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Database: UniProt
Entry: A0A1U8BLR4_MESAU
LinkDB: A0A1U8BLR4_MESAU
Original site: A0A1U8BLR4_MESAU 
ID   A0A1U8BLR4_MESAU        Unreviewed;      1319 AA.
AC   A0A1U8BLR4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=Mink1 {ECO:0000313|RefSeq:XP_012967120.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012967120.1};
RN   [1] {ECO:0000313|RefSeq:XP_012967120.1}
RP   IDENTIFICATION.
RG   RefSeq;
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};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   RefSeq; XP_012967120.1; XM_013111666.2.
DR   OrthoDB; 2904475at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_012967120.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777,
KW   ECO:0000313|RefSeq:XP_012967120.1}.
FT   DOMAIN          1..234
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1006..1293
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          244..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..280
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..549
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..639
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..709
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..812
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..831
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        892..920
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1319 AA;  149138 MW;  705CC8A2799E2B1E CRC64;
     MDVTEDEEEE IKQEINMLKK YSHHRNIATY YGAFIKKSPP GNDDQLWLVM EFCGAGSVTD
     LVKNTKGNAL KEDCIAYICR EILRGLAHLH AHKVIHRDIK GQNVLLTENA EVKLVDFGVS
     AQLDRTVGRR NTFIGTPYWM APEVIACDEN PDATYDYRSD IWSLGITAIE MAEGAPPLCD
     MHPMRALFLI PRNPPPRLKS KKWSKKFTDF IDTCLIKTYL SRPPTEQLLK FPFIRDQPTE
     RQVRIQLKDH IDRSRKKRGE KEETEYEYSG SEEEDDSHGE EGEPSSIMNV PGESTLRREF
     LRLQQENKSN SEALKLQQQQ QQQQQQRDPE AHIKHLLHQR QRRIEEQKEE RRRVEEQQRR
     EREQRKLQEK EQQRRLEDMQ ALRREEERRQ AEREQEYIRH RLEEEQRQLE ILQQQLLQEQ
     ALLLEYKRKQ LEEQRQSERL QRQLQQEHAY LKSLQQQQQQ QQLQKQQQQQ QILPGDRKPL
     YHYGRGINPA DKPAWAREVE ERARMNKQQN SPLAKTKPSS TGPEPPISQA SPSPPGPLSQ
     TPPMQRPVEP QEGPHKSLVA HRVPLKPYAA PVPRSQSLQD QPTRNLAAFP ASHDPDPAAV
     PTPTATPSAR GAVIRQNSDP TSEGPGPGPN PPSWVRPDNE APPKVPQRTS SIATALNTSG
     AGGSRPAQAV RARPRSNSAW QIYLQRRAER GAPKPPGPPA PPPGPPSASS NPDLRRSDPG
     WERSDSVLPA SHGHLPQAGS LERNRNRVEA STKLDSSPVL SPGNKAKPED HRSRPGRPAS
     YKRAIGEDFV LLKERTLDEA PRPPKKAMDY SSSSEEVESS EDDDEEGDGE PSEGSRDTPG
     GRSDGDTDSV STMVVHDVEE IAGNQPPYGG GTMVVQRTPE EERSLLLADS NGYTNLPDVV
     QPSHSPTENS KGQSPPAKDG GSDYQSRGLV KAPGKSSFTM FVDLGLYQPG GSGDTIPITA
     LVGGEGGRLD QLQFDVRKGS VVNVNPTNTR AHSETPEIRK YKKRFNSEIL CAALWGVNLL
     VGTENGLMLL DRSGQGKVYG LIGRRRFQQM DVLEGLNLLI TISGKRNKLR VYYLSWLRNK
     ILHNDPEVEK KQGWTTVGDM EGCGHYRVVK YERIKFLVIA LKNSVEVYAW APKPYHKFMA
     FKSFADLPHR PLLVDLTVEE GQRLKVIYGS SAGFHAVDVD SGNSYDIYIP VHIQSQITPH
     AIIFLPNTDG MEMLLCYEDE GVYVNTYGRI IKDVVLQWGE MPTSVAYICS NQIMGWGEKA
     IEIRSVETGH LDGVFMHKRA QRLKFLCERN DKVFFASVRS GGSSQVYFMT LNRNCIMNW
//
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