ID M1W9V2_CLAP2 Unreviewed; 532 AA.
AC M1W9V2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE SubName: Full=Probable adenylosuccinate lyase {ECO:0000313|EMBL:CCE30033.1};
GN ORFNames=CPUR_03881 {ECO:0000313|EMBL:CCE30033.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE30033.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE30033.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE30033.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE30033.1}.
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DR EMBL; CAGA01000018; CCE30033.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W9V2; -.
DR STRING; 1111077.M1W9V2; -.
DR VEuPathDB; FungiDB:CPUR_03881; -.
DR eggNOG; KOG2700; Eukaryota.
DR HOGENOM; CLU_030949_1_1_1; -.
DR OrthoDB; 460764at2759; -.
DR PhylomeDB; M1W9V2; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:InterPro.
DR GO; GO:0009152; P:purine ribonucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd03302; Adenylsuccinate_lyase_2; 1.
DR Gene3D; 1.10.275.60; -; 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; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR004769; Pur_lyase.
DR NCBIfam; TIGR00928; purB; 1.
DR PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF10397; ADSL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000313|EMBL:CCE30033.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016801}.
FT DOMAIN 421..505
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
FT COILED 5..32
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 532 AA; 59373 MW; 2087E4D79B9D92E3 CRC64;
MTDQAQDAQT QIQELQKKIM QLQAQVEEPQ KSPYDTYQTS LTSRYCSNEM TSLFSQRSRH
STWRKLWLGL AEAEASLGID VVTAEALDQM RAHLTVSDED FATASIEEKI RRHDVMAHVH
AFGVVAPAAA GIIHLGSTSC FVTDNTELIL MRDALDILLN KLAKVISNLA AFANRWKSEP
TLGLTHDQPA QPITVGRRAA QWAQDLMMDL EAIEAVRSGL KFRGAQGTTG TQASFLEIFQ
GDHTKCDRLN ELLCEKFGFR ACYDISTQTY TRKVDLIVAN AVAGLAVSAH KMCTDIRLLA
SNKEIEEPKE ASQIGSSGKS HRTLIIFRAS SVMKSMPYKR NPMRSERICS LSRALKAKPA
SFANTMSTQW FERTLDDSAI RRIDIPEMFL LADAILIGLD NVSDGLVVYP KRIRSRILEE
LPFMVTEAII MKLVAKGASR QEAHEKIRVL SNQASSTVKD EGKPNDLIER IRGNEYFKPI
WGELDSMLQP ELYIGRCPEI VNKFCGPGGV VEKALAPYQQ YILKSTTAQL NV
//
