ID M7BMB3_CHEMY Unreviewed; 1045 AA.
AC M7BMB3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=UY3_04409 {ECO:0000313|EMBL:EMP38374.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP38374.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
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DR EMBL; KB519916; EMP38374.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BMB3; -.
DR STRING; 8469.M7BMB3; -.
DR eggNOG; KOG2377; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0035658; C:Mon1-Ccz1 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR CDD; cd05146; RIO3_euk; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR040371; RMC1.
DR InterPro; IPR009755; RMC1_C.
DR InterPro; IPR049040; RMC1_N.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR12897; COLON CANCER-ASSOCIATED PROTEIN MIC1; 1.
DR PANTHER; PTHR12897:SF4; REGULATOR OF MON1-CCZ1 COMPLEX; 1.
DR Pfam; PF01163; RIO1; 1.
DR Pfam; PF07035; RMC1_C; 1.
DR Pfam; PF21029; RMC1_N; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1045
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004080155"
FT DOMAIN 178..423
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 77..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 119579 MW; D41F408E57511D90 CRC64;
MLTELLFPFF FFIVLSVAEG PFITGENTDT SSDLMLAQML QMEFDREYDA QLRREEKKFN
GDSKVSISFE NYRKVHPYED SDSSEDEVDW QDTRHDPYRA DKPTTTPKKG FIGKGKEITT
KHDEVVCGRK NTARMENFGP DFQVGDGIGM DLKLSNQVFN ALKQHAYSEE RRSARLHEKK
EHSTAEKAVD PKTRLLLYKM VNAGILETIT GCISTGKESV VFHAYGGKTG MDDKAVPPEC
ALKVFKTTLN EFKNRDKYIK DDYRFKDRFS KLNPRKVIRM WAEKEMHNLT RMQKAGIPCP
EVVMLKKHIL VMSFIGQDQV PAPKLKEVKL NSEDMKKAYY QILHMMQQLY KECSLVHADL
SEYNMLWHDG KVWLIDVSQS VEPTHPHGLE FLFRDCRNVS QFFQKGGVSE ALNERELFNA
VSGLNIAADN EADFLAEVFA VRSGGATGVV VKGLEDKNPI SFRMEDKGEV KCIKFSLGNK
ILAVQRTSKS VDFLNFIPDS PQLEYTQECK TKNANILGFC WTSSTEIVFI TDQGIEFYQV
LPEKRSLKLV KNQNINVNWY MYCPESSVIL LSTTVLGNVL QPFYFKGGTM SKLSKFEIEL
PAVPKSSKLS LSERDIAMAT IYGQLYVLYL RHHSRTSNST GAEVVLYHLP RESSCKKMHI
LKLNRTGKFA LNVVDNLVVV HHQDTETSVI FDIKLKGEFD GTVTLHQLVL PARSIQPYQI
PVADSSSWIV FQPDIIISAS EGYLWNLEVK LEPVVNLLPD KGKLMDFLLQ RKECKMVILS
VCSQMLSEPD RGTLAVIATV FDKLNHEYKK YLEAEQSYTM VVETGQSRGN PLLKRPVRTQ
AVIDQSDMYT HVLSVFTEKK EAPHKFTIAV LMEYIRSLNQ FQIAVQHYLY ELVIKTLVQH
NLFYMLHQFL QYHVLSDSKP LACLLLSLES IYPPAHQLSL DMLKRLSTAN DEIVEVLLSK
HQVLAALRFI RGVGGHDSVS ARKFLDAAKQ ADDNMLFYTI FRFFEQRNQR LRGNPNFTPG
EHCEEHVTFF KQIFGEHALM KPTTF
//
