ID N1QFE3_SPHMS Unreviewed; 479 AA.
AC N1QFE3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:EMF10457.1};
GN ORFNames=SEPMUDRAFT_150559 {ECO:0000313|EMBL:EMF10457.1};
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:EMF10457.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF10457.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF10457.1,
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; KB456267; EMF10457.1; -; Genomic_DNA.
DR RefSeq; XP_016758578.1; XM_016906257.1.
DR AlphaFoldDB; N1QFE3; -.
DR STRING; 692275.N1QFE3; -.
DR GeneID; 27903394; -.
DR eggNOG; KOG0257; Eukaryota.
DR HOGENOM; CLU_034385_1_0_1; -.
DR OMA; KNWRYPG; -.
DR OrthoDB; 5474881at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EMF10457.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Transferase {ECO:0000313|EMBL:EMF10457.1}.
FT DOMAIN 91..431
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 53577 MW; 4EFC1E44E8EB2E94 CRC64;
MSGIAFRGGN QGEHPPMQGH KPTTTKARRF STAQGPSNDE INSAIHLQFR QAHEGHKPHA
GLDPSRASTG VIWCTERAYE HGFADDPSSW ANLGQGAPEV DDEIEGCFKR PQTIDISMTG
REYGPTAGIK PLREAVAKLY NEHHRKGKES QYTWENVCIV PGGRAGLIRI AAILGNAYLG
FFIPDYTAYN EMLSLFKNFT PLPIPLNKND NYQIHAEKIE DEISRGTSVI LTSNPRNPTG
KMIAKGELAE IQDLCRDRAT LIMDEFYSGY NYTSDCDGSV VSAAENVEDV DDDGVLIIDG
LTKRFRLPGW RVAWILGPKE FCKALGSCGS YLDGGTNVPF QEAAVPMLEP DNVRAEMKAL
QLHFRMKRDY VVDRLQKMGF KLSYTPDSTF YLWLNLEHLP HSINDGLNFF QACLREKVIV
VPGIFFDLNP ARRRDLFDSP CHHYVRISYG PVLSTLVKGM DGIERVLQKH GAYSDDESE
//
