ID A0A0T6AWL3_9SCAR Unreviewed; 960 AA.
AC A0A0T6AWL3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:KRT79539.1};
GN ORFNames=AMK59_6841 {ECO:0000313|EMBL:KRT79539.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT79539.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT79539.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT79539.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT79539.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KRT79539.1}.
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DR EMBL; LJIG01022630; KRT79539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6AWL3; -.
DR OrthoDB; 5388799at2759; -.
DR Proteomes; UP000051574; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06624; STKc_ASK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046872; DRHyd-ASK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR043969; MAP3K_PH.
DR InterPro; IPR025136; MAP3K_TRAF-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11584:SF369; APOPTOTIC SIGNAL-REGULATING KINASE 1, ISOFORM C; 1.
DR PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF19039; ASK_PH; 1.
DR Pfam; PF20309; DRHyd-ASK; 1.
DR Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:KRT79539.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000051574};
KW Transferase {ECO:0000313|EMBL:KRT79539.1}.
FT DOMAIN 614..872
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 960 AA; 109305 MW; E33CF532ECC61C0E CRC64;
MLPPSLLMEP DADCRSTDSI GSHSDFSTHT MQPPISTSSM MTRPLMDVVI VMDVHQTDHL
AHRKRALEDV KQACAQIGAN LNHIQFEKLD FGESNVVSSF YNADVTIIDL SLTTQRHTLF
YHLGVRESFN MKQNILFCND TDSEATVRLK LSCTTYTFVS YTLSKDESVC VTTSGPGTEP
SELLHQRLRK HLQDVEVQSK AHMKEKFLAD LKKLKETHSA GDLKISLHAI RKRLDDPNVL
SGDVVLNMLF CFRDIQDYDA MVQLVDDLNT LPVSRKFVNS YILYWYAFAL NRRKLAGDRE
KALKVCVTAL QKKENHFPDM LCLCGRIYKD KFIESNHMDQ DSLKQAIHWY KEGFKVQPNE
YAGINLATLL VIGGEEMGKS DELESIGMVL INLIGKKGSL SSLKDYWDVA TFFEISVLIQ
HYANAVQAAE CMFKLKPPDW YLKSTVGNIQ LIDKFRRRKD EERSPEEQIF HFWMEFFYEA
TKAPAEDSIR FPALVHEPNK ELMPTYLCVN LGAEQQSIQI TNLCLKSLQH KCTQIHDWEF
TSPMIRSVSL YKRDERCLFL YVHQNSDDFQ IYFPSGACRE RFYSLVLKLT VDQEGLMENE
PLREIKYEYE RDEQGKKVVL GKGTYGIVYA ARDLNTQVRI AVKEIPEQNL RAVQPLHEEI
RLHSQLRHRN IVQYLGSVSE DSYFKIFMEQ VPGGSLSALL RSKWGPLKQN EHTIAFYTKQ
ILEGLKYLHD QNIVHRDIKG DNVLVNTYSG VVKISDFGTS KRLAGLSPIT ETFAGTLQYM
APEVIDKGQR GYGAPADIWS LGCTVVEMAT GKTPFIELGS AQAAIFKVGF YKDHPQVPEE
LSDRAKNFIL RCFEPDPDKR ATAQQLLEDP FLCERKKSVR LNTEYNRSVS VPADRVVHRL
SGHSSAPNQT PTTPDLDSQN RGALLPPIQM PSALSFNSLA STPSIDLDPD DHDGTQRRNS
//
