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Database: UniProt
Entry: M3AVT1_SPHMS
LinkDB: M3AVT1_SPHMS
Original site: M3AVT1_SPHMS 
ID   M3AVT1_SPHMS            Unreviewed;       305 AA.
AC   M3AVT1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|Pfam:PF13302};
GN   ORFNames=SEPMUDRAFT_71351 {ECO:0000313|EMBL:EMF10186.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF10186.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF10186.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF10186.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC       {ECO:0000256|ARBA:ARBA00009342}.
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DR   EMBL; KB456268; EMF10186.1; -; Genomic_DNA.
DR   RefSeq; XP_016758307.1; XM_016909936.1.
DR   AlphaFoldDB; M3AVT1; -.
DR   GeneID; 27907073; -.
DR   eggNOG; KOG4135; Eukaryota.
DR   HOGENOM; CLU_073102_0_0_1; -.
DR   OMA; HETHDIQ; -.
DR   Proteomes; UP000016931; Unassembled WGS sequence.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR039135; NAT9-like.
DR   PANTHER; PTHR13256:SF16; ALPHA_BETA-TUBULIN-N-ACETYLTRANSFERASE 9; 1.
DR   PANTHER; PTHR13256; N-ACETYLTRANSFERASE 9; 1.
DR   Pfam; PF13302; Acetyltransf_3; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          14..258
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13302"
FT   REGION          72..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..164
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  33393 MW;  8A509C1CBB4264A2 CRC64;
     MKINEHTALS SRSILLVPYS PHHVPTYHQW MQDPDLQAAT ASEPLSLEEE YAMQRSWRLD
     SDKLTFIICR PRDETSSSSS SSSTTTTTTT TPGSSSSSSS DREKETQEEK VQKDQITATK
     DDSPDRMIGD INLFLFPLDS SSSPSPPSPP SSEAIPPPPP PPKILGEIEI MIADKSSQRK
     GHGKTSLLIF LDYILEHWSL IGREFSSSFS SSSSSSSDPS TSFSAAAAAI SPQLAYLRVK
     VHETNVGSIR LFESVGFQRV SETANYFGEI EMRWYTTGDG DGGGHTGGEK ARELPYRMEA
     VTESS
//
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