ID A0A1D2MW12_ORCCI Unreviewed; 1479 AA.
AC A0A1D2MW12;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN ORFNames=Ocin01_09567 {ECO:0000313|EMBL:ODM97111.1};
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:ODM97111.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM97111.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM97111.1};
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 -!- 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=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000478};
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=2.7.11.25; Evidence={ECO:0000256|ARBA:ARBA00000106};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
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:ODM97111.1}.
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DR EMBL; LJIJ01000471; ODM97111.1; -; Genomic_DNA.
DR STRING; 48709.A0A1D2MW12; -.
DR OMA; EMQQHPH; -.
DR OrthoDB; 876955at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23257:SF947; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ODM97111.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:ODM97111.1}.
FT DOMAIN 234..298
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 312..617
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 39..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 634..684
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 160..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1479 AA; 164673 MW; E5B2B44C4987E461 CRC64;
MERIGAYLEE LSPMEQPAAS RPATNYLLGP YLANGGSRNN GYHYDDEEPL TDASNSRDHS
ATASLLSAEL ANEIATKNAK KFRSYSASSS PYISNYRLPN SKHVTNRHHQ SRHDESAQKP
AFMAMEPMTQ YQIHVGNNNV AKASFHRSLG HLIETDDSGG PSDQRGSNNF HHGISYENGG
FIRQHQSRYS DRSPRTFKKS SVELSQDCGA SSSETIMEER DSDKRDMNNS VNDKVDNIWT
AIYDYEPREL DEIPLKRGDF VRVLSQDVSL SGDAGWWVGS VGEYCGIFPS NFVTKVTKAD
LREPPKISYE ELSLAEVVGA GGFGRVHRAT WKGREVAVKA VNTDDDIETT IQSVQREATL
FWLLRHKNIV ALLGVCLAPP NICLVMEYAR GGPLNRELAK HRGQIRPSVL LNWAMQIADG
MHYLHHGAGA TIIHRDLKSS NGKCNDVFSL NFLSSLTKWI HNLCIHFHTL KATVSSFILI
LEATEPGDDF MNKTLKITDF GLAREVYNTT NMSQGGTYAW MAPEAIKGCQ FSTASDVWSY
GVVLWELLTG ETPYKGMDGL AIIYCVGVQK ISLHIPRTCP GSWRKLMEAC WAVDPHQRPS
FGAIRQELEL IAASPFLFQQ EEFYSMQESW RSEISEMVME IRNKERELLS LEEELKKMEM
IQQIQQQQQQ MKEENLRRRE EAIRQRELEV MQREIVIALL SQTSQPTPKP TPKKRRGKFR
AKALGKKEAS QIISSPSDFR HTLTVQPADR SKGIRSFSSP ETPPGSPLPR TFVLPSEGTK
GKTWGPSSIH QKERGKIISK VAESPKRWSK SAPNLDKSQK SLSVSSGGPS RSDSCENERL
VGSVPFIQLP NSATQEPRRA KKLSPIQQAL YNTAAIIAML TGFDIRKQKN QAQTTSATEE
ADTGPHQIVF LNKGFQNSGF GDSDSDLNDA LTLSSAPAAL MGSGKSSHTT YHNLQHQYRP
SLWTPGKSDG VSDSSVSQSS MSSNIPHKSI PLIATNGIAH QHDRRNKSAT STPSRSALTT
PTHRKYSPAH SHTNESENEN VQIQSPSGNR SKPHHGLAKG QHRILPNFEP GLQKRKRGSA
GTKHIYFVNE NGEVVSVNPF IHETGGYHYT TEEMQQHPHP PVTYFTQTSS RSNPYSSPYR
RAISNPSDRM IDTENSYFSS LVTHGLGPSN QRSTNPFISD QQQQQQQHHV YHNPLVYGNQ
VFEEFSPCDD AFDGRDEVLV GTMSNMRLGS GSGESGYHGA FQDTNPNSPL SSSTSASTNP
RTPLRHVSPM YSHQRTPSNL SNASSGSFGM NPSFEGDSIV SGIPAHRSSY EYGYEFRTPL
TPKLTPNPQR HQSGNNMLVT ERPATLELPR PLRSSLRKYN YSRNQGPSYN WGGDSGGGMT
NVETPPDSSL SEDSSYVSAK DSSLASMSSQ HSNPVARVRF SPIAMVCRDP MDLPVMDRTM
PLQPYRNVHS AGAASRAEYT PKLRKNMSDY GKFEFLRNF
//
