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Database: UniProt
Entry: A0A091E0E0_FUKDA
LinkDB: A0A091E0E0_FUKDA
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ID   A0A091E0E0_FUKDA        Unreviewed;       967 AA.
AC   A0A091E0E0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, 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   ORFNames=H920_10086 {ECO:0000313|EMBL:KFO28546.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO28546.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO28546.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO28546.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KN122754; KFO28546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091E0E0; -.
DR   STRING; 885580.ENSFDAP00000003012; -.
DR   eggNOG; KOG0584; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
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   CDD; cd14033; STKc_WNK4; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR   PANTHER; PTHR13902:SF114; SERINE_THREONINE-PROTEIN KINASE WNK4; 1.
DR   Pfam; PF12202; OSR1_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO28546.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          50..308
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          774..967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..674
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..689
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..800
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..947
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   967 AA;  104407 MW;  9A500A4E9FA78445 CRC64;
     MQGEETCSLC PPSSPHGLGP RSANPCGPRC LRSLCLPPCL SQAGAGASEG QFDIEIGRGS
     FKTVYRGLDT DTTVEVAWCE LQTRKLSRAE RQRFSEEVDM LKGLQHPNIV RFYDSWKSVL
     RGQVCIVLVT ELMTSGTLKT YLRRFREMKP RVLQRWSRQI LRGLHFLHSR APPILHRDLK
     CDNVFITGPT GSVKIGDLGL ATLKRASFAK SVIGTPEFMA PEMYEEKYDE AVDVYAFGMC
     MLEMATSEYP YSECQNAAQI YRKVTSGTKP NSFYKVKMPE VKEIIEGCIR TDKNQRFTIQ
     DLLAHAFFRE ERGVHVELAE EDDGQKPDLK LWLRMEDARR GGRPRGNQAI EFLFQLGRDV
     AEEVAQEMVA LGLVCEADYQ PVARAVRERV AAIQRKREKL RTAREPEALP PKPGPVPVTI
     PVAPGAPGAF PPEPEEPEAD QHQPFLFRHA SCSSTTSDCE TDGYLSSSGC LDASDPALAP
     PGEVPPSPAK PWLHLPPAFA VSVPCSGPGS DFSPGDSYAS DAASGLSDMG EGMGQMRRPP
     GKTPRRRPRS RLRVTSVSDQ NDRVVECQLQ THNSKTVTFR FDLDGDSPED IAAAMVYNEF
     ILPAEREGFL RRIREVIQRV ETLLKRDPGP AEAAEDAPGP QEEPAPLPAH EDLPRELQSS
     SGPGQRSWAA FCTSPTPPGT PPSPAAPVFP SPRLFSTSAQ PSSCPPQLPS CAFPFLTGAV
     QAPSSLLPLG SLPCSPQSPL CPSPATPAAP LLSLASAFSL AVMTVAQSLL SPPPGTLAQC
     PPAPPGPQPG LPPPPAPGGQ ENLLPYTAKA EAQSEATPNP TRPVLGEARL APISEEGKPQ
     LVGRFQVTSS KEPVECPALQ PAASAALPGS PKPPTPPQSP ESSDTEDSAG GRPGTREALA
     ESDRAAEGLG TVLDDGMDPR AGDSPLAPPS PVWTNYSYSS LCLSSEESES SGEDEEFWAE
     LHSLRQK
//
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