GenomeNet

Database: UniProt/TrEMBL
Entry: Q7QKB2_ANOGA
LinkDB: Q7QKB2_ANOGA
Original site: Q7QKB2_ANOGA 
ID   Q7QKB2_ANOGA            Unreviewed;      2003 AA.
AC   Q7QKB2;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 5.
DT   24-JAN-2024, entry version 136.
DE   SubName: Full=AGAP002246-PA {ECO:0000313|EMBL:EAA03662.5};
GN   Name=1269315 {ECO:0000313|EnsemblMetazoa:AGAP002246-PA};
GN   ORFNames=AgaP_AGAP002246 {ECO:0000313|EMBL:EAA03662.5};
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA03662.5};
RN   [1] {ECO:0000313|EMBL:EAA03662.5, ECO:0000313|Proteomes:UP000007062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA03662.5,
RC   ECO:0000313|Proteomes:UP000007062};
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
RN   [2] {ECO:0000313|EMBL:EAA03662.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA03662.5};
RG   The Anopheles Genome Sequencing Consortium;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAA03662.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA03662.5};
RX   PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA   Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT   "The Anopheles gambiae genome: an update.";
RL   Trends Parasitol. 20:49-52(2004).
RN   [4] {ECO:0000313|EMBL:EAA03662.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA03662.5};
RX   PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA   Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA   Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT   "Update of the Anopheles gambiae PEST genome assembly.";
RL   Genome Biol. 8:R5.1-R5.13(2007).
RN   [5] {ECO:0000313|EMBL:EAA03662.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA03662.5};
RG   VectorBase;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EnsemblMetazoa:AGAP002246-PA}
RP   IDENTIFICATION.
RC   STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP002246-PA};
RG   EnsemblMetazoa;
RL   Submitted (JAN-2021) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AAAB01008799; EAA03662.5; -; Genomic_DNA.
DR   RefSeq; XP_307938.5; XM_307938.5.
DR   STRING; 7165.Q7QKB2; -.
DR   PaxDb; 7165-AGAP002246-PA; -.
DR   EnsemblMetazoa; AGAP002246-RA; AGAP002246-PA; AGAP002246.
DR   GeneID; 1269315; -.
DR   KEGG; aga:AgaP_AGAP002246; -.
DR   VEuPathDB; VectorBase:AGAP002246; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   HOGENOM; CLU_001226_3_0_1; -.
DR   InParanoid; Q7QKB2; -.
DR   OMA; ARSITPI; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000007062; Chromosome 2R.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd12304; RRM_Set1; 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; 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:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007062};
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}.
FT   DOMAIN          105..178
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          1864..1981
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1987..2003
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..1331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1357..1614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1626..1677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1750..1774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..215
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..503
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..552
