ID M1EFK0_MUSPF Unreviewed; 759 AA.
AC M1EFK0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AER94713.1};
RN [1] {ECO:0000313|EMBL:AER94713.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AER94713.1};
RX PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(2013).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; JP006116; AER94713.1; -; mRNA.
DR AlphaFoldDB; M1EFK0; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR038980; ATM_plant.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR PANTHER; PTHR37079:SF4; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..267
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 387..707
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 728..759
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AER94713.1"
FT NON_TER 759
FT /evidence="ECO:0000313|EMBL:AER94713.1"
SQ SEQUENCE 759 AA; 87117 MW; 6090B22F7E9318D7 CRC64;
WAKKEQSLAL SILKQMIKKL DASCAENDPD LRLIYAECLR VCGTWLAETC LENPAVIMQT
YLEKAVEVAR NYDGESSDEL RNGKMKAFLS LARFSDTQYQ RIENYMKSSE FENKQALLKR
AKEEVGLLRE HKIQTNRYTV KVQRELELDE CALRALKEDR KRFLCKAVEN YISCLLSGEG
HDMWIFRLCS LWLENSGVSD VNGMMKTDGM KIPSYKFLPL MYQLAARMGT KMMGGLGFHE
VLNNLISRIS MDHPHHTLFI ILALANANKD EFLTKPEAAR RNRIIKNAPK QSSPLDEDRT
EAANRIIHTI RSRRPQMVRS VEALCDAYII LANLDAAQWK TQRKGINIPA DQPITKLKNL
EDVVVPTMEI KVDPTGEYRN LVTIESFKAE FRLAGGLNLP KIIDCLGSDG KERRQLVKGR
DDLRQDAVMQ QVFQMCNTLL QRNTETRKRK LTICTYKVVP LSQRSGVLEW CTGTVPIGEF
LVNNENGAHK RYRPKDLSAI HCQKKMMDVQ KKSFEEKYKT FMDVCQKFQP VFRYFCMEKF
LDPAVWFEKR LAYTRSVATS SIVGYILGLG DRHVQNILIN EQSAELVHID LGVAFEQGKI
LPTPETVPFR LTRDIVDGMG ITGVEGVFRR FRRCCEKTME VMRSSQETLL TIVEVLLYDP
LFDWTMNPLK ALYLQQRPED DTELQSTPAG EDQECKRNLS DTDQSFNKVA ERVLMRLQEK
LKGVEEGTVL SVGGQVNLLI QQAMDPKNLS RLFPGWKAW
//