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Database: UniProt
Entry: A0A0P4V495_9CYAN
LinkDB: A0A0P4V495_9CYAN
Original site: A0A0P4V495_9CYAN 
ID   A0A0P4V495_9CYAN        Unreviewed;       448 AA.
AC   A0A0P4V495;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Protein kinase {ECO:0000313|EMBL:GAP99576.1};
GN   ORFNames=NIES2104_61420 {ECO:0000313|EMBL:GAP99576.1};
OS   Leptolyngbya sp. NIES-2104.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya group; Leptolyngbya.
OX   NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP99576.1, ECO:0000313|Proteomes:UP000052243};
RN   [1] {ECO:0000313|EMBL:GAP99576.1, ECO:0000313|Proteomes:UP000052243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP99576.1,
RC   ECO:0000313|Proteomes:UP000052243};
RX   PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA   Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA   Kawachi M.;
RT   "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT   and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL   DNA Res. 22:403-412(2015).
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   -!- 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:GAP99576.1}.
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DR   EMBL; BBWW01000002; GAP99576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P4V495; -.
DR   STRING; 1552121.NIES2104_61420; -.
DR   InParanoid; A0A0P4V495; -.
DR   Proteomes; UP000052243; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR44858; TETRATRICOPEPTIDE REPEAT PROTEIN 6; 1.
DR   PANTHER; PTHR44858:SF1; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE SPINDLY-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13414; TPR_11; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 3.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:GAP99576.1};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:GAP99576.1}.
FT   DOMAIN          1..185
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          260..293
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          294..327
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          366..399
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   448 AA;  50509 MW;  4D1B5FDAD4152995 CRC64;
     MLEKIEGETL EQWLAQNGKT SEAVALRWMQ QLCAPENSQN LSGILTYLHS HNLIHRDIKP
     SNLILQPNGD LALIDFGGVR ELGQTDAIIS NYPTIITSLG YSPPEQVNGQ ATVTSDFYAL
     GRSWVSLLTG RNPIDLIDSQ TNQLRWRHHA PQVSKPFAAW LNTLMSASPY QRPQTTIEIY
     THLTEKLPQQ IRASQRVNSW WFKVSIASIS ASLILGIGWG VSLWVSNDYL RKGAENLRIE
     QYQSARTDFE TALKWNDRSA IAHNNLALSC YYLGDDDCAI AHYTRAIALS PDYWEAYYNL
     GAIYDRQERY DLASVQYLKA ANGSPETKAQ AINNLARLKN RQQQYTEAAS LVQSVVQLTQ
     AEPTLASLHK NLGWALFGLD RFEEAQIALE RALSLDGSRI DTYCLLAFVK QARKLESDAE
     LKTCLFSATK SPLPEVKEWR IQLAKRGF
//
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