ID A0A261KPT3_9CYAN Unreviewed; 964 AA.
AC A0A261KPT3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=AFK68_16615 {ECO:0000313|EMBL:OZH53593.1};
OS Hydrocoleum sp. CS-953.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Hydrocoleum.
OX NCBI_TaxID=1671698 {ECO:0000313|EMBL:OZH53593.1, ECO:0000313|Proteomes:UP000215798};
RN [1] {ECO:0000313|EMBL:OZH53593.1, ECO:0000313|Proteomes:UP000215798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-953 {ECO:0000313|EMBL:OZH53593.1,
RC ECO:0000313|Proteomes:UP000215798};
RA Willis A., Parks M., Jameson I., Burford M.A.;
RT "Comparative genomics of marine benthic cyanobacteria including Hydrocoleum
RT sp. CS-953 from Moreton Bay, Australia.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the leucine-binding protein family.
CC {ECO:0000256|ARBA:ARBA00010062}.
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:OZH53593.1}.
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DR EMBL; LGSU01001127; OZH53593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261KPT3; -.
DR OrthoDB; 446586at2; -.
DR Proteomes; UP000215798; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd06268; PBP1_ABC_transporter_LIVBP-like; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028081; Leu-bd.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR30483; LEUCINE-SPECIFIC-BINDING PROTEIN; 1.
DR PANTHER; PTHR30483:SF6; PERIPLASMIC BINDING PROTEIN OF ABC TRANSPORTER FOR NATURAL AMINO ACIDS; 1.
DR Pfam; PF13458; Peripla_BP_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000215798};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 12..361
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 205..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 106629 MW; BF98B1AE36EDE1E8 CRC64;
MINPGQILQD RYQAIKLLGD CGFGQTWEVD DGGTRKILKI LQVPKAIDDE EMEQVISLFE
QEANVLTQLH DLGLPEVGPE AYFIESTEDV GPLHCLVMEK IEGINLSDWL EQNNQGEPIE
EEQAIAWLTQ LVEIISKLHQ YHCIHRDIKP TNIILRSTAE NQNNTIAQQI VSDNLSNSSQ
VQPKDIEARE AKNLAPISLT PKNVAQLGNN TKTLGATEGD KSEVENKKSQ TANQEDSQKQ
EWGQLALIDF GATRQVTETY LRQVEGKNVS GIISQGYTSP EQYEGKVTRQ SDVFAIGRTL
VFLLTAENPS NLPTEPQTGR LMWRDHATQI SKELADLIDE MMTNLPQCRP QTNEDILERL
ATCKQQVETE TEVELKPKPT QNQKPTPVTE NQSYSRLLQS KLLNFKGKSQ KNTPQPNKWL
GKISLFTLGV IAVFIAFLPE APTTCPLKFD DKLSCGEEIL IPGSATTDKE EGVKAFADAN
YLQAVTLLET ARKKQINDPE TLIYLNNAKL AANNTEAYTI AVAVPMTGDS RSLNYSLEIL
RGVAQAQDVI NQSDSWLGGK GLIVIIADDI NSSTQAVRRA NALAATGQVL AVVGHLSSQI
TMEVAPIYEE NKLVLISPTA NASTLSNRNN FLFRMIPSDA TMAQAMASYL ISQSEDEQPK
VALFHIPNDV YSESLRNQFS VSFTAGRGKI VKDLDEKFDL SRTAFNASAA IDRAEKQKAT
AIVLLPPKVA LFHIPNDVYS ESLRNQFSVS FTAGRGKIVK DLDEKFDLSR TAFNASAAID
RAEKQKATAI VLLPDIFSLS KGIEVIKANW QLNLPIVAGD SLYNDYALKF GADEAERNLI
VATPWHSLNS PNLDFPQQAK ELWGGAVSWR TAFAYDSVQA LITALESLPE QKELNRIGLQ
KVLAAENFSS YGATGEITFL PNGDRQESRI SFTEVVKSSC SPLGYTFLPL DYPVSQFNLL
ECEE
//
