ID A0A2I3SGQ8_PANTR Unreviewed; 1205 AA.
AC A0A2I3SGQ8; A0A2J8PCR3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=SLK {ECO:0000313|Ensembl:ENSPTRP00000076193.1,
GN ECO:0000313|VGNC:VGNC:5785};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000076193.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000076193.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000076193.1}
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; AACZ04051143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04051144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001137318.2; XM_001137318.3.
DR AlphaFoldDB; A0A2I3SGQ8; -.
DR Ensembl; ENSPTRT00000079850.1; ENSPTRP00000076193.1; ENSPTRG00000002920.6.
DR GeneID; 450716; -.
DR KEGG; ptr:450716; -.
DR CTD; 9748; -.
DR VGNC; VGNC:5785; SLK.
DR GeneTree; ENSGT00940000156184; -.
DR OrthoDB; 2880940at2759; -.
DR Proteomes; UP000002277; Chromosome 10.
DR Bgee; ENSPTRG00000002920; Expressed in colon and 21 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd06643; STKc_SLK; 1.
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:SF1; 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:UP000002277};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 876..911
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 309..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 828..976
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1005..1039
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1080..1151
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 315..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1205 AA; 139084 MW; 9084D0313F5C02AE CRC64;
MSFFNFRKIF KLGSEKKKKQ YEHVKRDLNP EDFWEIIGEL GDGAFGKVYK AQNKETSVLA
AAKVIDTKSE EELEDYMVEI DILASCDHPN IVKLLDAFYY ENNLWILIEF CAGGAVDAVM
LELERPLTES QIQVVCKQTL DALNYLHDNK IIHRDLKAGN ILFTLDGDIK LADFGVSAKN
TRTIQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADVWS LGITLIEMAE IEPPHHELNP
MRVLLKIAKS EPPTLAQPSR WSSNFKDFLK KCLEKNVDAR WTTSQLLQHP FVTVDSNKPI
RELIAEAKAE VTEEVEDGKE EDEEEETENS LPIPASKRAS SDLSIASSEE DKLSQNACIL
ESVSEKTERS NSEDKLNSKI LNEKPTTDEP EKAVEDINEH ITDAQLEAMT ELHDRTAVIK
ENEREEKRPK LENLPDTEDQ ETVDINSVSE GKENNIMITL ETNIEHNLKS EEEKDQEKQQ
MFENKLIKSE EIKDTILQTV DLVSQETGEK EANIQAVDSE VGLTKEDTQE KLGEDDKTQK
DVISNTSDVI GTYEAADVAQ KVDEDSAEDT QSNDGKEVVE VGQKLINKPM VGPEAGGTKE
VPIKEIVEMN EIEEGKNKEQ AINSSENIMD INGEPGTTEG EEITESSSTE EMEVRSVVAD
TDQKALGSEV QDASKVTTQI DKEKKEIPVS IKKEPQVTAV SQPTEPQPVL IPSININSDS
GENKEEIGSL SKTETILPPE SENPKENDND SGTGSTADTS SIDLNLSISS FLSKTKDSGS
ISLQETRRQK KTLKKTRKFI VDGVEVSVTT SKIVTDSDSK TEELRFLRRQ ELRELRFLQK
EEQRAQQQLN SKLQQQREQI FRRFEQEMMS KKRQYDQEIE NLEKQQKQTI ERLEQEHTNR
LRDEAKRIKG EQEKELSKFQ NMLKNRKKEE QEFVQKQQQE LDGSLKKIIQ QQKAELANIE
RECLNNKQQL MRAREAAIWE LEERHLQEKH QLLKQQLKDQ YFMQRHQLLK RHEKETEQMQ
RYNQRLIEEL KNRQTQERAR LPKIQRSEAK TRMAMFKKSL RINSTATPDQ DRDKIKQFAA
QEEKRQKNER MAQHQKHENQ MRDLQLQCEA NVRELHQLQN EKCHLLVEHE TQKLKELDEE
HSQELKEWRE KLRPRKKTLE EEFARKLQEQ EVFFKMTGES ECLNPSTQSR ISKFYPIPSL
HSTGS
//
