ID K9WL86_9CYAN Unreviewed; 738 AA.
AC K9WL86;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AFZ20544.1};
GN ORFNames=Mic7113_4878 {ECO:0000313|EMBL:AFZ20544.1};
OS Allocoleopsis franciscana PCC 7113.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ20544.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ20544.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ20544.1,
RC ECO:0000313|Proteomes:UP000010471};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003630; AFZ20544.1; -; Genomic_DNA.
DR RefSeq; WP_015184679.1; NC_019738.1.
DR AlphaFoldDB; K9WL86; -.
DR STRING; 1173027.Mic7113_4878; -.
DR KEGG; mic:Mic7113_4878; -.
DR PATRIC; fig|1173027.3.peg.5408; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_135_5_3; -.
DR OrthoDB; 568198at2; -.
DR Proteomes; UP000010471; Chromosome.
DR GO; GO:0009579; C:thylakoid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 5.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
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; 2.
DR Pfam; PF00515; TPR_1; 6.
DR Pfam; PF13432; TPR_16; 2.
DR SMART; SM00028; TPR; 10.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50005; TPR; 10.
DR PROSITE; PS50293; TPR_REGION; 8.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:AFZ20544.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AFZ20544.1};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transferase {ECO:0000313|EMBL:AFZ20544.1}.
FT DOMAIN 13..306
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 367..400
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 401..434
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 435..468
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 469..502
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 503..536
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 537..570
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 571..604
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 605..638
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 639..672
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 673..706
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 707..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 738 AA; 83541 MW; FD3E2C0CDB0E9D2E CRC64;
MNLGLGQTIG GRYTIISQLG QGGFGRTFVA QDQHLPDHQQ CVVKQLKPQA TDPFTLQTAR
RLFDTEAKVL HRLGSHDQIP QLFAYFEENQ EFYLVQEFIE GDDLSQELTP PTPPYQGGAN
TGNPSLYQGK ASAGNLPLYQ RGARGGQLSE DKVISLLKEI LEILDFVHQQ NVIHRDINPR
NIIRRKQDGK LVLIDFGAVK QVSTQVVQGG RTNITIAIGT PGYLPSEQAN SNPKLSSDIY
AVGMVGIQAL AGISPEQLPI NPDTGEISWQ DKASVSLEFA EVLDKMVRYD FRQRYQSAAL
ALQALNELKT ISKSTVSLPA AASSKPIIAK PKLSKSLLYK VLISMGVLSL GLAATVLIVN
LVKSSNATDL YKRGDTFLEL KRYDDALASY NRAVELKPEY AAAWNGKGNT LLALKRYEEA
RNAYDKAIQI QPDYAEAWIG RGNALDSLQQ YKEAINSFDR ALEFKSDSLE AWNNKGNVQI
KLQKYSDAIA SFDKAIELQP NYAPTWNHRG WALHNLRQYE EAVKSYNKAV EYQPDFPNAW
YQRGNALINL QKYQEAVESY DKAVQFQPNF YKAWYSRGSA LLNLRQYEQA FASFDQAVKF
NPDDSEAWYN RGWSLHQLQR YQEAVASYNK AIQLRKKFYQ AQYNLGNVFY KLKRYQDAFV
SYNKVLEIQP NHYEAWYSRG NALVNLKRYQ DAIDSYNKAL QYKPDYQAAK DARNQAESQL
DSVPKKPEEQ KQQGEAKN
//
