ID A0A1S1RE37_9ACTN Unreviewed; 783 AA.
AC A0A1S1RE37;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=CC117_10040 {ECO:0000313|EMBL:OHV44009.1};
OS Parafrankia colletiae.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Parafrankia.
OX NCBI_TaxID=573497 {ECO:0000313|EMBL:OHV44009.1, ECO:0000313|Proteomes:UP000179627};
RN [1] {ECO:0000313|Proteomes:UP000179627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc1.17 {ECO:0000313|Proteomes:UP000179627};
RA Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA Nouioui I., Abebe-Akele F., Simpson S., Thomas K., Gtari M., Tisa L.S.,
RA Hurst S.;
RT "Sequence Frankia sp. strain CcI1.17.";
RL Submitted (JUL-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 -!- 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:OHV44009.1}.
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DR EMBL; MBLM01000025; OHV44009.1; -; Genomic_DNA.
DR RefSeq; WP_071082494.1; NZ_MBLM01000025.1.
DR AlphaFoldDB; A0A1S1RE37; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000179627; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 2.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000179627}.
FT DOMAIN 8..265
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 627..694
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 273..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..783
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 79471 MW; A82FC5578F585A28 CRC64;
MRKLGSRYVL HELLGQGTAG QVWRGAHVSD GEPVAIKVLR PELAHDPEVV DRFLRECDLL
VQLDSPDLVR VRELIQEPGT LAIVMDLVEG IDLRAHLDQA GPRPVTEAVR LVVGLLWALD
SVHGAGIIHR DVKPENVLID TSDPRRPYVR LTDFGVARMI HTPSRASLTG PIGTPLYMAP
ELADEVPPTP AVDIYAAGVV LYELIAGSPP FDASHPADLM RAHREDVPQP IQGVPPAVWE
VLAAMLAKSP QQRPASAADA AEDLLDAIED EDRDHDLDEG DDDHHWEREQ DRRADPRDTG
ASRQHGGAGR GAPRGRPGSR DFDTAQTRID RDRATAGAPQ RDPARSGTTG RQPAVVGAGA
LGAGALGAGA ARTGPVGAAA GATAVLSGGD ATGAHGGWDD AAHTQVGGIP ATQAGSPPSG
RTGWNDDAHT QVAGIPPVRP DRGGADQTWA GRAPDRWDEA DAATGAQPAV RVPARSAGSA
ADRNTVISRS KDSAPASTVS GPGSPAARSA ADRRRRSRIA AGAGLVVALV AGAGGWALAA
GDSESGLTAD GQTQTLIDPS ITATLPGGLP MPPGMDPAQV GSSGGASGPA RTNPAASPGQ
SASPGATPSQ SGQPSASPSA TTSPSATPKD ATVPDVQGQS QSAATNTMSG KGFTNVSSSE
TCQKGKKGGV VIDQNPNAGS VVPVSTKVTL TVQATNCVEV PGVAGRSLEA ARSALVSAGL
GVLNGGGGCQ WGTGSTAAST NPAAGTMMRK GENVWLEPSC SASPAPAPPP SSAPPASPAP
RGT
//
