ID   A0A1B8AJJ9_FUSPO        Unreviewed;      1059 AA.
AC   A0A1B8AJJ9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Adenylosuccinate lyase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FPOA_06992 {ECO:0000313|EMBL:OBS20647.1};
OS   Fusarium poae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS20647.1, ECO:0000313|Proteomes:UP000091967};
RN   [1] {ECO:0000313|EMBL:OBS20647.1, ECO:0000313|Proteomes:UP000091967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2516 {ECO:0000313|EMBL:OBS20647.1,
RC   ECO:0000313|Proteomes:UP000091967};
RA   Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA   Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT   "Living apart together: crosstalk between the core and supernumerary
RT   genomes in a fungal plant pathogen.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OBS20647.1}.
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DR   EMBL; LYXU01000003; OBS20647.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8AJJ9; -.
DR   STRING; 36050.A0A1B8AJJ9; -.
DR   Proteomes; UP000091967; Unassembled WGS sequence.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:InterPro.
DR   CDD; cd01597; pCLME; 1.
DR   Gene3D; 1.10.3020.20; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
DR   InterPro; IPR005674; CocE/Ser_esterase.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR000383; Xaa-Pro-like_dom.
DR   InterPro; IPR013736; Xaa-Pro_dipept_C.
DR   NCBIfam; TIGR00976; CocE_NonD; 2.
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   Pfam; PF02129; Peptidase_S15; 1.
DR   Pfam; PF08530; PepX_C; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SMART; SM00939; PepX_C; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000091967}.
FT   DOMAIN          326..585
FT                   /note="Xaa-Pro dipeptidyl-peptidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00939"
FT   DOMAIN          973..1052
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
SQ   SEQUENCE   1059 AA;  117783 MW;  7C4B8892BEB7F863 CRC64;
     MPFTVGGIKV LQRDSPSPAL PHAQYPGLKT ETVVLRQGHQ KDPSRKAFRV DTILEKDIEV
     VTRNGHILRA DVYRPAETNP KDQVPALLAW SPYGKSGTGA FTLDIIPRRV GVTLAQTSGY
     ESFEALDPAE WTARGYAIVN INPKGSFDSE GDLVWHSTEG GRNGYDVIEH LAKLPWCSGK
     ISLVGNSWLA MVQWFIAAAM PPHLTCIAPL EGSSDIYRES LCRGGVPNKA FWGYLQDCLF
     GSHKAEDIVG MLDRYPLQNA YWADKRADMS KINIPAYVLA SYSTALHTVG SFRGFEEIPH
     DKKWLRVHST QEWYDLYSDE CVEDLQSFFD RYLKDKQNGW EETPRVRLST LAFNKDPEVN
     HHFADWPLPE TNYTTLYLSD DNRLVSAPSS KAAALSYQSD VPDMQMDAQV EELSFEYTFE
     ERTYLIGYPR AVLYMSTEDS NDMDVFVSLR KADSKGNVLR NINIPLKDLG MEADEVPLVN
     SLVYTGPSGI LRASHRKVDA SKSKPYWPFH PHDEKELLEP GQIVKLDIGL WPAGIVFEAG
     EKLMLRVAGH HMVLAEFEPL RGAFQTDNRG RHNVHVGPQY QSHVILPFAD SDVVYRKARQ
     PGAFRAMGSI SAFDSVIFRN LLGTDQVREI FSDKAYISRC IDAETALARA QASCGLIPKE
     AAACITEKCD ISVLDLDKLR QETDIVGYPI LPLVKQLSAV IGQEGRYLHW GATTQDIMDT
     AHMLQMKQGL QLVRHHIDAV IAALEKLSRD FRSTPMAGRT HLQHALPVTF GYKCAVWLSS
     FYRHRERLDQ LEPRSLLVQY GGAAGTLASL GPGRKGIQVR KAMAAETGLH DSTITWHVAR
     DGVAEIANFL ALVGGSLGKI ALDLMIMCSN ELSEVAEPFV PHRGASSTMP QKRNPISSEV
     MLAASKSLRS NASLVLDGMV TDFERASGPW HLEWIAIPEL FVMAVGALNQ ASFVLSGLDV
     DEENMARNLY STKGLIVGEA VMMGLAPFIG RQDAHDVVYQ ACKQAIEEKM TLHQVLKGMP
     EVTDKISDKQ LEELCDPVNY LGSCREMVDD TLALSKGQE
//