ID A0A168I1F8_9ACTN Unreviewed; 627 AA.
AC A0A168I1F8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:OAA18675.1};
GN ORFNames=UG55_110213 {ECO:0000313|EMBL:OAA18675.1};
OS Frankia sp. EI5c.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA18675.1, ECO:0000313|Proteomes:UP000077018};
RN [1] {ECO:0000313|EMBL:OAA18675.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA18675.1,
RC ECO:0000313|Proteomes:UP000077018};
RX PubMed=27389275;
RA D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA Tisa L.S.;
RT "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT Nodules of Elaeagnus angustifolia.";
RL Genome Announc. 4:e00660-16(2016).
RN [2] {ECO:0000313|EMBL:OAA18675.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA18675.1,
RC ECO:0000313|Proteomes:UP000077018};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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}.
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:OAA18675.1}.
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; LRTK01000102; OAA18675.1; -; Genomic_DNA.
DR STRING; 683316.UG55_110213; -.
DR PATRIC; fig|683316.3.peg.5489; -.
DR OrthoDB; 4326323at2; -.
DR Proteomes; UP000077018; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; 2.60.40.1240; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR029051; DUF4352.
DR InterPro; IPR029050; Immunoprotect_excell_Ig-like.
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 PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF11611; DUF4352; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:OAA18675.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000077018};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:OAA18675.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:OAA18675.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 455..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..285
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 627 AA; 65164 MW; AB3B4FCA517AC494 CRC64;
MDHNGEQAPA ARGQPGGRTP PGESLHPHEP RVIGKYRLLR RLGAGGMGTV YLSESAGRRV
AVKIVRPDLA ADEEFRRRFR QEVDAARRVA PFCTAEVLDA DPDAPAPYLV TEFIDGVRLD
HAVEDGPIGG STLTGLAVGV ATALTAIHSA GLVHRDLKPS NVLLSMSGPR VIDFGIAQAL
EGAKAKPTAW GFGSAGWMAP EQVNGQPIGP EADVFTWGIL VAFAGTGHHP FGTGTDLELS
TRIVGWEPDL VGLPPGLKAL VAAALAKNPD ARPSARDLLL NLISLPPARP GDSGGDRAWR
PSSTAVNQAE ELLNLTQGVV LPSSTSSAPV RPPLPAGDRV PAAQVPHGQS DRWRAARQHR
PGAVRPPNQA GLPNQAGPAG LPAGSASGGA PAPGAAHPGG VAVPVPAGAP SFSGAPAGGW
PPPRPPGRGY VHQVPDPGAF PDAAPNPSRS IRQRLILFGA VAFVVVLAAW LISTATGGDT
DQSVTPGPQS GAALTPAASR TARPGTPARD DQLEFLAGKI ECNVSKLDGI FPRRPSGQFC
LXDXSVTNSG TVXRVLSNSN QFLITSDGER RSADYLARFY LNDGLWETIT QGSTVTGTIV
FDIPADATPR ALELHERPES KGVTIQL
//
