ID T1JIH4_STRMM Unreviewed; 951 AA.
AC T1JIH4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR013655-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR013655-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) to UniProtKB.
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};
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DR EMBL; JH432085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1JIH4; -.
DR STRING; 126957.T1JIH4; -.
DR EnsemblMetazoa; SMAR013655-RA; SMAR013655-PA; SMAR013655.
DR eggNOG; KOG1152; Eukaryota.
DR HOGENOM; CLU_006086_0_0_1; -.
DR OMA; CVNEAKH; -.
DR OrthoDB; 5403755at2759; -.
DR PhylomeDB; T1JIH4; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF51; PAS DOMAIN-CONTAINING SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF13426; PAS_9; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000014500}.
FT DOMAIN 639..892
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 951 AA; 105215 MW; E86C791E07458EF5 CRC64;
MAEGSNRFKQ DSSSPMSTKR RVKGTTAGLL SWKSGKGFLS SKEAGAVQFV FPSPLDRIRS
GIGRRERATQ LGLSLSAQPE SFEGNQSFPR IERLEIGTEN SCTMDKFRGD ELNTFSFSPG
HVRGSFAQTP DSAASRTVSF NDSWTFYNNL LGQAPSPAVT ASSSIYNPNK AVVTIDAKSS
EILVANDMAC RLFGYNSDEL CRRRLADMFK HRSNRKAIVE THLDSSGEVI VVSGKVIDMI
DSEGEVVPVS LWVKKLEMAR RCLAVMEPVE RTAANFTFDE RGAILSCDNI MAVLHGYSCA
DEVVGLDIRT LIPSFALPSA DTISKNVKKQ QATGRTKDGA TFPVSVTVDF VSDEASAASA
ASSVDYAGLV WVFANISGMI TILPNGNIHS CNHYFALMLF GYTQSQLVGK NISALVPTFY
DDVEFLEADS TPYNDDDVDV DEDIWQTYRT PEKDEDVSIT KAFRKMLLSR DESCQHDLNG
NDHRGGGEDD DVDDDDSKAA EEEEEEESRA FAAEAAATTT PEVRSIPEGS FFGLGRHRDG
SDLSIIYQIK RVNLDDGDTL YCVWVSRDPE EPAEGGRGNN LTFASSVNST LDASASSLSL
GQVSFAILLL NIINEKAHSA AELDHSDVDY TSGSFAERYT TLQQIGKGAF GCVKMAFRNT
DKLLVITKFI GKCKVYDECW VDDNLLKKTV PLEVSLLTTL KHSNIVQVLD VFENADYFQM
VMEKHGCGMD LFEFIDRGPS LDEPLASLIF RQVASAVTYL HGLNILHRDI KDENIILNEN
FHIKLIDFGS ATFMAPGKLF STFCGTVEYC SPEVLQGNKY RGPELEMWSL GVTLYTLIFG
ENPFFDVDET IKADLRPPFQ ASKDLMHLIG GLLNADPKSR FGLRELETNV WLHQPIDADS
YSFQNIISCS LDEANPPRYY YDLEIGDHHP FSASSQHQEF KLRDLSDEGE L
//