.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR04891.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
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DR EMBL; KK734180; KFR04891.1; -; Genomic_DNA.
DR STRING; 30419.A0A091WTX7; -.
DR PhylomeDB; A0A091WTX7; -.
DR Proteomes; UP000053605; 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:KFR04891.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053605};
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:KFR04891.1}.
FT DOMAIN 35..123
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 1774..1891
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1897..1913
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 173..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1462..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1719..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..934
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..990
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1043
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR04891.1"
FT NON_TER 1913
FT /evidence="ECO:0000313|EMBL:KFR04891.1"
SQ SEQUENCE 1913 AA; 212357 MW; E8D02D97322F241F CRC64;
NSGIAPVDCV RDPRIGRIWT KTKELELSVP KFKIDEFYVG PVPPKQVTFA KLNDNIRENF
LTDMCKKYGE VEEVEILYNP KNKKHLGIAK VIFATVKGAR EAVQHLHNTS VMGNIIHVEL
DTKGETRMRF YELLVNGLYT PQTLPVGTEQ DVSPTVNETL QLTDSLKRLK DSNLSSAGSS
VTPNSSTPFS HDTAYSSCRQ DTPNSYSQFT PQSQGTPHTP RLGTPFSQDS TYSSRQTTPV
YHFGQDSGYK PRRHETKFTD AYNRRPGHHY VHNSAGVFRG TEHQFSTYKS HQQEPVQFSH
TPPLSHSSSS SYKSAFSPYQ APAVFPQSDE QQFPQTSRET EYRRPAPPPT EMVVESSAAT
NIDFVPVKEK QEEPPPLPDS NSVPESSTAS FSQTPERSET PGTPTMESEM QHNSLDSRIE
MLLKEQRTKL PFLNEHDSDN EVRMEGSPIS SSSSQLSPIP MYGSNSQPGY RGQTPSSRPS
STGLEDISPT PLPDSDDDEP IPGMVSLSQN SRGTSEASMT PIEQLSRTSK IETSEAKEMV
PGDQTPTSEK MDEGQHSSGE DMEISDDETN PAPITSAECA KTIVVNSSVS NTAVMAPSIP
PMPPPPPPPP THPAVTVPPP PLPAPPGVPP PHILPPLPPF HPGMFPVMQV DMISVLGNQW
GGMPMSFQMQ TQMLSRMMQA QNTYQYPPFM TGRMQFVNLP PYRPFSMGAA LARGQQWPPL
PKFDPSVPPP GYEPKKEDPH KATVDGVLLV IVKELKAIMK RDLNRKMVEV VAFRAFDDWW
DKKERLAKAS LTPVKSGGEL EEKPKPKDRI ASCLLENWNK GEGLGYEGIG LGIGLRGAIR
LPSFKVKRKE PPEAASAGDQ KRIRPSTSVD DEDEESERDR DASDTTSDLS KKDAEAVGLR
RRPARPLELD SEGEEGDETS GKEEESSSEK EEEQEEEGGL VKAAPGKDDE EDEDDEEDED
EDEEDDEDDD EEETGVDTSD KEEEQDSEED VASPSSSKAE VESSDESEDS SEFESSSDSD
DEDEDDDDEE EEEEEEEEEQ VAENQDREAM VAETEHEPAG HELPDDERET ILELYPVDDY
MDTMGLGLTE PALAVKDEGM EEIKAGEGEC GEVPEASIAA ETLKHLVMER DQETKHVLSP
ICRPEEESEP ATMLETEVQE GPKPESQDDE AGLCLSAPVG VFGEPLPIKS SFFSKSDDSS
SLEVCVKTKL PLAAEEDDRL PRTPGREVMI HSETDTLLLP AHKVPSSMLP LPSTPGKEES
LVPPEKFPEQ LLVTKTSVEE EVPRTPGRDI LAKSSHPLAK SQSTDTVPAT PGSDAPLTGS
SLTLSSPQVP GSPFSYPSQS PGINSGIPRT PGRDFNFTPT FPEAGATIPC LLSGKKQSED
ELDEKPFKEP LGASLTISMN SVPSPIPFAS PPQADFRTDI GLPPDEPIPV AVLPCVHGDG
RMPIEECKAE VKSVLLSPEV PTGASILPPP PPPSILPKRR PGRPRRSPPS VLSLDVYSSK
TIEPPPVPVA LVEGTVGKEL LSGHPDAFYG LKDPEAVTLD FRNDGFHEKI AAETVAEKLP
FKELENQWNE DFKEEEAHVK PKRQWRRPKK TSEDLPVIPS PEYSPPRPQF RPRSEFEEMT
ILYDIWNGGI DEEDIKFMCI TYDRLLQQDN GMDWLNDTLW VFHPYILSHW RSVFSTPKKK
KRDDGMREHV TGCARSEGYY KIDKKDKLKY LNNSRAFAEE PPADTQGMSI PAQPHASTRA
GSERRSEQRR LLSSFTGVCD SDLLKFNQLK FRKKKLKFCK SHIHDWGLFA MEPIAADEMV
IEYVGQNIRQ VIADMREKRY EDEGIGSSYM FRVDHDTIID ATKCGNFARF INHSCNPNCY
AKVITVESQK KIVIYSKQHI NVNEEITYDY KFPIEDVKIP CLCGSENCRG TLN
//
