ID A0A015IT77_RHIIW Unreviewed; 302 AA.
AC A0A015IT77;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE RecName: Full=protein-ribulosamine 3-kinase {ECO:0000256|ARBA:ARBA00011961};
DE EC=2.7.1.172 {ECO:0000256|ARBA:ARBA00011961};
GN ORFNames=RirG_179850 {ECO:0000313|EMBL:EXX60437.1};
OS Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX60437.1, ECO:0000313|Proteomes:UP000022910};
RN [1] {ECO:0000313|EMBL:EXX60437.1, ECO:0000313|Proteomes:UP000022910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA Huang S.;
RT "Single nucleus genome sequencing reveals high similarity among nuclei of
RT an endomycorrhizal fungus.";
RL Submitted (FEB-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 -!- SIMILARITY: Belongs to the fructosamine kinase family.
CC {ECO:0000256|PIRNR:PIRNR006221}.
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:EXX60437.1}.
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DR EMBL; JEMT01025927; EXX60437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A015IT77; -.
DR STRING; 1432141.A0A015IT77; -.
DR Proteomes; UP000022910; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-UniRule.
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 PIRSF; PIRSF006221; Ketosamine-3-kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|PIRNR:PIRNR006221};
KW Reference proteome {ECO:0000313|Proteomes:UP000022910};
KW Transferase {ECO:0000256|PIRNR:PIRNR006221}.
SQ SEQUENCE 302 AA; 34271 MW; 6E965FD888E9B2BF CRC64;
MSQIAQVILE TLQNNGICTK VLNKTALSGG CLNDAFKLST DTGNVFVKTN SGSNSRLMFE
GESESLNAIH EAVPGFAPKP LCFGTLPNEG AFIVTTYIRL STSNSASIQI LFARKLAEMH
SSQSPNGKFG FPVMTMCGIT EQDNTWEVDW PTFYKERRLR PILEKCLQNN PGDSELRRLG
EIVIDKVVDH IMKDIEIKPV LIHGDLWSGN WGVNLDANEP VIYDPSSCYG HNEYELGILT
MFGSPGSEFF REYHKYHPRQ EPYFEQRQEL YQLYHYLNHY YLFGGGYQRS AISIMRRLCD
LV
//
