ID G9NRK0_HYPAI Unreviewed; 293 AA.
AC G9NRK0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=HpcH/HpaI aldolase/citrate lyase domain-containing protein {ECO:0000259|Pfam:PF03328};
DE Flags: Fragment;
GN ORFNames=TRIATDRAFT_179014 {ECO:0000313|EMBL:EHK46633.1};
OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK46633.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK46633.1, ECO:0000313|Proteomes:UP000005426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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:EHK46633.1}.
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DR EMBL; ABDG02000022; EHK46633.1; -; Genomic_DNA.
DR RefSeq; XP_013944828.1; XM_014089353.1.
DR AlphaFoldDB; G9NRK0; -.
DR STRING; 452589.G9NRK0; -.
DR GeneID; 25777059; -.
DR eggNOG; ENOG502SJMS; Eukaryota.
DR HOGENOM; CLU_059964_2_0_1; -.
DR OMA; IVHEAIF; -.
DR OrthoDB; 1822991at2759; -.
DR Proteomes; UP000005426; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005426}.
FT DOMAIN 39..232
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHK46633.1"
FT NON_TER 293
FT /evidence="ECO:0000313|EMBL:EHK46633.1"
SQ SEQUENCE 293 AA; 32213 MW; 35934A65D6AC3D5C CRC64;
PEPSAGMAAY AATSLFQPHH ARQAIRDAHK KKIPPLLGYY CGLGSQKITR WVAPLNFDVV
WVDWEHSSMN VETMTTIVHE AIFMSHGKTI PFVRVPGHDH AAIGYALDAG ASLVIPQVES
VEQAKHVVSA AKFGSKQNGS RSAPPFRLFP GVTDRPFEEG RDIFEALNHQ AAIMIQIESL
AGINNLDAIL TEVPDIDMVW LGTLDCRVEM NMPSNMGMGG TEPEWLEARQ KFFDVLDKHD
KPYGGFAFPN PPFGGEESFK KAAERMSFIM AAADTLALAG MGEILKMSRE YVA
//
