ID A0A182K1T6_9DIPT Unreviewed; 1740 AA.
AC A0A182K1T6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Enhancer of yellow 2 transcription factor {ECO:0000256|HAMAP-Rule:MF_03046};
GN Name=e(y)2 {ECO:0000256|HAMAP-Rule:MF_03046};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR004720-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR004720-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR004720-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Involved in mRNA export coupled transcription activation by
CC association with both the TREX-2 and the SAGA complexes. The
CC transcription regulatory histone acetylation (HAT) complex SAGA is a
CC multiprotein complex that activates transcription by remodeling
CC chromatin and mediating histone acetylation and deubiquitination.
CC Within the SAGA complex, participates to a subcomplex that specifically
CC deubiquitinates histones. The SAGA complex is recruited to specific
CC gene promoters by activators, where it is required for transcription.
CC The TREX-2 complex functions in docking export-competent
CC ribonucleoprotein particles (mRNPs) to the nuclear entrance of the
CC nuclear pore complex (nuclear basket). TREX-2 participates in mRNA
CC export and accurate chromatin positioning in the nucleus by tethering
CC genes to the nuclear periphery. {ECO:0000256|HAMAP-Rule:MF_03046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2
CC complex (transcription and export complex 2). Component of the SAGA
CC transcription coactivator-HAT complex. Within the SAGA complex,
CC participates to a subcomplex of SAGA called the DUB module
CC (deubiquitination module). {ECO:0000256|HAMAP-Rule:MF_03046}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000256|HAMAP-
CC Rule:MF_03046}.
CC -!- SIMILARITY: Belongs to the ENY2 family. {ECO:0000256|HAMAP-
CC Rule:MF_03046}.
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DR STRING; 43041.A0A182K1T6; -.
DR EnsemblMetazoa; ACHR004720-RA; ACHR004720-PA; ACHR004720.
DR VEuPathDB; VectorBase:ACHR004720; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000075881; Unassembled WGS sequence.
DR GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-UniRule.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000124; C:SAGA complex; IEA:UniProtKB-UniRule.
DR GO; GO:0070390; C:transcription export complex 2; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051246; P:regulation of protein metabolic process; IEA:UniProt.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:UniProtKB-UniRule.
DR CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
DR Gene3D; 1.10.246.140; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR HAMAP; MF_03046; ENY2_Sus1; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR018783; TF_ENY2.
DR InterPro; IPR038212; TF_EnY2_sf.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042:SF197; EIF-2-ALPHA KINASE GCN2; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF10163; EnY2; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50908; RWD; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|HAMAP-Rule:MF_03046};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Chromatin regulator {ECO:0000256|HAMAP-Rule:MF_03046};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW mRNA transport {ECO:0000256|HAMAP-Rule:MF_03046};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03046};
KW Protein transport {ECO:0000256|HAMAP-Rule:MF_03046};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_03046};
KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_03046};
KW Transferase {ECO:0000256|ARBA:ARBA00022527};
KW Translocation {ECO:0000256|HAMAP-Rule:MF_03046};
KW Transport {ECO:0000256|HAMAP-Rule:MF_03046}.
FT DOMAIN 96..206
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 306..580
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 597..1052
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 252..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..758
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1740 AA; 193667 MW; 3993270E552040B7 CRC64;
MYSKSVDQIT ILHGDRTKLK DLLRLRLIEC GWNDQVRYLC RQAIAESSQT NVDAVVQVVT
PEARTLIPDV VKRELLQKIR MSLLQQEKLD LSISSRYAHE PGSIFHDEVE DLRPRTGKWK
PLELRLHLTP QRGSAKEAYV KADLLITCPP KYPKCPPKLE LKNAVGLSDS VVRELTEKLE
QLAEELKGEV MIFELANTVQ AFLHQYNVPP KGSFYDEMLA NQQKQALARQ NTLQAEENLK
RQAIQDELQR RKKELERTRR ESRHSTNESS PMHRLHSSSS TENSDGAVCL EHKRSEVLYF
RDGRKVLRGS CLGHSQRGCI TYAGIDQQTG ELVYLTEWTL YYDGDSSTES RTIRGRPVET
VIGDMERLLE SLIPLKHKHL IAYEGVLCRM GKEALTLFVV QEFILGTSLF SISGSLGWSV
EGASMVAKGT LEALIYLHNN GVSHDNLSDS TVFMDNAGMV RVADFRLIPF IQELGDGHYL
LHQSLRSPDL SSLGGLIEAL LAPHSEMKDF VDRCKSERTI SATELLDHPF LRSTLLHIDH
VTVGLQQVTA AVHKTLPAST AVGQRTEIDQ QQLVPYMPLM MNGSGTGQEK SRIQTEFELL
SYLGKGAYGD VLKVRNKLDN REYAIKRIRL PARSKQFYKK MTREVELLSR LNHENVVRYY
NSWVEATSTS EMVAATDTEG EMAGGTLSSC DWSVASRPKR KSSRVRRTTE VATGVVKKGI
SDKNIECFVD FLPNDTSSED DDEDDDDETN DLDGDSSSSS ESDESSGSLS NHRKLDEVSF
NDSSGGIEFV GSNGEAPSYN SYGEAGSAAE NGAAGDAGGK KVPTVTTPAP PEILYMYIQM
EFCEKSTLRT AIDAGLHQDI DRVWRLFREI VEGLSHIHQQ GMIHRDLKPV NIFLDSRDQV
KIGDFGLATT SILALQTQGH QNASSGQVGY LAVATTQPGK SSDIGYSLTG KVGTALYVAP
ELTGNASRST YNQKVDLYSL GIILFEMSSQ PINTGMERVK TLMDLRSDAI RLPETLLTDA
RYSRLVQVIR WLLNHDPQRR PTAEELLCSE LVPRTRLEAE EIQDVVRHIL SNPQSRHYKH
LIARCFSQES DPICELSYHL DMVPMIPILP RFDYVKAKLV ALFRKHGAIE VVTPLLTPYT
KQHAARSNTV KLMTHSGSVV TLPDDLRVPF LRYIALNGIK NIRRYSIGRV YREKKVFNFH
PKQVYECAFD IVTPSRGHLI TDAEMLAIAT NVMRELDLLQ GRNVFFRLNH IGLLRAILIH
CNVPLDKYRE LFEMVAEFLD DKISKFQLSS LINSLIGGST AKINVSYLCD ALQLELSSVG
LLGGSILKSI IRGKGEAASL AKVALRELET VVTLAQNMGV QCPLNVCPGL PVNYERAKTG
GIVWQLLGEL KPKRKNPLTT IAVGGRYDGK LAEFQKSGIN NGLQVPKVDL SGAGFSFLLD
KLVNAIAPSA GYEPTEVMIG VTGSRPQLKE VAQILRPLWS NSIKTCVVET SAGAVDDLGK
EAGATVVVML GDGGEMRVRS WNHDRFQEHH VTRPELMPYI LRTLRRSDVS TGEISQALQT
TSLGGSSTSA SFSYSSSFTA ISSSASMRLS SATSGAASQQ PSINTSPPLD LVFLTSEKIN
TSKKRRYEHQ VEHKMSPVLS KFHRKEKVTL IMVDVPSVPL RGLVGLIDPL ECGSQEDDDI
PSGSSIDRLE LQSLCERYPK YKRQLMEIYN EIVDLFAQSK GTTPVVGLYS VIDTFCRLIL
//
