ID A0A194UNF3_9PEZI Unreviewed; 340 AA.
AC A0A194UNF3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 03-MAY-2023, entry version 17.
DE RecName: Full=protein-ribulosamine 3-kinase {ECO:0000256|ARBA:ARBA00011961};
DE EC=2.7.1.172 {ECO:0000256|ARBA:ARBA00011961};
GN ORFNames=VP1G_00818 {ECO:0000313|EMBL:KUI53183.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI53183.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-D-ribulosyl-L-lysyl-[protein] = ADP + H(+) + N(6)-
CC (3-O-phospho-D-ribulosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:48432,
CC Rhea:RHEA-COMP:12103, Rhea:RHEA-COMP:12104, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:90418, ChEBI:CHEBI:90420,
CC ChEBI:CHEBI:456216; EC=2.7.1.172;
CC Evidence={ECO:0000256|ARBA:ARBA00001616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48433;
CC Evidence={ECO:0000256|ARBA:ARBA00001616};
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; KN714668; KUI53183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194UNF3; -.
DR OrthoDB; 2101593at2759; -.
DR Proteomes; UP000078576; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0102193; F:protein-ribulosamine 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR016477; Fructo-/Ketosamine-3-kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR12149; FRUCTOSAMINE 3 KINASE-RELATED PROTEIN; 1.
DR PANTHER; PTHR12149:SF8; PROTEIN-RIBULOSAMINE 3-KINASE; 1.
DR Pfam; PF03881; Fructosamin_kin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KUI53183.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078576};
KW Transferase {ECO:0000313|EMBL:KUI53183.1}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 38780 MW; AB186515FA380AD0 CRC64;
MSDDSEYSTS SQGGGSIANH SDGLKIQADE LDERVLAATG GTSQRMMQGC FESEGIFHAY
APMNVQKPVA FGNYKTNPET WFFLAEFYDM LDKVPEPSQF VPLIANIHKA SMGKSPNGKH
GFQVPTHLAN IPNDNTWQDT WEVFFTQLMK KMFEQEELAH GKDDRVEYLK EALYEKVIPR
LLRPLETEGR SIQPCLIHSD IWPGNLKLDV ETKKVILFDS CAFWGHNEAD LGTWRAPRYR
MGRPFFREYQ RAMQISEPQE DWNDRNALYA LRYDLLVSAL FPDDGGLKFR DLAMVELERL
VAKYPEGYDG YHSTRTATLL SGKTEVETLP SSTVEEVLVK
//