ID A0A096M7S3_POEFO Unreviewed; 1184 AA.
AC A0A096M7S3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000027464.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000027464.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 EMBL; AYCK01010167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01010168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01010169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096M7S3; -.
DR Ensembl; ENSPFOT00000025124.1; ENSPFOP00000027464.1; ENSPFOG00000022073.1.
DR GeneTree; ENSGT00950000183196; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 1..250
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 871..1158
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 269..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1184 AA; 135391 MW; BCA3327E583302CD CRC64;
YKGRHIRTGQ LAAIKVMDVA TDEEDEIKSE INMLKKYSNH RNIATYFGVF VKKQPPGIDD
QLWLVMEFCG AGSVTDLIKN TKGNSLKEDW NAYICREILR GLAHLHHHKV IHRDIKGQNV
LLTENAEVKL VDFGVSAQMD RTVGKRNTFI GTPYWMAPEV IACDENPEAT YDCKSDLWSL
GITAMEMAEG APPLCDMHPM RALFLIPRNP APRLKSKKWS KKFQSFIEST LVKSHSHRPS
TEQLLLHPFI TELPNERHLR IQLKDHIDRT KKKRGEREDE TEYEYSGSEE EDEERDKGEP
SSIINVPGES TLRRDFLRLQ QANKERSEAQ RRQQLEQKQN DEHKRLLLAE RQKRIEEQKE
QRRRLEEQLR IRREKQSEPS RDSVLRQQQQ QRERELRKRF EEQEKIRRED ERRQAAREQE
YIRRQLEEEQ RQLEILQQQL LQEQALLLEY KRKQIIEQRQ AELLQMKLQQ ERAYLVSLHL
QHLKPHQNAN SNPLARNLKN SHPSQHGKEN KSCKESPGGI VCEVEERSKM NRQSSPALQH
KVSHRISDPS LPPRSESFSS GGMQPTRTPP IHRSIEPQVP QRTTSISPAL VRKNSPNGGV
GLGPRSGSQF IRASNPDLRR SELSLDAMLQ RTSSNSSSSS SPSSQGGSSE RKGFIGQTKQ
VGTLLGANEE VKPKQEEGRE SARPSRPAEE LDLSALAKEL RELRVEEGSR PPVKVTDYSS
SSEDSESSDE DGEVLGHDGT VAVSDIPRIM PGVQGSSESY GGLAEDALGD SYDSSRDSTL
MMRESGLVSL QFGLSGSKAS FTPFVDPRVY QTSPSENDES SAAAMFANEL LRQEQARLNE
ARKISVVNVN PTNIRPHSDT PEIRKYKKRF NSEILCAALW GVNLLVGTEN GLMLLDRSGQ
GKVYNLITRR RFLQMDVLEG LNVLVTISGK KNKLRVYYLS WLRNRILHND PEVEKKQGWI
TVGELEGCVH YKVVKYERIK FLVIALKNSV EIYAWAPKPY HKFMAFKSFT ELQHRPQLVD
LTVEEGQRLK VIYGSCVGFH VIDVDSGNPY DIYIPSHIQS QVTPHAIVVL PKTDGMEMLL
CYEDEGVYVN TYGRITKDVV LQWGEMPTSV AYIHSNQIMG WGEKAIEIRS VETGHLDGVF
MHKRAQRLKF LCERNDKVFF ASVRSGGSSQ VFFMTLNRNS MMNW
//
