ID A0A4D9EV08_9SAUR Unreviewed; 1122 AA.
AC A0A4D9EV08;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=DR999_PMT07015 {ECO:0000313|EMBL:TFK09970.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK09970.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK09970.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK09970.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK09970.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK09970.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK09970.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK09970.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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:TFK09970.1}.
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DR EMBL; QXTE01000047; TFK09970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4D9EV08; -.
DR STRING; 55544.A0A4D9EV08; -.
DR Proteomes; UP000297703; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21777; MobB_LATS2; 1.
DR CDD; cd14398; UBA_LATS2; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF149; SERINE_THREONINE-PROTEIN KINASE LATS2; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000297703};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 97..138
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 702..1007
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1008..1086
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 22..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 731
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1122 AA; 126030 MW; F90AA595757EC49B CRC64;
MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KSSGQGLPVG PGSETSLDPK ILIGKDAARQ
QQMRPTAKFG PYQKALREIR YSLLPFANES GTSASTEVNR QMLQELVNVG CDQEMAVRAL
KQTGSRSIEA ALEYISKMGY LDPRNEQIVR VIKQTSPGKG IVPNNVARRP SFEGSNESFP
SYHQISNTAY EGTSFGTEGA NMLSDVPRTY MDYLLSASQS AAMNAAVQRP SGVGSHSTPG
SHQQKTYSAN MDSPVINYPV TNHNSQALQL QAPHGSNSPH YSRQHMMVQG EPMGYGVQRS
PSFQNKMQQE GGYANLPNKG TVQNNSGHAF QQAPASLYIH THHKQTSPSP HQMHVIARGP
AFANDFSDSP PQNLIAPSRN SLNMDLYDMN NPQVQQWQTA APSHRDSLQN PGIETSPRQH
VSFRPDASVP SRTNSFNNHQ QQQVPVSIRQ VPPGKPDPSI TSPNTITAVT SAHILQPVKS
MRVMRPEPQT AVGPSHPGWL PAQAPPVDSL EIIEQHPLPV GGANAYQLDV DYSNQEPRCP
PPPYPKHLLL PGSSEQFDIN CLCMGVEQTL RGVPNSTCNK AEENSERNDK SSKNAKVEKT
SKDKKQIQTS PVPVRKNAKD EEKRESRIKS YSPFAFKFYM EQHVENVLKT YQQKINRRLQ
LEQEMAKAGL CEAEQEQMRK ILYQKESNYN RLKRAKMDKS MFVKIKTLGI GAFGEVCLAC
KVDTHALYAM KTLRKKDVLN RNQVAHVKAE RDILAEADNE WVVKLYYSFQ DKENLYFVMD
YIPGGDMMSL LIRMEVFPEH LARFYIAELT LAIESVHKMG FIHRDIKPDN ILIDLDGHIK
LTDFGLCTGF RWTHNSKYYQ KGSHSRQDSM EPSDLWDDVS NCRCGDRLKT LEQRAKKQHQ
RCLAHSLVGT PNYIAPEVLL RKGYTQLCDW WSVGVILFEM LVGQPPFLAS TPTETQLKVI
NWESTLHIPL QIKLSPEASD LITKLCCAAE ERLGRSGADD IKAHPFFNSI DFSTDIRRQT
APYVPKISHP MDTSNFDPVE EESPWNDTSG DSTRTWDPLA SSNSKHTEHA FYEFTFRRFF
DDNGYPFRYP KPSGIESSQS EKSDAENKDV VDQTGACQPV YV
//
