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Database: UniProt/TrEMBL
Entry: Q2PBA9_ACYPI
LinkDB: Q2PBA9_ACYPI
Original site: Q2PBA9_ACYPI 
ID   Q2PBA9_ACYPI            Unreviewed;       418 AA.
AC   Q2PBA9;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   05-JUL-2017, entry version 83.
DE   SubName: Full=Putative H3K9 methyltransferase {ECO:0000313|EMBL:CAJ18343.1};
GN   Name=su(var)3-9 {ECO:0000313|EMBL:CAJ18343.1};
OS   Acyrthosiphon pisum (Pea aphid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha;
OC   Aphidomorpha; Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon.
OX   NCBI_TaxID=7029 {ECO:0000313|EMBL:CAJ18343.1};
RN   [1] {ECO:0000313|EMBL:CAJ18343.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Krauss V., Fassl A., Fiebig P., Patties I., Sass H.;
RT   "The evolution of the histone methyltransferase gene Su(var)3-9 in
RT   metazoans includes a fusion with and a re-fission from a functionally
RT   unrelated gene.";
RL   BMC Evol. Biol. 6:18-18(2006).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000256|SAAS:SAAS00591578}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|SAAS:SAAS00563877}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00574581}.
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DR   EMBL; AM050261; CAJ18342.1; -; Genomic_DNA.
DR   EMBL; AM050262; CAJ18343.1; -; mRNA.
DR   RefSeq; NP_001119634.2; NM_001126162.2.
DR   UniGene; Aps.14615; -.
DR   UniGene; Aps.48322; -.
DR   UniGene; Aps.51163; -.
DR   ProteinModelPortal; Q2PBA9; -.
DR   GeneID; 100161603; -.
DR   KEGG; api:100161603; -.
DR   CTD; 41483; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000231244; -.
DR   KO; K11419; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR011381; Histone_H3-K9_MeTrfase.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF009343; SUV39_SET; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Chromosome {ECO:0000256|SAAS:SAAS00508265};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009343-2};
KW   Methyltransferase {ECO:0000256|SAAS:SAAS00590675,
KW   ECO:0000313|EMBL:CAJ18343.1};
KW   Nucleus {ECO:0000256|SAAS:SAAS00574642};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR009343-1,
KW   ECO:0000256|SAAS:SAAS00591079};
KW   Transferase {ECO:0000256|SAAS:SAAS00591533,
KW   ECO:0000313|EMBL:CAJ18343.1}; Zinc {ECO:0000256|PIRSR:PIRSR009343-2}.
FT   DOMAIN       10     69       Chromo. {ECO:0000259|PROSITE:PS50013}.
FT   DOMAIN      201    263       Pre-SET. {ECO:0000259|PROSITE:PS50867}.
FT   DOMAIN      268    394       SET. {ECO:0000259|PROSITE:PS50280}.
FT   DOMAIN      402    418       Post-SET. {ECO:0000259|PROSITE:PS50868}.
FT   REGION      279    281       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR009343-1}.
FT   REGION      351    352       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR009343-1}.
FT   METAL       203    203       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       203    203       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       205    205       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       209    209       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       245    245       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       245    245       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       249    249       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       251    251       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       255    255       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       354    354       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       406    406       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       408    408       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       413    413       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   BINDING     393    393       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR009343-1}.
FT   BINDING     407    407       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR009343-
FT                                1}.
SQ   SEQUENCE   418 AA;  47990 MW;  AA5F49B147053A5B CRC64;
     MHKGVADNEY EIESILFDDT YGSKTMYLVK WKNYPMDQCT WEPYRNLTNC TQALNDYRSN
     KIVATEIYQT ARYKELYDSL NIFADQELLE LLHHVIQDGM PSIDDKFVRG TIAYLSTVSP
     SSRSSSLTKL IRHNLMIIEV DKKRQKQQER LNKWQNDMAR VCGFNLSVLN NVDFEGPPKR
     FYYVDECVAG KGVVIPNDPP VWCHCDVTCG GKKRKKTECH FGDFQLAYNK FKRIIVPQGT
     PIYECNRKCT CDATCVNRVV QHGPSKNLKL QIFRTDNNRG WGVKTLLSIK QGTYITKYTG
     EVITRSEADQ RAVTHGSKST YLFDLDYNTE KNDSVYSIDA TTYGNVSHFI NHSCDSNLAI
     FAVWIDCLDT NIPTLALFAS RDISAGEEIT FNYMTSVNNE NRRIKCKCLS DNCRGYLC
//
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