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DescriptionSubName: Full=Pim proto-oncogene, serine/threonine kinase,-related 173 {ECO:0000313|Ensembl:ENSDARP00000116433}; Flags: Fragment;
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MyHits synonymsQ1LX85_DANRE , Q1LX85 , 02C1BD5A61184BB7
match map segment
ipat:PROTEIN_KINASE_ST ismart:S_TKc ipfam:Pkinase ipat:PROTEIN_KINASE_ATP iprf:PROTEIN_KINASE_DOM  
Legends: 1, ACT_SITE Proton acceptor. {ECO:0000256|PIRSR:PIRSR037993-1}; 2, BINDING ATP. {ECO:0000256|PIRSR:PIRSR037993-2}; 3, BINDING ATP; via carbonyl oxygen. {ECO:0000256|PIRSR:PIRSR037993-2}; 4, NON_TER {ECO:0000313|Ensembl:ENSDARP00000116433}; 5, ipat:PROTEIN_KINASE_ST [T]; 6, ipat:PROTEIN_KINASE_ATP [T].
ID   Q1LX85_DANRE            Unreviewed;       281 AA.
AC   Q1LX85;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   15-MAR-2017, entry version 80.
DE   SubName: Full=Pim proto-oncogene, serine/threonine kinase,-related 173 {ECO:0000313|Ensembl:ENSDARP00000116433};
DE   Flags: Fragment;
GN   Name=pimr173 {ECO:0000313|Ensembl:ENSDARP00000116433,
GN   ECO:0000313|ZFIN:ZDB-GENE-041210-89};
GN   Synonyms=pcloa {ECO:0000313|ZFIN:ZDB-GENE-041210-89},
GN   si:dkey-108d22.5 {ECO:0000313|ZFIN:ZDB-GENE-041210-89};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000116433, ECO:0000313|Proteomes:UP000000437};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000116433, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116433,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000116433}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116433};
RG   Ensembl;
RL   Submitted (MAY-2013) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSDARP00000116433}.
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DR   EMBL; BX469931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; Q1LX85; -.
DR   STRING; 7955.ENSDARP00000116433; -.
DR   PaxDb; Q1LX85; -.
DR   Ensembl; ENSDART00000140018; ENSDARP00000116433; ENSDARG00000070015.
DR   ZFIN; ZDB-GENE-041210-89; pimr173.
DR   eggNOG; KOG0583; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   GeneTree; ENSGT00760000119045; -.
DR   HOVERGEN; HBG106846; -.
DR   InParanoid; Q1LX85; -.
DR   PhylomeDB; Q1LX85; -.
DR   TreeFam; TF320810; -.
DR   Proteomes; UP000000437; Chromosome 4.
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:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017348; PIM1/2/3.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF037993; STPK_Pim-1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR037993-2,
KW   ECO:0000256|RuleBase:RU000304};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Kinase {ECO:0000256|RuleBase:RU000304};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR037993-2,
KW   ECO:0000256|RuleBase:RU000304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|RuleBase:RU000304}.
FT   DOMAIN        7    281       Protein kinase.
FT                                {ECO:0000259|PROSITE:PS50011}.
FT   ACT_SITE    140    140       Proton acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR037993-1}.
FT   BINDING      36     36       ATP. {ECO:0000256|PIRSR:PIRSR037993-2}.
FT   BINDING      93     93       ATP; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR037993-2}.
FT   BINDING     100    100       ATP. {ECO:0000256|PIRSR:PIRSR037993-2}.
FT   NON_TER       1      1       {ECO:0000313|Ensembl:ENSDARP00000116433}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       136    148       ipat:PROTEIN_KINASE_ST [T]
FT   MYHIT         7    280       ismart:S_TKc [T]
FT   MYHIT         7    218       ipfam:Pkinase [T]
FT   MYHIT        13     36       ipat:PROTEIN_KINASE_ATP [T]
FT   MYHIT         7    281       iprf:PROTEIN_KINASE_DOM [T]
SQ   SEQUENCE   281 AA;  31878 MW;  02C1BD5A61184BB7 CRC64;
     DIILRHYKIG DKLGKGGFGS VYKATRRRDG LKVAVKCTVK SSKMKEITVP GYDKPLPTEI
     ALTIMANNGP YVPEIIKLLD WEDNDDHYVI IMERPIPCMD LFCFLNHNNG PLDEKTGRHI
     MRQAIHAVSV CFNRGVFHRD IKLENLLVNP DTLEVKLIDF GCGAIAKESG YKVFCGTREY
     FPPEYELYGR YHAQPATVWS LGIVLFAMMC WALPTVSDHS LIRDYLWTRT DLSKGHGVRQ
     EKQLSNPSTP EDCCIGLLFV LYCCLVNFCN NAGQLTYECL C
//