ID A0A0D2BJ15_9EURO Unreviewed; 367 AA.
AC A0A0D2BJ15;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=protein-ribulosamine 3-kinase {ECO:0000256|ARBA:ARBA00011961};
DE EC=2.7.1.172 {ECO:0000256|ARBA:ARBA00011961};
GN ORFNames=PV06_10445 {ECO:0000313|EMBL:KIW37402.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW37402.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW37402.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW37402.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) 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};
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DR EMBL; KN847344; KIW37402.1; -; Genomic_DNA.
DR RefSeq; XP_016257618.1; XM_016411998.1.
DR AlphaFoldDB; A0A0D2BJ15; -.
DR GeneID; 27362519; -.
DR VEuPathDB; FungiDB:PV06_10445; -.
DR HOGENOM; CLU_036517_1_2_1; -.
DR OrthoDB; 2101593at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0102193; F:protein-ribulosamine 3-kinase activity; IEA:UniProtKB-EC.
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 Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT REGION 340..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 42046 MW; CFBE13267E6D141A CRC64;
MAESVRTLVE HQTTFSAPFA GDFPVDDNVL SSLPPGTELL SANRFGQSKW TLTARLNVKT
ADGTAMAYFL KCAAGDAGRL MMEGEFNSMS ELYRTMPEFV PKPLTWGKFS RPSPETYFFI
SEFIDMSDRP PEPNQFCTKL AKLHKTSTSP TGKFGFHITT CQGCNPQAVT WESNWTVFFG
NLLRNVIKLD DAENGHWDAL TVLEQRLLSH VIPHLLDNLT KNGRVVKPCL IHGDLWEGNT
GTSYQTGNVY LFDAAVMYAH NEFEIGDWRC DYNKIHNRVY TRTYLRHYAP SEPRNEWDDR
NRLYCIYYNI LYSVNHQGQG KAVRQRAFDD MYYLIDKYEP FPDGEGPARL SDGERAELPD
ERDHTKN
//
