ID A0A1D2MYB5_ORCCI Unreviewed; 906 AA.
AC A0A1D2MYB5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=Ocin01_08685 {ECO:0000313|EMBL:ODM97982.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM97982.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM97982.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM97982.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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}.
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:ODM97982.1}.
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DR EMBL; LJIJ01000391; ODM97982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2MYB5; -.
DR STRING; 48709.A0A1D2MYB5; -.
DR OMA; NDESVHC; -.
DR OrthoDB; 152877at2759; -.
DR Proteomes; UP000094527; 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; 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.
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:ODM97982.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038172};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Transferase {ECO:0000256|PIRNR:PIRNR038172}.
FT DOMAIN 20..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 546..871
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 319..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 906 AA; 102370 MW; 2F3F29096C4C7112 CRC64;
MAQAQTISAD ISRRNPQDEY ELIQRIGSGT YGDVYKAKRL SNGEFAAIKV IKLEPGDDFA
VIQQEILMMK DCRHPNIVAY YGSYLRRDRL WICMEYCGGG SLQDIYHITG PLTESQIAYV
CKETLRGLAY LHALGKMHRD VKGANILLTD GGDVKLADFG VSAQLTATLG KRRSFIGTPY
WMAPEVAAVE RKGGYNELCD VWALGITAIE LAELQPPMFD LHPMRALILM AKTSFKPPTL
KDRDKWSVNF HNFVKVALTK NPKKRPTAER ILLHPFLMGD LTKRTALELL HKVSNPNVSF
YDMDPDEEGT VQNVPHRIAS RRTDRVDQRT PSEIRNVTPD LGQRRRHPHP QDNDYNNDHL
PLPFEWNDRG SDDADRKATL PMGDPMSVSS HELMDSRNHN LSNGIARKAD RRRHNSFSGE
IEELTSRLDS TLTRGSIDSP VELRVSAHAS PRRQQTNRTL SDSAAMLSSS PDLSSRMPTT
SGGDQQNGRP DLTAGLPPVP PPRTRVERKN KHEDNGSPPR LVSNGLPPTP KVHMGACFMK
VFNGCPLRMH CCVSWVNPET RDQHILLGAE EGIYTLNLNE LHETAMDQLY PRRTIWMFVV
KDVLMSLSGK TVQLYRHDLI GLHASINNKH TLRFSLRMSN KIPEKLVPRK FALTTKVADT
KGCMKCCVRR NPYNGYRYLC GAVPSGVFLM QWYDPLNKFM LLKHFDFCIT SPLKTFEMII
TPDVEYPLVC INVRREPDTP NLKLDLLNLN TSSSWLHSSE LSNEVDKSAT VIHRKDYMNV
VSVTQLEKDT LMVCYDSIAK FVNINGKVKS SRKTCSEIKF DFQIDSVVCL TDSVLAFHKH
GMQGRSFRQG DITQEITDQS RIFRLLGSDR EDKVILVESR PNPTGPPLTT EEGVNLYTLA
GHEATF
//
