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Database: UniProt
Entry: C4JKN9_UNCRE
LinkDB: C4JKN9_UNCRE
Original site: C4JKN9_UNCRE 
ID   C4JKN9_UNCRE            Unreviewed;       324 AA.
AC   C4JKN9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=HpcH/HpaI aldolase/citrate lyase domain-containing protein {ECO:0000259|Pfam:PF03328};
GN   ORFNames=UREG_00637 {ECO:0000313|EMBL:EEP75790.1};
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP75790.1, ECO:0000313|Proteomes:UP000002058};
RN   [1] {ECO:0000313|Proteomes:UP000002058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CH476615; EEP75790.1; -; Genomic_DNA.
DR   RefSeq; XP_002541123.1; XM_002541077.1.
DR   AlphaFoldDB; C4JKN9; -.
DR   STRING; 336963.C4JKN9; -.
DR   GeneID; 8438658; -.
DR   KEGG; ure:UREG_00637; -.
DR   VEuPathDB; FungiDB:UREG_00637; -.
DR   eggNOG; ENOG502QQPK; Eukaryota.
DR   HOGENOM; CLU_044864_1_1_1; -.
DR   InParanoid; C4JKN9; -.
DR   OMA; AWLFCPA; -.
DR   OrthoDB; 2874421at2759; -.
DR   Proteomes; UP000002058; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR32308:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002058}.
FT   DOMAIN          9..244
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         137
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   324 AA;  35443 MW;  C86CBEE526AF60D4 CRC64;
     MAANNVLRRA LFYVPGSNRR MLEKSRSIAV DCVAYDLEDS VTFSQKDEAR KMVRNEIDQT
     KPDSIREQSV RINSVGSGLA EKDLEQMLQS PNLSTIVVPK VDSASDLRFV HDMVHHALST
     AAPSTPRTPI SILALIESAK SLTNLSEICT ASPLLSGLIF AAEDFALDLN LTRTPSLSEF
     LYARSAIVTA ARAHNIPSVI DLVCTSYSSR TAANPEDKRA VDILKAEAQG GKRLGFNGKQ
     CIHPTQVPIV QDTFSPEMEE LQWAVRVSIA DEKAARQGRG AWSLGGKMID VPVAEKARVI
     VKKAVACGMD VEAVKREWID QEPE
//
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