GenomeNet

Database: UniProt
Entry: K1WS67_MARBU
LinkDB: K1WS67_MARBU
Original site: K1WS67_MARBU 
ID   K1WS67_MARBU            Unreviewed;       276 AA.
AC   K1WS67;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=HpcH/HpaI aldolase/citrate lyase family protein {ECO:0000313|EMBL:EKD15896.1};
GN   ORFNames=MBM_05907 {ECO:0000313|EMBL:EKD15896.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD15896.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD15896.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD15896.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH921440; EKD15896.1; -; Genomic_DNA.
DR   RefSeq; XP_007293796.1; XM_007293734.1.
DR   AlphaFoldDB; K1WS67; -.
DR   STRING; 1072389.K1WS67; -.
DR   GeneID; 18761842; -.
DR   KEGG; mbe:MBM_05907; -.
DR   eggNOG; ENOG502QR7H; Eukaryota.
DR   HOGENOM; CLU_059964_3_0_1; -.
DR   InParanoid; K1WS67; -.
DR   OMA; WNRVDDY; -.
DR   OrthoDB; 2785075at2759; -.
DR   Proteomes; UP000006753; 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:EKD15896.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT   DOMAIN          33..249
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   276 AA;  29240 MW;  FDEE93AAB1DCBDB9 CRC64;
     MATTMQRANR LKTAFDAAKG PSMGCWQMFP GSNVSRTLAR TGVDWVLVDC EHGNMDDAAM
     HEAVPAIAAC GVSPIVRIPD NQGFLVKRAL DSGAHGVLVP LLYTVEDAKK LVKSAKFPPA
     GQRGFGSPFP HERFSPSLGS TDYLQQANDA ILVMVQIETK EALDDVDAIA AVPGVDVLFV
     GPFDLGNNIG HPIIEGKMDD NLHAAIKKVL EASRKAGKKA GIFCTSGDQS KGYADMGFDM
     ISCATDVMIL QASVMGALYT AKGLGEVPKL TGPYGK
//
DBGET integrated database retrieval system