ID K2QVQ7_MACPH Unreviewed; 461 AA.
AC K2QVQ7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Adenylosuccinate lyase C-terminal domain-containing protein {ECO:0000259|SMART:SM00998};
GN ORFNames=MPH_09008 {ECO:0000313|EMBL:EKG13826.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG13826.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG13826.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG13826.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC {ECO:0000256|ARBA:ARBA00034772}.
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:EKG13826.1}.
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DR EMBL; AHHD01000383; EKG13826.1; -; Genomic_DNA.
DR AlphaFoldDB; K2QVQ7; -.
DR STRING; 1126212.K2QVQ7; -.
DR VEuPathDB; FungiDB:MPH_09008; -.
DR eggNOG; KOG2700; Eukaryota.
DR HOGENOM; CLU_030949_3_1_1; -.
DR InParanoid; K2QVQ7; -.
DR OrthoDB; 1364594at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd01597; pCLME; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR InterPro; IPR019468; AdenyloSucc_lyase_C.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF2; ADENYLOSUCCINATE LYASE C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF10397; ADSL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 368..447
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 461 AA; 49824 MW; 1E329CEC61ED7D08 CRC64;
MSATTVFDSK LFGNIFGTEE IRQCFSERAY VANLIEAECA LAQAEAAEGV IPAEAAATIR
QHSDVSKVDW ELLAARTEIV GYPVLPLVEQ MSQWVPEEAS GYIHWGATTQ DIMDLASILQ
VKQGLSIVER HLLALQATLT SLATRYRDTP MAGRTHLQHA LPITFGYKCA VWLSSINRHL
ARLPSLKQTT LLAQFGGAAG TLASLGPSAA GLRVRRRVAA ILALRDPVVT WHVARDGVAD
CVNYLALVGG TLGKLALDLI VMSSNELGEV AEPYVPHRGA SSTMPQKRNP ISSEVMLAQS
KILRAQAGLV LDGMVSDFER ASGPWHLEWA AVPTAFVACV GALAQAVFAL AGLVVHERAM
MQNLVSTRGL ICAEAVMMGL ARWTGRQEAH EIVYRACVAA HEEGISLQES LERVPEVTRH
LKGQELEELC DPTKYLGCCQ LMIDELVGQV EAEGKSRAGE A
//
