GenomeNet

Database: UniProt
Entry: E1ZV73_CAMFO
LinkDB: E1ZV73_CAMFO
Original site: E1ZV73_CAMFO 
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}.
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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
//
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