ID A0A428P8M9_9HYPO Unreviewed; 904 AA.
AC A0A428P8M9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RSL49412.1};
GN ORFNames=CEP54_012433 {ECO:0000313|EMBL:RSL49412.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL49412.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL49412.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL49412.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase
CC family. {ECO:0000256|ARBA:ARBA00006477}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase
CC family. {ECO:0000256|ARBA:ARBA00009349}.
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:RSL49412.1}.
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DR EMBL; NKCI01000180; RSL49412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428P8M9; -.
DR STRING; 1325734.A0A428P8M9; -.
DR Proteomes; UP000288168; Unassembled WGS sequence.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR CDD; cd01065; NAD_bind_Shikimate_DH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR001381; DHquinase_I.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041121; SDH_C.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR21090:SF27; QUINATE REPRESSOR PROTEIN; 1.
DR Pfam; PF01487; DHquinase_I; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR Pfam; PF01202; SKI; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000288168}.
FT DOMAIN 563..643
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 705..747
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 847..876
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 28..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 99909 MW; 211DAE35763376F9 CRC64;
MAGVKRSLGT MLGHEDIMLR SNGLGKIRDH GNGISSRNSE AQTEQTQTLT LTETLHSQSR
NSSRSQSQSQ PPSTRQEQHD AVTRTPSPTF PPLTGEVPEF TPDASMLLAG IRGAGKSTLA
IMASSAMDRR VIDLETAFQK TSGLSSAAYK AEHGSAECYK HQAKVLQNAL DRHRTGCILV
CSWMESRVQN LLREFAATNP VIHIVRDADA IQNHLKFRDK AKIRNLLSVS NAIFRSCTNF
EFFNVSEKPA KSSLARISLK QRTPAPYLTL KHVERHFLKF LSLIYPTGTI PFMNSAFPLA
KIPPEDRQFT YATSIPLSDI LDESVDAEDH VNGADVVQIV VHDLADHAEA GTLTAETSNQ
LLADITRGIG VVRRSTILPI ILHLFLPHTA SDDVLRVYLD LLHHTLRLAP EMMTVDLRLE
DSHISRILAI RKRTKIIGNA FIITDPPPWE SPMWMNWYQK ANNLGCHLAR LIRPALTIED
NFRINYLRSS VDSLQGPKIP LISYNSGRLG RHSAALNSIL TVVRPDSLES VNPRPPITPC
ITAVGATKAL FSSFIHDEMK LYVFGTNVSY SLSPAMHRSA LKACGVPHTY EPVSSSSLQG
IRHLIEDSRF AGASIGLPFK VEIITLTHSL SNHARAIGAV NTLIPIRTLN EDGSIPTEAA
FFNNVNQSGP IKALYGENTD WIGIRACIRR GLSPANAVVS GTCGLVIGAG GMARATTYAM
LQVGIKNIVV YNRTPQNARK MVSHFTQLLQ RKDFKLLVSG SQGARFHVLE SLEDAWPEGF
RLPTVVVSCI PTHRIGNVPA PDLTLPDGWL GSRTGGVAIE LGYKTLDTPF LAQFRKESSR
GWVSMDGLDM LPEQGFAQFE FFTGRRAPRR IMRREVFQAY PDEEGKSNLE ELQPRLQSVD
EQEI
//
