ID T1ISC4_STRMM Unreviewed; 1180 AA.
AC T1ISC4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
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:SMAR003991-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:SMAR003991-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) to UniProtKB.
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; AFFK01018942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1ISC4; -.
DR STRING; 126957.T1ISC4; -.
DR EnsemblMetazoa; SMAR003991-RA; SMAR003991-PA; SMAR003991.
DR eggNOG; KOG0199; Eukaryota.
DR HOGENOM; CLU_001143_1_0_1; -.
DR OMA; LPECKPE; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; T1ISC4; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd05040; PTKc_Ack_like; 1.
DR CDD; cd09539; SAM_TNK-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR049587; TNK-like_SAM.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418:SF444; ACTIVATED CDC42 KINASE-LIKE; 1.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 120..383
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 488..502
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 529..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1180 AA; 132164 MW; 391D5BBA0FE315A8 CRC64;
QEETMGAMGR GPGLYEFLVE AELQPYYGTL KNDLRVNTVA QIKYVEDEDL AQVGMSKPEM
RRLKKYFHKY YPQTYLRRIK QMILPKREEI LRASLVISDP VQERGMVKVP SKHIISSENI
TINKELGVGE FGVVQQGVWT NEDGDRIQVA IKKLSKERMQ NNSMEFLKEA AIMHTVDHEH
VVRLYGVVLE TSALMLVTEL APLRSLLECL KEPALRPSFP ILSLCDFAFQ ICDGMQYLES
KRLIHRDLAA RNILVFSKNK IKISDFGLSR ALGVGKDYYQ TNFNVNLKLP IAWCAPECIN
YLRFTSASDV WAYGVTLWEM FSYGFQPWAA LTGQQILEAI DEPNFQRLEQ PECCPKEYYI
LMLKCWQHDP NKRPKFSDIS AILPECKPEQ VQCIKDYTED ASSSPKSKRE QLQYKVSDVI
AVLDKKPLAD SVNVWKGALT NCKTGLFNPA HTVAYLGTNI PSMKPSFTRS DSKSGVYSSK
RRLRAEMISR PQADFRHTGH VGLDGAFFGD ISCLGDKYHL LPKQIVTPYK PHEDGDQSTS
SLNRAPSDVS DRAPLLIKGG ELGKGGPAID TWSDSSSDKK ITIDENHVAK QIADHEYHEI
SDDENQVESP RFETFFQRCL DFGPSLMDEV FKALGNKDDE LEETTKDESN NVRNEIREMA
AKNKESGTKK KQATVKPISA SDQRTLESAI AMANEMASKS MLELVNKPDS DLAQESPHTP
SSPTKRKFSF RLPTAKSPKN ERRNFTEETE SIADIQESLT EEAKDAYNTL VEKGQTEAVE
DGDTNPLRML RSGLTVRPKV RGNKHGTSGR NSFGQDGQTA PNALRFTSES RIHLHPRNTL
GIPPAPPVQN NATESARSPP AVSLKPVITA NEMSDVTTHR EGEEAIPPHE NGGSISTGDE
GDSEHSSDQN PLPLPPRDRT KPMQQHKPRQ RKHPLIIPGS TARPLVKPSL TSDDVEPVQT
NGNSDEVSEP GSDTVDSPNT TTPIIIHSSP KFDVVKNGSV STTPPAPVKP PRVKFMLNSN
HYLKQHRSQS SLDDSFDNQI QADMDSLDDI PEEEAPLPPV DHHVSCEDLL DFACDRPNTK
RTQGRARGTD ADEVRILQKV LAGKIPTLQV TREDCVATLN ETDWDVHKAI KYMKLQTLLR
NELSCDSNCK QTLVNCDWDV QKAYSYLLAT YGVTEDSTEV
//
