ID V2XNW1_MONRO Unreviewed; 440 AA.
AC V2XNW1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Aminotransferase class-iii {ECO:0000313|EMBL:ESK95442.1};
GN ORFNames=Moror_996 {ECO:0000313|EMBL:ESK95442.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK95442.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK95442.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95442.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK95442.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWSO01000082; ESK95442.1; -; Genomic_DNA.
DR RefSeq; XP_007845256.1; XM_007847065.1.
DR AlphaFoldDB; V2XNW1; -.
DR STRING; 1381753.V2XNW1; -.
DR KEGG; mrr:Moror_996; -.
DR HOGENOM; CLU_016922_10_0_1; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:ESK95442.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transferase {ECO:0000313|EMBL:ESK95442.1}.
SQ SEQUENCE 440 AA; 47611 MW; EB09C8F5B30A9DBD CRC64;
MTTPSLNEDS TFWTAADASL IRYGGPFIRR IIERAEGIYL YDADGKSIID FTSGQMSSIL
GHGHPEIVSV INKYAKDLDH LFSGMLSRPV VDMATKLAGL LPPGLDKVQL LSTGGESNEC
AIRIAKLYTG KFEIVALSNS WHGVTQAAAS VTYQPTRKNY GPASVGSLVL PSPNAYRSPF
RKPDGTYDWE AELDYGFSLV DTLSVGSLAA VIVEPILSSG GVIPLPFGYL RRLKEHCVRR
GMLLIVDEAQ TGIGRTGKNF AFEHEGVVPD ILTLSKTLGA GLPLSAVVTS CEIEENIFSK
GFSFYTTHVS DPLPAAVGLK VLEILTREDL AGRAARLGAI FRDFLLDLQS RYHCIGDVRG
QGLMIGFEIV KNRSTKEPDE HLGAVLADRM MELGLSANVL RIPGTGSCFR IAPALTITEE
ELKMGLGIIE EAFKTTPGVE
//
