ID A0A195CMD7_9HYME Unreviewed; 988 AA.
AC A0A195CMD7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038172};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038172};
GN ORFNames=ALC62_07327 {ECO:0000313|EMBL:KYN01855.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN01855.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN01855.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN01855.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN01855.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in the response to environmental stress.
CC Appears to act upstream of the JUN N-terminal pathway.
CC {ECO:0000256|PIRNR:PIRNR038172}.
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 ECO:0000256|PIRNR:PIRNR038172};
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 ECO:0000256|PIRNR:PIRNR038172};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000256|ARBA:ARBA00008874,
CC ECO:0000256|PIRNR:PIRNR038172}.
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DR EMBL; KQ977574; KYN01855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195CMD7; -.
DR STRING; 456900.A0A195CMD7; -.
DR Proteomes; UP000078542; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06613; STKc_MAP4K3_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF18; HAPPYHOUR, ISOFORM A; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 2.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038172};
KW Kinase {ECO:0000256|PIRNR:PIRNR038172, ECO:0000313|EMBL:KYN01855.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038172};
KW Reference proteome {ECO:0000313|Proteomes:UP000078542};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Transferase {ECO:0000256|PIRNR:PIRNR038172}.
FT DOMAIN 22..279
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 638..957
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 988 AA; 111916 MW; 9F2780DEB4E0DD36 CRC64;
MAAVNANVLS SDISRRNPQD EYELIQRIGS GTYGDVYKAK RLSMNDLAAI KVIKLEPGDD
FAIIQQEILM MKDCRHPNII AYYGSYLRRD KLWICMEYCG GGSLQDIYHI TGPLTEIQIA
YMCRETLTGL AYLHSMGKMH RDIKGANILL TESGDVKLAD FGVSAQITAT INKRKSFIGT
PYWMAPEVAA VERKGGYNQL CDIWACGITA IELAELQPPM FDLHPMRALF LMSKSGFKPP
TLKDRDKWSP TFHNFVKIAL TKNPKKRPTA EKLLQHAFFQ GEMSKRLALE LLQKVSNPSH
MFTDLEADED GAVPNVPQRI ASRHTARPRP KSPISQLDSD DQINIDGGTL HRDSISPSVD
SPAWDIMDIM NNVKVVHNCD VHPDCGIGSA FEDIQENFQK YTYFCIRILG ANFKTNKILK
RSKTGTEMFH MSLRSLLQYI DEELLLRYWQ NTLFIKLQNI IISSPTKLVY NFIVYDHKVS
HVYRGNAMSM VDGHCDQLYS LQATLPLGES SNDCEVHCPY YNVSGSQASP RRHSSVDELY
GLVNSSQSLT AVNGQRQRSL SDSGPRDEPA QTNGDNEISA DRDRESMSPD LLSDTPPIPP
RRRDRKRHTP PRPISNGLPP TPKVHMGACF SKVFNGCPLR IHCTASWIHP DTRDQHLLIA
AEEGIYNLNL NELHETAIDQ LYPRRTIWMY VIKDVLMSLS GKTPQLYRHD LLAMLSKQTH
RFSLHMNKIP ERLVPRKFAL TTKVPDTKGC TKCCVGRNPY NGYKYLCGAM PAGIFLMQWY
DPLNKFMLLK HFDCVLPSPL NVFKMIITPE MEYPMVCVSV KQPYQQNKIK LDLINMNSGA
SWFHSDELED MDGSATVIPR RENLNVINVT QFEKDAILVC YDNMVKMVTL QGKPRISKKQ
LSELQFNFEI ESIICLPDSV LAFHKHGMQG RSFKNGEVTQ EISDPSRTYR LLGSDKVVML
ESHLVHSGTL TESEGADLYI LAGHEASY
//
