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Database: UniProt
Entry: A0A182MDI2_9DIPT
LinkDB: A0A182MDI2_9DIPT
Original site: A0A182MDI2_9DIPT 
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
//
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