ID   A0A0B4HZ95_METMF        Unreviewed;       321 AA.
AC   A0A0B4HZ95;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=HpcH/HpaI aldolase/citrate lyase family protein {ECO:0000313|EMBL:KID95521.1};
DE   Flags: Fragment;
GN   ORFNames=MAJ_08547 {ECO:0000313|EMBL:KID95521.1};
OS   Metarhizium majus (strain ARSEF 297).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC   Metarhizium majus.
OX   NCBI_TaxID=1276143 {ECO:0000313|EMBL:KID95521.1, ECO:0000313|Proteomes:UP000031176};
RN   [1] {ECO:0000313|EMBL:KID95521.1, ECO:0000313|Proteomes:UP000031176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 297 {ECO:0000313|EMBL:KID95521.1,
RC   ECO:0000313|Proteomes:UP000031176};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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:KID95521.1}.
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DR   EMBL; AZNE01000074; KID95521.1; -; Genomic_DNA.
DR   RefSeq; XP_014574515.1; XM_014719029.1.
DR   AlphaFoldDB; A0A0B4HZ95; -.
DR   HOGENOM; CLU_059964_2_1_1; -.
DR   OrthoDB; 1822991at2759; -.
DR   Proteomes; UP000031176; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR   PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KID95521.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031176}.
FT   DOMAIN          39..232
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   REGION          286..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KID95521.1"
SQ   SEQUENCE   321 AA;  34586 MW;  23B2DD18B00F0D85 CRC64;
     MLDTNHYNAL SLAQPTNFKS MLHSGKLLWG TGCRIPHEEA ARIVASTPYH FCFIDAEHTP
     LNATLLVSLV RTIQYHSNGS MVPFVRIPGC SPELVNYALN AGAGGVMMPH IQNAKQAEDL
     VRLARFPPMG DRSFPPAALI NKKQQRTPES QTVYDVWNNH AAVICQIEDL QGLDNIEEIC
     RVPGVDGLFI GTGDLRMCMG LAVGSLDGDE AVFVSALRRI RDAAKANDLP IMGFGISPCT
     LERRIDMGWN AFIIHGDIDA ICTSAIRSLD TYSDAADRCL SKTSGKNGNG SANGLDDDLG
     SKTREEGAVG SLNGSGFVGP Q
//