ID A0A0S4JGP0_BODSA Unreviewed; 1615 AA.
AC A0A0S4JGP0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Protein kinase, putative {ECO:0000313|EMBL:CUG90644.1};
GN ORFNames=BSAL_28120 {ECO:0000313|EMBL:CUG90644.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG90644.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CYKH01001852; CUG90644.1; -; Genomic_DNA.
DR VEuPathDB; TriTrypDB:BSAL_28120; -.
DR OMA; LWERKHA; -.
DR OrthoDB; 127060at2759; -.
DR Proteomes; UP000051952; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd00130; PAS; 1.
DR CDD; cd06606; STKc_MAPKKK; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR11584:SF369; APOPTOTIC SIGNAL-REGULATING KINASE 1, ISOFORM C; 1.
DR PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; cGMP {ECO:0000256|ARBA:ARBA00022535};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Kinase {ECO:0000313|EMBL:CUG90644.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW Transferase {ECO:0000313|EMBL:CUG90644.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 133..250
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 253..373
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 457..494
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 565..774
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 807..922
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 950..1218
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 60..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 911..938
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 60..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1305
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 979
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT MOD_RES 854
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1615 AA; 176970 MW; 478C256E86125E23 CRC64;
MPQISGLREH IIHLLDQTED ETAFIRCIKL LENTGDDARP SILSMQVTSE LDANSLNMEE
DGRGDLNRDS VDDGDVNEAS QPSTVAAVSE GRRIAVSAAP IAMNTIKDYK PRVVPKTPSE
EEVVRKGVQG CHLFATMEAE EREVIVKALE KEEFDAGTDV LKQGAAPKDR FFMITEGTCE
VIKNGKHVAS LNGGATFGEL EMMYKQTECA ATIRCVTNCV MYSLDQQSYQ HIVLNVSVQK
RERYQRLLHR VGFLEALSDY DRMTIAEALV TTEYRADDKI ISFGEKGQWM HIIIDGEVQV
VGRDRGKKVD VVRLGEGNVV GELEFLFDHL TVADVVAATP RVVTARINRK HFEMVLGPIT
DQLKKFVAKN ETYAHYLADA DEKVKAEITM LEKRVRRVAK AHGGELLDNL DKDGEIVITD
PTPIIDQGIS VNRNGTQQKE AVYRFPLKPV MEANFIMIGL REDGMIVLWN DAMSRVTNYQ
SAEVCGQSFY SFIHSIKDQE TMHTAINDAR AFTGNIEGFY QSQVGKEKNT FVFARSDGLT
KATLQLTVIP SVVAQGSNVA DIMLAIGHEV KRPPPMKQND YSHWVAEQVR SLINDTALEA
DDRLSRIGGV VQKFETLIKG SNISADELRV VNVRQLIGQV VMDYGAMCVE KGLSVKQNYD
EMYCDEVYCD AHLLPECLRY AMSNCTNHIS ENCSIRIKVA VEEVFGSEQL MISINDNGPG
FPSKVLDEFN GVTSTGSFAA LLRVKAAVEK QGGTMQISSV PGDTHVIFRI PFIPQEESED
MSDIPMDLGG SLANHQSMAF VKKQTYTTLV VEDMPAHRNM LCAFLWERKH AVLPAYSLTD
INRLADVTDI LIIDPQQSIL SDPSAIADPF AMLREKARSV AVIVTAPSFD EGTKKAYQAA
GFFTLQKPCT AIQAVQVLRK AEEKISKIKS EADKIAQTRD TLAKNSRGAW KKGMLLGKGA
FGEVFEAIDV LTGGKMAVKM LRVTDKMNKD ELLHEIEVMC TLQHPNIIHY FYCEDNTEAR
TINVFMEFAA GGTVQGLLAK KGKLDFKEFQ TLLRDIVEGI AYTHGKRYVH SDIKTANVLL
NHEGKGKIGD FGTAKQLSEG ELLYIMQGSP LYMSPECMSA GELKEDGSGE QIGFSYPSDI
WSLGCVVMEM ATNKPPFSHI EFNGPVGLMS FVTGLTDIPD LSPLFDLPPS VIEFVSACLH
PDPAKRPTAQ ALLGYSIFNE TTDDDLKSAL KALKRAQLLH VLNKFVAFQD EEELEQQKRD
QARFKTARRD SAFFDSSDDD ESGGDKDGES DFFASSDDEE DDDDEKKSHE KEKATEAEGS
APPSKTGSKS GMTPISAVPS GVHGQPKRNL FAVDDPAASV AGSTSTSQTT VQQQQHHTAP
SSQTSVTAPA FAVCGAEDDE APAMFAALHT LESDTPHHAT AAALPTSAAV TATPPPGEAK
IEQHSDAMDL LPSTQTTQVA HIQPASESDE DAASAPKVGF TPKPPSQNPP SSPHGRHTSV
EIGSTSSGSG IRSPPTNVVE SAAIHTQQRH QVIVLHDALL SLVDELRKLN RNVEATDALL
HQYKAHTSNT EGGDDGTPKS SPTATSSFLP DVEQLLRDDT EVIRTLIQTL AGGIP
//
