ID I3ZG44_TERRK Unreviewed; 981 AA.
AC I3ZG44;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AFL88212.1};
GN OrderedLocusNames=Terro_1923 {ECO:0000313|EMBL:AFL88212.1};
OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL88212.1, ECO:0000313|Proteomes:UP000006056};
RN [1] {ECO:0000313|EMBL:AFL88212.1, ECO:0000313|Proteomes:UP000006056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC {ECO:0000313|Proteomes:UP000006056};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete genome of Terriglobus roseus DSM 18391.";
RL Submitted (JUN-2012) 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 protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR EMBL; CP003379; AFL88212.1; -; Genomic_DNA.
DR RefSeq; WP_014785781.1; NC_018014.1.
DR AlphaFoldDB; I3ZG44; -.
DR STRING; 926566.Terro_1923; -.
DR KEGG; trs:Terro_1923; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_013589_0_0_0; -.
DR Proteomes; UP000006056; 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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 3.
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; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AFL88212.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006056};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AFL88212.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:AFL88212.1}.
FT DOMAIN 12..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 569..602
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 284..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 981 AA; 104419 MW; AB7017FE94168B1B CRC64;
MEQNGPLQYG PYVVLEQIGA GGMGAVYRAR DRRLERDVAI KVLHRHLEMA SARERFLREA
RAVSSLNHPN ISTIFDIGEQ DGDPYLVMEL LHGQSLKDRL VDGVPMLPAE LEAIATQAAL
ALAAAHAKGI VHRDIKPANL FLVDGPHGEK QLKVLDFGLA KMETDRILYG DAGGLTRTGS
TVGTVEYMSP EQARGEDLDA RSDLFSLGAV LYELATGDVP FRGATSAVVF AELLGSDPVP
PRMQNSHLSP GMDAIIRKLL EKKRENRIQS ATVLLEDLRK LKHEAPARPS VSSGASVTSV
PQDTPAAVSQ ELPVRPLPSR ETQPKHVVPV QEPTVRGPRI KPSGSRPSQI YARTSGSRPS
LELDAARLLQ DLSFERAAAE GDSEEVEATG RIRWWIPVLA VLLLAGIAAA IFLRPRGAAT
SAASVFTGSL QITQFDNSTG NAVLQETPAV AMQILLKEMP SLHLTGFAPS PDTVDLDAAE
MAKRSGAAAY LTGSVSRDGE RYHVHAEILK TTDSSRLAQE DVDAASMVEL PNALSRLAVA
LRTHMGETPE QAGADTVQLA NEATASLSAL ALYARGSSLL RAGQPTAAVE QFQKALADDP
SFVTARLDLV ESLRQAGAEP ERLQAAALLK PMAGRVGVCE RNRAVYEIAD AAGALDAAQQ
WATACPTQTE AQIALARQLL AAGRGAEAEA VGNKAVLFDP AGRGAITIAT EAMISQDHYE
SALKQQAHAV SLRASTPGLL LLAAYLRGDL ATESMALALA EASSNWQDQW AVVTYLANRG
RLVEASRFGQ GAAARLQQMR EVASTGTLMR TRISALQAMA GHCDGGAIRA AKAGDLAEFY
AEIAGAWCKH APGSAGINDV HLATIARAAD TWSNGDAQGA LDILQSSRGG RQAPVAAMLR
GEIHLAMKER VLAIGDFQAV ITKRGASLLT GTLVYPAAQA GLATAYHRMG DEPNAARVED
DLKALWKDAP RNEPLLRRAV K
//
