ID A0A1J0AA38_9CYAN Unreviewed; 686 AA.
AC A0A1J0AA38;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:APB32773.1};
GN ORFNames=GlitD10_0462 {ECO:0000313|EMBL:APB32773.1};
OS Gloeomargarita lithophora Alchichica-D10.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeomargaritales;
OC Gloeomargaritaceae; Gloeomargarita.
OX NCBI_TaxID=1188229 {ECO:0000313|EMBL:APB32773.1, ECO:0000313|Proteomes:UP000180235};
RN [1] {ECO:0000313|EMBL:APB32773.1, ECO:0000313|Proteomes:UP000180235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D10 {ECO:0000313|EMBL:APB32773.1,
RC ECO:0000313|Proteomes:UP000180235};
RA Moreira D., Tavera R., Benzerara K., Skouri-Panet F., Couradeau E.,
RA Gerard E., Loussert C., Novelo E., Zivanovic Y., Lopez-Garcia P.;
RT "Description of Gloeomargarita lithophora gen. nov., sp. nov., a thylakoid-
RT bearing basal-branching cyanobacterium with intracellular carbonates, and
RT proposal for Gloeomargaritales ord. nov.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017675; APB32773.1; -; Genomic_DNA.
DR RefSeq; WP_071453459.1; NZ_CP017675.1.
DR AlphaFoldDB; A0A1J0AA38; -.
DR STRING; 1188229.GlitD10_0462; -.
DR OrthoDB; 500858at2; -.
DR Proteomes; UP000180235; Chromosome.
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 CDD; cd00200; WD40; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19879:SF1; CANNONBALL-RELATED; 1.
DR PANTHER; PTHR19879; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:APB32773.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000180235};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:APB32773.1};
KW Transferase {ECO:0000313|EMBL:APB32773.1};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 34..298
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 388..429
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 433..474
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 479..520
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 521..562
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 577..608
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 609..650
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 651..686
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 317..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 686 AA; 74347 MW; A6C4BC10055CD4D9 CRC64;
MSYCLNPDCP APENAPTELN CCACGSSLVL KGRYRAVKPI GQGNFGRTFQ AVDESIPSRP
PCVIKLFQPQ VIQSPEAMQK AVTLFEQEAV QLDRLGNHPH IPDLLAYFIL DGKSYLVQKF
IDGQDLSGEL LRKGAFDEAK VRQLLADLLP VLDYIHKENV IHRDVKPKNI IRQQSDQKLF
LVDFGAVKFV RESGLFKTGT AIGSSGFAAP EQMMGKAVFA SDLYSLGATC IYLLTGISPA
KLFNIRENVW LWRQALKQPL SEGLMQLLDK LLQRLPGQRF GSAALALTAL QNLEQPARPV
STLGRLGVPG GGLSTPLNPL PGLGRVGGSV TATGNTNPPT QTGQPSGRLN PESGRLTQNP
PSRIGTRTPP PQVTTVQKDP TWTCLHTLAG HSNWVKAVRF SPDSRYLFSC SRDGMVLCWG
LSSLSYPRQL SWGSNNPTAL HALALSPDGR FLAAAGEERV IKIWQLPGEK PLRTLGNLFN
KHGGTIDSLA MRPDGLVLAS ASEDKTIKLW QVDNGALLTT LTAHASYVRS VTFTPDGRLI
VSGSWDNSIK VWLTDGGDPL RNILGSSSFS GSGFNVVAVS PDGRVIVAGS EDTAAHVWHL
HNGDPITTLT GHKEGVRALA YSPNGRYLVT GGWEGSIRVW DGQSYNLLMT LAGHEKGITS
LAFSLDQQWL ASGSRDNTIK LWQVGK
//
