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Database: UniProt
Entry: T1IUD3_STRMM
LinkDB: T1IUD3_STRMM
Original site: T1IUD3_STRMM 
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};
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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
//
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