ID E1ZV73_CAMFO Unreviewed; 1290 AA.
AC E1ZV73;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=EAG_09452 {ECO:0000313|EMBL:EFN74932.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN74932.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL434441; EFN74932.1; -; Genomic_DNA.
DR STRING; 104421.E1ZV73; -.
DR InParanoid; E1ZV73; -.
DR OMA; LEKRNGW; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFN74932.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFN74932.1}.
FT DOMAIN 28..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 974..1264
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 292..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 143859 MW; 62213F61B5CCC225 CRC64;
MAHNLAPSVN CSLDDIDLNA LKEPAGIFEL IEVVGNGTYG QVYKDEEEEI KLEINVLKRY
SNHRNIATYY GAFVKKSSPG KDDQLWLVME YCGAGSVTDL VKSTKGQSLK EEWIAYISRE
ILRGLSYLHS NKVIHRDIKG QNVLLTDNAE VKLVDFGVSA QLDRTIGRRN TFIGTPYWMA
PEVIACDENP DATYDNRSDL WSLGITALEM AESQPPLCDL HPMRALFLIP RNPPPRLKSK
KWAKKFHGFI ETVLVKDYHQ RPYTEQLLKH PFIRDQPTER QVRIQLKDHI DRCKKRKQEK
ERDDYRYSGS ENEEDEPALA GEPSSIVQAP GGDTLRRNFQ QIQEGRTLTQ DVPPQAPAAK
EKPGNRSQRE VPEPGPPARP AIPHRLIVVP DPQPPSRPLP PTPRDDPRQP HKVSTPPSNH
QTPTGGGGSG GSGGQPAPQR NSVFKPMLPP KKPEDMEILA AQLIELGVSQ GPEAPPRPNR
QHKGLAASST SNSVQPASGN DQNNKQMPQS SSILDQALSI ESDSDDDLED AGGNNLRNDG
TLLASDPPKP LPSSDSSSSS SHNAQNSHHE DKPKGGAPNR PLPPTPDEEE SGDRTLVMKR
KLSQMSDDRA TASGNRRSEI DEQLLLKEWD FTRFFQGFNE KLDKMKQEHQ QEAAGQASKS
TGSNEDRSSS SNERTLKRQE QLARRKHEQH HQKQHQLKPV HRRQESDSKL GNASNAFTRA
FRRENSDFFP SARHSAYLKS SDSSQRSSIF ASGNRRGSEM SVAGIIGKKG SGGGGLNSGE
PILTDFSLNR EGPQRPRREK TESEIVFGNR HEARRFDFGR DKDENARRRS CRPSDATASA
VVDDAGTIKS TASTTASEYS PIVTQNREGD RSRGGGDFQR SDSSPGSRPS SVLPDLLTSS
PGQRQDKSTS EEYRQAVKSP PPFALQQKQR SFLTFGFGAG PARRESHVNV NVTPTSHDLA
SDTPEIRKYK KRFNSEILCA ALWGVNLLIG TENGLMLLDR SGQGKVYQLI SRRRFQQMEV
LEGQNILVTI SGKKNRVRVY YLSWLKSKIL RTDGHSDQVE RRNGWINVGD LQGAVHFKIV
KYERIKFLVI ALKDSIEIYA WAPKPYHKFM AFKSFGELAH RPLLVDLTVE EGTRLKVIYG
SADGFHAVDL DSATVYDIYL PKHTQGPICP HCIVALPNSN GMQLLLCYDN EGVYVNTYGR
VSKTMVLQWG EMPTSVAYIG TGQIMGWGNK AIEIRSVESG HLDGVFMHKK AQRLKFLCER
NDKVFFSSAK GGSSCQIYFM TLNKPGMANW
//