ID T1IUD3_STRMM Unreviewed; 1477 AA.
AC T1IUD3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:SMAR004755-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:SMAR004755-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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; JH431527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 126957.T1IUD3; -.
DR EnsemblMetazoa; SMAR004755-RA; SMAR004755-PA; SMAR004755.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_249868_0_0_1; -.
DR OrthoDB; 4580305at2759; -.
DR PhylomeDB; T1IUD3; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24342:SF14; DEATH-ASSOCIATED PROTEIN KINASE DAPK-1; 1.
DR PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 79..339
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 340..372
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 373..405
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 406..438
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 511..762
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1118..1199
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
SQ SEQUENCE 1477 AA; 167484 MW; A20D4546DB585A8D CRC64;
MLLDRYALTP VIKLIDFGLS RRILPGMDVR DMIGTPEFVA PEVINYEPLG TATDMWSVGV
VXXXXXXXXX XXXXXXXFFF FYIFNVIGQF AVVRRCVEVK TRHEFAAKFI RKRRLASSRR
GAKMEDIRKE VDILMQISHK NVISLHDVFH NGHQVILVLE LVRGGELFDF ISEKEKLSEK
DAVVFIKQIL EALDHLHCKN IAHLDLKPEN IMLLDRYALT PVIKLIDFGL SRRILPGMDV
RDMIGTPEFV APEVINYEPL GTATDMWSVG VVTYILLSGA SPFLGDDQQD TFENISALDY
TFDEEDFSHT SDLAKAFISH LFVRNPRSAR CSRIIYFYFH GETALHIAVW HDYPSVVEIL
CKVGAQLNLC NTEGESPLHC ASVRGHLDCV HCLTEARAQL DLIDKRGFTA LHLAIRRHHV
QVAMLLLQTG CQIDVIDSHG DASIHLVAKE GLLPIAQTLC AFGCKVDVPN KDGIVAEITA
LAQGHTYIGD LLNRLNNEQL RQEYISQLIP SNQTISRVKV KLFGHNNVGK TTLIDSLKCG
YFSSFFRRSR SSSSSLNLGS RRRSSVSASS RSTLELNANK PSHSSSQPSI CTNINNYTRG
IEIHQIVLSG VGDLSLWEFS GQESYHMLYD HFIGNNHCIH LIVFSLSDSF EVQLKQVIFW
LHFLQARIVP LEPYGTYRTC GKNNKPTQVA LIATHADTAN CPKNNAGEYA NAAVMKLHCE
VQKMFEHVFD LHNRVFIVDA HVASSPSMKA FKFYLADVKT KVLQGLPYST GFLESVLRQI
PAWRRNFNSF PVLAWQQFID TVHGQVNPLA GEEHMRELLQ QLQLLGEMLY IKSETQDLIV
INPKWLCRDI IGHLLSQEHI DVARVTGCYT VDDFQLLFPD TDALDLLQVL EAIGLCTQCD
NDGDIEYEFP CFNFVETLHG LWEKDDKYHA DSTYGGIQFK TRENAHAQLA CVFPRIQAHL
RKTTQEHQEP ENDLYQWCQG SKFCSGNTEG ILTVENKGEY VELKVRGNTS AAAPTFYFLE
DLALVVEHVV EDMCPGMSLI RHWMNPTDLK EHNQQVLTYE PRTLMSAQLE NGVVENNNNN
TATTLVELLC FGLKSPVAGM VWGKDLPVSL LPIPLKQTLA SLLDPAESLG RDWCMLAVLL
GLSDFLPSLD SDENFNISRT IRVLEEWNQI HSNCTVGSLI GALKGLQRDD VIAAILHEAP
LFRVMHCFDE KQCESTAAAT TVTVARIMES SYYSLNAYQK LLVDQEVSIQ ESRNIKGFYD
FCVLHSEKDQ EDVISFRDDF CETYSLKGCL ECDEEPMKEP DFFQRLDEMV RRSTYVLVYV
SPNFYVDEIC RIQKSDLLSR YKNNLKLIPL YLDEDYQSLT PVGLGGSSKI ELFKSSGDGQ
KIRALFNEDV KKIRILKEEA EKYELAIRVD TIRECESRKL LNAEETEDTE DSIRKERIIE
SLSRSVSYCD GAQDEEMRRL FSMVNLNQRD EPDGEIN
//