ID A0A158NNE4_ATTCE Unreviewed; 1312 AA.
AC A0A158NNE4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=105622241 {ECO:0000313|EnsemblMetazoa:XP_012059052.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012059052.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012059052.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; ADTU01021332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01021333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01021334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01021335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01021336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01021337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01021338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01021339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01021340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01021341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012059052.1; XM_012203662.1.
DR STRING; 12957.A0A158NNE4; -.
DR EnsemblMetazoa; XM_012203662.1; XP_012059052.1; LOC105622241.
DR GeneID; 105622241; -.
DR KEGG; acep:105622241; -.
DR eggNOG; KOG0587; Eukaryota.
DR InParanoid; A0A158NNE4; -.
DR OrthoDB; 2904475at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd06608; STKc_myosinIII_N_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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
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.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 28..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 996..1286
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 311..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1312 AA; 146526 MW; C52A822D5CE549F7 CRC64;
MAHNLAPSVN CSLDDIDLNA LKEPAGIFEL IEVVGNGTYG QVYKGRHTKT GQLAAIKVMD
VTEDEEEEIK LEINVLKRYS NHRNIATYYG AFVKKSSPGK DDQLWLVMEY CGAGSVTDLV
KSTKGQSLKE EWIAYISREI LRGLSYLHSN KVIHRDIKGQ NVLLTDNAEV KLVDFGVSAQ
LDRTIGRRNT FIGTPYWMAP EVIACDENPD ATYDNRSDLW SLGITALEMA ESQPPLCDLH
PMRALFLIPR NPPPRLKSKK WAKKFHGFIE TVLVKDYHQR PYTEQLLKHP FIRDQPTERQ
VRIQLKDHID RCKKRKQEKE RDDYRYSGSE NEEDEPALAG EPSSIIQAPG GDTLRRNFQQ
IQEGRTLTQD ISPQAPIAKE KPGSRSQREV PEPGPPARPA IPHRLIVVPD PQPPSRPLPP
TPRDDPRQPH KVSTPPSNHQ TPVGGGGGSG GQPVPQRNSV FKPMLPPKKP EDMEILAAQL
IELGVSQGPE APPRPNRQHK GPAASSTSNS VQSAGGNDQN NKQMPQSSSI LDQALSIESD
SDDDLEDAGG NNLRNDGTLL ASDPPKPLPE FSPFRPSSDS SSSSSHNAQN SHHEDKPKGG
APNRPLPPTP DEEETGDRTL VMKRKLSQMS DDRAMASGNR RSEIDEQLLL KEWDFTRFFQ
GFNEKLDKMK QEHQQEATDQ TSKSGSNEDH SSSSSERTLK RQEELARRKH EQHHQKQQQL
KPIHRRQESD SKLGNASSVF ARAFRRENSD FFPSARHSAY LQKSSDSRSS IFASGNRRGS
EISVAGIVGK KGGNVLNSGE PVLTDFSLCR EGPQRPRREK TESEIVFSNR HEARRCDFGR
DKDENARRRS CRPSDAAASA IVDDAGTIKS MASTTASEYS PVVTQNREGG DRSRGGGSGD
FQRSDSSPGS RPSSVLPDLL TSSPGQRQDK STSEEYRQAV KSPPFALQQK QRSFLTFGFG
AGPARRESHV NVNVTPTSHD LASDTPEIRK YKKRFNSEIL CAALWGVNLL IGTENGLMLL
DRSGQGKVYQ LISRRRFQQM EVLEGQNILV TISGKKNRVR VYYLSWLKSK ILRTDGHSDQ
VERRNGWINV GDLQGAVHFK IVKYERIKFL VIALKDSIEI YAWAPKPYHK FMAFKSFGEL
AHRPLLVDLT VEESSRLKVI YGSADGFHAV DLDSATVYDI YLPKHTQGPI CPHCIVALPN
SNGMQLLLCY DNEGVYVNTY GRVSKTMVLQ WGEMPTSVAY IGTGQIMGWG NKAIEIRSVE
SGHLDGVFMH KKAQRLKFLC ERNDKVFFSS AKGGSSCQIY FMTLNKPGMA NW
//
