ID K7G6S8_PELSI Unreviewed; 1186 AA.
AC K7G6S8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000015989.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
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).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000015989.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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};
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DR EMBL; AGCU01126594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01126595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01126596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7G6S8; -.
DR STRING; 13735.ENSPSIP00000015989; -.
DR Ensembl; ENSPSIT00000016064.1; ENSPSIP00000015989.1; ENSPSIG00000014135.1.
DR eggNOG; KOG0579; Eukaryota.
DR GeneTree; ENSGT00940000156818; -.
DR HOGENOM; CLU_001965_3_0_1; -.
DR OMA; QMRSVRR; -.
DR TreeFam; TF351445; -.
DR Proteomes; UP000007267; 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-EC.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR46538:SF4; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
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.
DR PROSITE; PS50151; UVR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..291
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 866..901
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 314..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 828..882
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1107..1160
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 422..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1186 AA; 135335 MW; 73E3FEFC67F9C8BB CRC64;
MAFLLKLFRL GLEKKKVRHY ENVKRDVNPE DVWTVLGELG DGAFGKVFKA QNRVTGVLAA
AKVIDTQGEE ELEDYMVEID ILAGCDHPNI VKLLDALYWD GRLWILIEFC PGGAVDAAML
ELEKGLTEEQ IRVACRQILL ALQYLHSHKI IHRDLKAGNV LLTLEGDVKL ADFGVSAKNA
RTLQRRASFL GTPYWMAPEV VQCETSKENP YNYKADIWSL GITLIEMAEM EPPYHELNPM
RVLLKISKSH PPTLCYPKRW SEEFKDFLRK SLERNPEARW SAIQLLQHPF VAEVSEKRPL
RELIAEARAE VMEEVEEEEE EEGHVLKGNI RPRGPGQPAP QRAPADPGLP WGERDQLQQK
NCIAKSVLEG IQTSTGGLSI TESWRHVWPK GSGTCVNQGS SGVRLQTENC LPAAEVRAIA
EQTPCESEKE QLPKELAQSD ENQQEPEPSS VTNETEGDVE NTNENIKVGS AALEEQQEPH
CMGEAETVGN RFSKETEVLS KEERGKTEEE IPDYRRGPVN EDPQSGVDTS PKEIMGPARE
ETERVPVKQV VEEYFNGDQS AEVDTSSQEI LGPAKERAQE GNTTLGYLNL EAENSVVDIS
PEESLVPAKA HSGEKMKDTI DSSRGGPLHV VEDRNHKAEG GVHGRETAKE ERRPPGEDLA
EAAPDSEGAS GAGKEEISAP LGNGAVPEPQ RAPAEHPKVQ KRVSFGEEPL EQAADRGAMR
DGKDPSGLLP IPERRWEWSH RHSGKGLPND GGWLALGCPS APGSLASCGQ AYLSEPVALR
RTVRKTRKFV VDGKEISVTT SKTISKVDMK DEKMRSERRQ ELHELRLLQK EEQRAQSHLE
QKLHQQREQM FRHIEQEMMS KKQYYDQEVE SLERQHRQAR ERQEHEFTTR LRDEAKRLKA
LQEKDYGKKL PALRGNRREV PACREPTVSS LLRTLQTGCP GPASCDSNWQ EQRFLQQQQE
ELNLALQRIV QEHKKKVTSI EWECVSKIHS LKRARESVVW SVEQGHLQEK YHLFKQQVKE
QYSLQQQQLN KRQEQETERM TRFHQRLLAE LRQQQAHQQV QLLKTQRGEA KLRLAMFKES
LKIQEVMGAE QRDRTKQFLQ QEEPRQRAEV QRQQQQHKQQ LQDLQQHLAE SLSELEQLQR
EKLRLLVEQE KKQLKGLDEE HTMELSEWKQ RLAARKEMLE EELAHR
//
