ID A0A182MDI2_9DIPT Unreviewed; 1899 AA.
AC A0A182MDI2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Enhancer of polycomb-like protein {ECO:0000256|RuleBase:RU361124};
OS Anopheles culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA015627-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., 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 culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA015627-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA015627-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair. Involved in gene silencing by neighboring
CC heterochromatin, blockage of the silencing spreading along the
CC chromosome, and required for cell cycle progression through G2/M.
CC {ECO:0000256|ARBA:ARBA00025513}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU361124}.
CC -!- SIMILARITY: Belongs to the enhancer of polycomb family.
CC {ECO:0000256|ARBA:ARBA00008035, ECO:0000256|RuleBase:RU361124}.
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DR EMBL; AXCM01010687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 139723.A0A182MDI2; -.
DR EnsemblMetazoa; ACUA015627-RA; ACUA015627-PA; ACUA015627.
DR VEuPathDB; VectorBase:ACUA015627; -.
DR OrthoDB; 5398022at2759; -.
DR Proteomes; UP000075883; Unassembled WGS sequence.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR InterPro; IPR024943; Enhancer_polycomb.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR PANTHER; PTHR14898; ENHANCER OF POLYCOMB; 1.
DR PANTHER; PTHR14898:SF0; ENHANCER OF POLYCOMB-LIKE PROTEIN; 1.
DR Pfam; PF10513; EPL1; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361124};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU361124};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU361124}.
FT DOMAIN 10..87
FT /note="Enhancer of polycomb-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10513"
FT REGION 267..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1805..1825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1899 AA; 202947 MW; 3D3D28B3243EAFE9 CRC64;
LQRAICTGLI IPTPEVYDST DSEFYDKYYP PDYKLPKQLI HMQPLNLEQD IPDYDMDSAD
EVWVTSHEKK LDLDPLKFEI MMDRLEKSSG QTVVTLNEAK ALLKQDDEVS IAVYDYWLNK
RLKMQHPLIL YVKTENRGNM TPNNPYLAFR RRTEKMQTRK NRKNDESSYE KMLKLRRDLS
RAVTLLDMIK RREKLKREQL HLSIEIYEKR YQAQDFHGHL LSEFTSNATR VARPAFAPIY
TNQYAPLAGG QGVNAVGTGS YLNSGGSSAQ YEGHGTGGTS GTNKRDNESL SSRKEKRQYK
KRKLKLQKDR GLSSGTGSGT GSAGGRGDGA GGTNSAGGLG SSTMHHQQQH YHGTMLGGIG
GRGVDGTVSG GHGADHHHHL HASGDHVVSS DDEELSNLQG GSSAEEEYAY AFRRSKHSQY
HRPRADGYGN WPWTSREENG SADPRYRFTL TSLRYPRPRC IGFARRRLGR GGRVIIDRVA
TDFDDLWSRL DYTIVESETI ASLNLTEPTP KAWDDKKADE NNEPIVVPTR RRQIERTVSV
SSNCSNASSS AGVVVSLKPP RFAALYNHLH QNPPLVNGSA EMPSATTANG GNAPRTTTVG
RRKLILKEEQ PALSDYESDG GEIQFLASIG LMNKAEKDAE ATFANTKRRL RFDSEDKDEV
RPAGEGDSSE VSKDGGVLCD ERTLRDVQNS DSIVIKSEDS TELVMSTGRG GTAVVKQEPD
VMEDYQKPGG GTGLPMGEDF EQLIDSVNSH NNVRNRFNAA AGAGSSNSIS STSNDAGVMA
AGGELSNPHH SQTQPQTLGS ARKRQGPDGS PSRLHDATSE DINAVYKDLL NDIQSNWLHF
RPKTPEPSQD DLLTLDGDLE HCFGLTDRKR ITLELQALDE QLPSTIFAPS KGTTNSSQFR
TTPYDMDNLI EPHPLSLEEE DNSISAMAKG AAVASSSASA IEVKLETSGS SSADNNLSVP
SELNLSLNES SEDNEKMLDN ILQECAIDDP KQLHQTSNFW NGILDDGVLN NLESGDSEKS
TQEDEPMLED QEVSGESNLF ASSAAKIGYH SDLVGYGRPS GASDRRTSKS KRRKMLNRCS
YLVGSSYFSV KSLPKEEIFQ PLLDANGQPI LLSDGDVDCT VDGVTEQDAE DTMHGDLQST
AVGVEAMEIK MEEEATLTAT NELSEGIASV PVAIAGGEHV IKMEPPDELV VPAADAGGCD
ATLLGSTPTT VQFLPHNSTM AAPAATTIKL EPFNHISQIT ARSSTPDGGG RVVPTGSTTL
IPGTIVVSQP SSTGSSSMFS STSGTVPTVV SVALQQGSLH QLVHTSSAPS MGAGTTMLVM
QSIPANNGTS IQSSPSVSVA GTPTSFLLTT TGNVISGSNA MGTASSIAGS ILVQSSASST
LSNAVQSSSS STGSLLSGST PIVVTVPPAS SSGMSVTGGG SQPMSVVMPT SGTNTVVSIA
APIVVSSSSA TLAQSIAHAQ SQSATSVIGN STVASNNATS SANTTTALNS YIVQHNSTPI
MLSHQQMQQL ANSGGGNIVT VGGQQVVTAK QHHGETYVLT QTPLNKQING PSDGNKNVTT
TAVNAQNIKN QKIHALLSQK LGSKSADLNK KQLEIIRQAL GSSQKMIVKS TNHAQQLHGG
GAASGSAGIA GHHQQSPAQQ QQQQQYNVIH QNSLNSPITI VSAQSAGQPT QNKIILTSSP
HLLQQAAGVG GATAGQLIAA GHGKIQLTTV QQGQQQAQPG QVTATARGQI VTLDPSGQQG
AGTVGGVQQQ LKLEKNSILY NIKNSRGQFL HLNPKVVNII QPVQQQKIVN SLTIQQQQQQ
QQQQQQLLHN QTGHGGTTTI LSKGQTVQRI PTVSIRTQQQ AQQQQQQQQQ QQQQQQTNLV
DMVVVNNASN IKFIQAASAA AAAAAAGSGS TVNNTAGQD
//