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Entry: A0A4S2KPQ6_9HYME
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Original site: A0A4S2KPQ6_9HYME 
ID   A0A4S2KPQ6_9HYME        Unreviewed;      1474 AA.
AC   A0A4S2KPQ6;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-JUN-2025, entry version 24.
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=DBV15_06611 {ECO:0000313|EMBL:TGZ49838.1};
OS   Temnothorax longispinosus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Temnothorax.
OX   NCBI_TaxID=300112 {ECO:0000313|EMBL:TGZ49838.1, ECO:0000313|Proteomes:UP000310200};
RN   [1] {ECO:0000313|EMBL:TGZ49838.1, ECO:0000313|Proteomes:UP000310200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole body {ECO:0000313|EMBL:TGZ49838.1};
RX   PubMed=30967075;
RA   Kaur R., Stoldt M., Jongepier E., Feldmeyer B., Menzel F.,
RA   Bornberg-Bauer E., Foitzik S.;
RT   "Ant behaviour and brain gene expression of defending hosts depend on the
RT   ecological success of the intruding social parasite.";
RL   Philos. Trans. R. Soc. Lond., B, Biol. Sci. 374:20180192-20180192(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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:ARBA00048679};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00047899};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral
CC       membrane protein {ECO:0000256|ARBA:ARBA00004184}. Golgi apparatus
CC       {ECO:0000256|ARBA:ARBA00004555}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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:TGZ49838.1}.
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DR   EMBL; QBLH01002093; TGZ49838.1; -; Genomic_DNA.
DR   STRING; 300112.A0A4S2KPQ6; -.
DR   Proteomes; UP000310200; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:TreeGrafter.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:TreeGrafter.
DR   GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR   GO; GO:0005795; C:Golgi stack; IEA:TreeGrafter.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:TreeGrafter.
DR   GO; GO:0048211; P:Golgi vesicle docking; IEA:TreeGrafter.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0045056; P:transcytosis; IEA:TreeGrafter.
DR   GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:InterPro.
DR   CDD; cd12122; AMPKA_C; 1.
DR   CDD; cd14079; STKc_AMPK_alpha; 1.
DR   CDD; cd14336; UBA_AID_AMPKalpha; 1.
DR   FunFam; 1.25.10.10:FF:000394; general vesicular transport factor p115; 1.
DR   FunFam; 1.10.510.10:FF:000079; Non-specific serine/threonine protein kinase; 1.
DR   FunFam; 1.10.8.10:FF:000055; Non-specific serine/threonine protein kinase; 1.
DR   FunFam; 3.30.200.20:FF:000136; Non-specific serine/threonine protein kinase; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR032270; AMPK_C.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR041209; P115_Arm_rpt.
DR   InterPro; IPR049020; PRKAA1/2_AID.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR006955; Uso1_p115_C.
DR   InterPro; IPR024095; Vesicle_P115.
DR   InterPro; IPR006953; Vesicle_Uso1_P115_head.
DR   PANTHER; PTHR10013; GENERAL VESICULAR TRANSPORT FACTOR P115; 1.
DR   PANTHER; PTHR10013:SF0; GENERAL VESICULAR TRANSPORT FACTOR P115; 1.
DR   Pfam; PF16579; AdenylateSensor; 1.
DR   Pfam; PF21147; AMPK_alpha_AID; 1.
DR   Pfam; PF18770; Arm_vescicular; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF04871; Uso1_p115_C; 1.
DR   Pfam; PF04869; Uso1_p115_head; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF103243; KA1-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:TGZ49838.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000310200};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:TGZ49838.1}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1417..1439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1451..1471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          878..1130
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1239..1262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          662..696
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          734..808
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1243..1256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         907
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1474 AA;  166232 MW;  6A757DA1DEE0A95B CRC64;
     MEYFKSSLKS VLGTAPAGTQ PTGADTVEKL VDRLQSSTLL DDRRDACRAL KAFSRTYRVE
     VGAQGMDALR QVLEVDRTDC EIIGLALDTL CNITXPETFD EEVGKHDSKS QIGEQFTEIF
     IKHSDSVGLV LTFLEEFDFR VRWPALKLLT HLLANRSKDI QEIILVSPMG VSKLMDLLSD
     SREVIRNDVL LLLIQLTKGN ANIQKIVAFE SAFDRIFDVI EQEGNADGGI VVEDCLLLML
     NLLRGNVSNQ NFFKEGSYIH KLTPMFQIPN ETEDNNLGGS WSPQKVSNVH CMVRVVRALV
     APSAPAQVVA ACQRTMRACG LLQALCDILM ASGVPADVLT EIINTVAEVI RGNASNQEFL
     AGVMAPSTPP RPAIVVLLMS MVNEKQLFVL RCSVLYCFQC FLYKNEVGQT QLIQTLLPQG
     NEGSSVTTGQ LLCGGLFSID SLSNWFSAVA LSHALIEXIS QKEQLLRVLL ATNIGKPPVT
     LMQQCVMLLQ QGNKTQCKLG LLILLCRWTS YCPLAVKSFL AIDSSVAYLT ALLSSQENND
     DLQETLLQSM CALLIGICVH FNDDSVPTYT KEKVCNLIEN RIGLEKFQDA IGGIVRHEIY
     SRTLKHPQPS AKNPSELLLD HEFCRLLKSL EGVIIKSVID ANNEHQNKNQ LSVMNLPDNT
     LVSQYKDLIR EQDTQIQRLN QANDFLTKEK QELEVTQVQE LRSTVSHLRD QNLVLRAAQA
     NIGDGKETIA SSNNLDLEKE LQTYKTMVAD LENRLAEYTH IMQQHDEKNK ENKESELEYQ
     LKLKTDELEK LKKDQEDLLE LLTDQDSKIT LYKERLIELG DKVESDETRM IFQSGRAKPG
     GVSAAHVSWE RPSVLTRLKM SEKLPSNQPQ PIVKIGHYTL GQTLGVGTFG KVKIGEHVLT
     KHKVAVKILN RQKIKSLDVV GKIRREIQNL KLFRHPHIIK LYQVISTPTD IFMIMEYVSG
     GELFDYIVKH GKLKEYEARR FFQQIISGVD YCHRHMIVHR DLKPENLLLD HNLHVKIADF
     GLSNMMMDGE FLRTSCGSPN YAAPEVISGK LYAGPEVDIW SCGVILYALL CGTLPFDDEH
     VPTLFRKIKS GVFPIPEYLN KSVVSLLCHM LQVDPMKRAT IEDIKKHEWF QKDLPSYLFP
     SPVEQDSSVI DIDAVNEVCE KFNVKEPEVH SALLGGDPHD QLAIAYHLII DNKRIADEAA
     KAELKDFYVA SSPPPVAFSP NETNSSPLRP HPERIAPYRE RQGSQGSAPA QMQGNRGTPV
     KRAKWHLGIR SQSKPNDIMN EVYRAMKALN FEWKIINTYS VRVRDKNNLT DRYSKMSLQL
     YQVDHKSYLL DFKSLSSEEE DIGRDPTLPP PQATGHHTME FFEILRRTYA TCDYNDDDDD
     NDDDGNVKCT YTMCCFKLVA QPMANRRCLS SLCVAHAAPI TLGEFLLNLL IVFTSLIIYK
     LHVRKWEVPD LAVQFTFPLA IDISLCHFYH ITYF
//
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