ID A0A177D571_ALTAL Unreviewed; 381 AA.
AC A0A177D571;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=protein-ribulosamine 3-kinase {ECO:0000256|ARBA:ARBA00011961};
DE EC=2.7.1.172 {ECO:0000256|ARBA:ARBA00011961};
GN ORFNames=CC77DRAFT_1025553 {ECO:0000313|EMBL:OAG14656.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG14656.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG14656.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG14656.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441498; OAG14656.1; -; Genomic_DNA.
DR RefSeq; XP_018380077.1; XM_018526087.1.
DR AlphaFoldDB; A0A177D571; -.
DR GeneID; 29111681; -.
DR KEGG; aalt:CC77DRAFT_1025553; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1025553; -.
DR OMA; CWDGNTA; -.
DR OrthoDB; 2101593at2759; -.
DR Proteomes; UP000077248; 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:OAG14656.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Transferase {ECO:0000313|EMBL:OAG14656.1}.
FT REGION 346..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 42805 MW; BBE0553D9390855D CRC64;
MPTEPLLPPQ ISGSYKVNER VIAAFPIPKT QVIDAYNYGK SLWGKTAKIV VQLPTGQTDN
YFLKVVSLGS IGRHMCEGEY ESLKSIYAVS PSFVPQPYGW GQIDEGLAET YFLLAAFRDV
GEQPADPVNL AAGLADMHQR SISPTGKFGF HFSTCHARIA QAVDTWEDSW CTLYGRHLGH
VMKLAKPILQ WPEFDVVCDL TLQKVVPRLL LPLQAEGRIL KPCLLHGDCW DGNTAIEAKT
GEAFVFDVCS FYGHNEYDIG NWRAPRHRLS SEAYIRNYKQ NFPVSEPVED RDARNLLYSL
TFNIGNTIYI PGSQQRQIVF DDMHMLCHLF CPDELKAAMD KLKGDSTIGE SSQTGHPTMH
QNDGFVEAEA QGNEEEEEWL L
//
