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NA30A_DROME
ID   NA30A_DROME             Reviewed;         377 AA.
AC   Q95RC0; O46309; Q9W5A3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=N-alpha-acetyltransferase 30A;
DE            EC=2.3.1.-;
DE   AltName: Full=N-acetyltransferase MAK3 homolog;
DE   AltName: Full=NatC catalytic subunit;
GN   Name=Naa30A {ECO:0000312|FlyBase:FBgn0024362};
GN   ORFNames=CG11412 {ECO:0000312|FlyBase:FBgn0024362};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oregon-R;
RX   PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA   Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA   Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA   Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA   Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA   Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA   Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA   McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA   Glover D.M.;
RT   "From sequence to chromosome: the tip of the X chromosome of D.
RT   melanogaster.";
RL   Science 287:2220-2222(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Probable catalytic component of a complex displaying alpha
CC       (N-terminal) acetyltransferase activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. MAK3 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA17683.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AE014298; AAN09042.1; -; Genomic_DNA.
DR   EMBL; AL022018; CAA17683.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY061492; AAL29040.1; -; mRNA.
DR   PIR; T13614; T13614.
DR   RefSeq; NP_726727.1; NM_166878.3.
DR   AlphaFoldDB; Q95RC0; -.
DR   SMR; Q95RC0; -.
DR   BioGRID; 57639; 3.
DR   DIP; DIP-19808N; -.
DR   IntAct; Q95RC0; 3.
DR   STRING; 7227.FBpp0070203; -.
DR   DNASU; 31079; -.
DR   EnsemblMetazoa; FBtr0070209; FBpp0070202; FBgn0024362.
DR   GeneID; 31079; -.
DR   KEGG; dme:Dmel_CG11412; -.
DR   UCSC; CG11412-RA; d. melanogaster.
DR   CTD; 31079; -.
DR   FlyBase; FBgn0024362; Naa30A.
DR   VEuPathDB; VectorBase:FBgn0024362; -.
DR   eggNOG; KOG3139; Eukaryota.
DR   GeneTree; ENSGT00390000005665; -.
DR   InParanoid; Q95RC0; -.
DR   OMA; AAHDNQY; -.
DR   OrthoDB; 1323575at2759; -.
DR   PhylomeDB; Q95RC0; -.
DR   BioGRID-ORCS; 31079; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 31079; -.
DR   PRO; PR:Q95RC0; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0024362; Expressed in mouthpart and 27 other tissues.
DR   ExpressionAtlas; Q95RC0; baseline and differential.
DR   Genevisible; Q95RC0; DM.
DR   GO; GO:0031417; C:NatC complex; ISS:FlyBase.
DR   GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:FlyBase.
DR   GO; GO:0016573; P:histone acetylation; IMP:FlyBase.
DR   GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; ISS:FlyBase.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR044542; NAA30-like.
DR   PANTHER; PTHR45896; PTHR45896; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..377
FT                   /note="N-alpha-acetyltransferase 30A"
FT                   /id="PRO_0000320035"
FT   DOMAIN          229..377
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          1..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   377 AA;  42250 MW;  ACE9AB010249D932 CRC64;
     MADAQAAAAG KKKYKNKKNS AEKNPNHNPN SSGQVEAQTP SNGHVQHQEE EATEDQEPAQ
     ELRGLLKKMH LCNGHGHKEQ EARPLGEVVN GHAHGHSNNN HIRCTSGSSN NNNSTHNNNS
     VDSSNNNRKQ RREGGDGGGS DSNSLKPEEK PITATSKTTA NIHPTTTTDP KPKVSEDVAV
     EQGVHVATGS GHSREQERKQ PPSDYAEGAT PTITAQLQLP EPAISADEIV YKEYEAEHQM
     HDIMRLIQAE LSEPYSIYTY RYFIYNWPKL CFLASHDNQY VGAIVCKLDM HMNVRRGYIA
     MLAVRKEYRK LKIGTTLVTK AIEAMLADNA DEVVLETEMR NQPALRLYEN LGFVRDKRLF
     RYYLNGVDAL RLKLWFR
 
 
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