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..629
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..659
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..741
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..985
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1045
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1086
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1159..1200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1242..1268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1269..1311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1314..1331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1434..1448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1482..1507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1523..1537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1544..1575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1589..1614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2003 AA;  217674 MW;  8B36143ED3DEBF17 CRC64;
     MNGTVENNPM ANAPPLPGAS PAASMVAQQK AARNFKLLVD PFLHRGTQKI YRYDGVVPGD
     PNHPPVIPRD PRNPLARIRS RVEPLDIPVP RFKIDQHYVG EPPAIEITIT NLNDNIDKPF
     LSDMLAKCGT FTELYIYYHP VSNKHLGLAR IVFEQVRSAL LCVEKLNGTS VMGKVLNVFK
     DPFGEQCKRI LQEKTSEKKP SQPQPPLPPL PPASTNHHSL VPNASVGDPL GLKASLSSRP
     PAPYRKAPPE PDHAPEPWEK KGHQTLGEDS ELWDGDEFSG SAGNSQDSSY YSKEKSASRS
     QYGGEWDDDG RSRDGKYYDE KERKHHHHHK SDRVRDRDRE REKDRDRYRD RERDRDRDRD
     RDRERDRDRE RTRDRHRDRD RTRERDRDRT RDREYRDREF DSKKRNKSYR DSWYGGETEG
     YTGGSRYEGG AAYDYYSTPS AYTGSAEYGS TYGYPPSESS YGTPSSSAAK WAPPQPPAPP
     PPPPPEENWD SASKPPAPPP LPIGGSSSSN ASKTILDEGE LWDTDTVPSS TGTKAAPPLP
     VSSPPPEPKA PKGPGANDED SGSTLDLDTR IALLFKEKTF GGSFLQLSDD EEEDRKQEIV
     PGSGGATAED STHPDTSHLK EEPMDLDDAV SISHRPPSPP PPMEAAQPPP PLPPPTDEES
     NEPKQPKREP KIECLKEEGA SDISSSDDEI LAKDEDENSR SMPPGEAKLA SLDDAKLGPL
     QPAAPPLPTE PAPAVPPPPE PIEGAGFSFL YPTNQYYSYG AQPASATSAY YPGYPTGFPG
     APLFNSYGMP ASGGMYYASG KSADDGPSAL LEAAGAAGMK DRARGTKRNR YEVVIDAVVE
     RVVTELKQIL KKDFNKKMIE NTAFKKYEAW WDEEERKHKG GAGKSAAGES SGLAGTSAGA
     AGTVGGATVA GVALKIEKPP DINHLLSQTY DNLDSNSGGF VGLGLRATIP KMPSFRRIRK
     QPSPVPQDED SRKSDQDDMV RGSDSEKESS SGGGGGSGGA AAGPSTASGS GESSSAGKGR
     DAEQSSPSHM TPSSSSSSSR AGGVSSDSAP GRIAPAATSS AVPGSSRATE KRMPSVSSFT
     SSSEEEESSV SDSDDSLESG SLSDVDTNAV TAAAGYGAKR ARERRERENR IYSDSDSDTG
     ETQPIKARPG NSFAVRRLKE GGKVGKIYSD SDSDEVRAPP RKEVLPAVST ERRRSRTRSP
     LDGLVKPAGE KPTRPVDSSQ LPKLSLQELH EDFSPSSGDE MLLMSDDRDE QKEQDEEEKR
     KQSKEHQEAP QQTPRTPGRE SPKTANSNSV TASNSDSNRQ NHQSSSAYGM LDRIYSDSDE
     EREYQEKRRR KAECLQQIDK ECMEEWERMA VEIGARKERD AGLARGKTLA SLDSKKAFAS
     GGKMSSLDEP LTPNLTQPPP TPGAGLGELR KHPLNSLFPG STTDGEGADQ KEGGAKEQTT
     SLPSTSAKKR KSGGAAAVGR PPKGAARKGG VKEELNGSEP LPVAQGESTA TTTVRTALVS
     SSSDDFFMPG DESVRRAAKA SPASSDGGSS QASQVALDHC YSLPPSASPS SSSPQQQSDS
     STTATNSTHT NKYAPTSKHV LAHDHGYTNS NDGGEQQPVA PNSTSTLPPL GSDAASNATT
     VIMTVTPQPA GSDHPSADGG SAAMKPPIPA KQKNLERKQR QSLSFSDYDP DTAMQQQQQV
     ERFVPVPKYR PRELATEMGI LFDFLTRGVD AEDVRYIRQS YDMLLMDDAS SYWLNATHWV
     DHCATDRNFE PALLAPPPSK RRKKDKGGAG GSSLADIKLH RTGCARTEGY YKIDPREKAK
     YKYHHLKGTV AANHLTNLEL AKAVAKMQGI SREARSNQRR LLNAFGASTE SELLKFNQLK
     FRKKQLKFAK SAIHDWGLFA MEPIAADEMV IEYVGQMVRP SVADLRETKY EAIGIGSSYL
     FRIDMETIID ATKCGNLARF INHSCNPNCY AKVITIESEK KIVIYSKQPI GVNEEITYDY
     KFPLEDEKIP CLCGAPGCRG TLN
//
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