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Database: UniProt
Entry: M4AM75_XIPMA
LinkDB: M4AM75_XIPMA
Original site: M4AM75_XIPMA 
ID   M4AM75_XIPMA            Unreviewed;      1441 AA.
AC   M4AM75;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000015569.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000015569.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000015569.2};
RG   Ensembl;
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   STRING; 8083.ENSXMAP00000015569; -.
DR   Ensembl; ENSXMAT00000015592.2; ENSXMAP00000015569.2; ENSXMAG00000015491.2.
DR   eggNOG; KOG0032; Eukaryota.
DR   GeneTree; ENSGT00940000153424; -.
DR   HOGENOM; CLU_002849_2_0_1; -.
DR   InParanoid; M4AM75; -.
DR   OMA; RSMHDFQ; -.
DR   OrthoDB; 4580305at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR   GO; GO:0010033; P:response to organic substance; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd08782; Death_DAPK1; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.5.460; Single helix bin; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24342:SF17; DEATH-ASSOCIATED PROTEIN KINASE 1; 1.
DR   PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 7.
DR   PROSITE; PS50088; ANK_REPEAT; 8.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          378..410
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          411..443
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          444..476
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          477..509
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          510..542
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          543..575
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          576..608
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          609..641
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          681..953
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          1326..1405
FT                   /note="Death"
FT                   /evidence="ECO:0000259|PROSITE:PS50017"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1441 AA;  160050 MW;  9CB3B52A37A87B43 CRC64;
     MTVFNPDNVE EFYQIGDELG SGQFAVVRRC RHRRTGAEYA AKFIKKRRNK SGRRGVAKED
     IEREVNILKE IQHPNVITLH EVFESKAEVI LILELVAGGE LFDFLAEKES LSEEEATQFL
     KQILDGVLYL HSKQIAHFDL KPENIMLLNR SMPHPRIKLI DFGLAHKIDF GNDFKNIFGT
     PEFVAPEVVN YEPLGLEADM WSIGVITYIL LSGASPFLGD NKQETLANVS AVDYTFDEEF
     FSNTSALAKD FIKRLLIKDP KKRMTIQDTL LHPWIKPKDT QQALSRKESA VNMEKFKKFA
     ARRKWKQSVR LISLCNRLSR SFLSRSNISV ARSDDTLDEE DSFVMKAIIH AINDDNVPGL
     QHLLGSLNSY DVNQPNKHGT PPLLIAAGCG NIQIIEVLMR KGAEIQANDK SGANAVYYAA
     RHGHVDTLRF LHEKKCPLDV QDKSGETALH VAARYGNVDV VSYLCSIRAN PDLTDREQET
     PLHCAAWHGY SAVARALCQA GCHVDAKNRE GESPLLTASA RGFVDIVECL VEHKADLEAT
     DKDGHTALHL AVRRCQVEVV RCLLRRRCHL DQQDRHGNTP LHIACKDGNL AVVTAMCSAK
     ASLDLPNKHG RTPLHLAAGN GSLEVVRHLC LAGANIDAVT NDGKTAEDLA SADHHEHIVD
     LLGKLKKDNH KLSYIQQLRP TQTIQPRIKL KLFGHSGSGK STLLESLKCG ILRSFFRRRR
     TTRMTNSARH PNSPVNSKPA VSVSISNLYP GCENVSVRSR SMMFEPSLTK GVLEVFSPVH
     SALSAADEQA TKAIDIQHAN IHGVGDFSVW EFSGNPVYHC SYDYFAANDV TAIHLVLFSL
     EEPYETQLGH ITYWLNLLKA LTPPQDNIVF GGRIQQPLSV VLVATHADLA DIARAFSGEF
     SYDKERALLK EVRNRFGNDL QISDKLFVMD AGASNSKDLK LLRSHLQELR ASIISRCGPM
     TQLSERLLAA LPSWRKLSGP NQLTSWQQFV SDVQEQINPL VSQDHLRTLA MQLHSMGEIN
     IMQSETVQDV VVLEPRWLCT SVLGKLLSVE TPKAIHHYRG RYRLEEVQAL APESDVEELL
     QILDAMDVCA RDITNPSMVD VPALIKTNGL HRSWTEDEDE DALIYGGVRL VPAEHLTPFP
     CGLFHKLQVN LCRWSHQQKP EEDGADDSDG DIHLWTNGAK VSQAGVEAMI LLVNHGQGVE
     IQVRGHESQR AKCYALLDTV CSITENLLAS TLPGLLTARY YLSPQQLREH HAPIMVYQPK
     DFCRAQIQRE TSLTNTMGGY RESFSSILAF GCAEVYQHGV LGTDIHIADV PLLARRKLCR
     MLDPPDALGK DWCLLAMNLG LTDLVAKHSG GGATPDADAQ PPPPSPTAAL LREWSGRAGS
     KVGVLMIKLR ELGRRDAADF LLKASPVFRV NMEALSGAPN GYPPTCNGGT SYNSISSVIS
     R
//
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