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Database: UniProt
Entry: A0A3P8RHA8_ASTCA
LinkDB: A0A3P8RHA8_ASTCA
Original site: A0A3P8RHA8_ASTCA 
ID   A0A3P8RHA8_ASTCA        Unreviewed;      1370 AA.
AC   A0A3P8RHA8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE            EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000040482.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000040482.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000040482.1}
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=2.7.11.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00000478};
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=2.7.11.25; Evidence={ECO:0000256|ARBA:ARBA00000106};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00006529}.
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DR   STRING; 8154.ENSACLP00000040482; -.
DR   Ensembl; ENSACLT00000041434.1; ENSACLP00000040482.1; ENSACLG00000027238.1.
DR   GeneTree; ENSGT00940000159155; -.
DR   OMA; ICLAHSK; -.
DR   OrthoDB; 5388799at2759; -.
DR   Proteomes; UP000265100; Chromosome 15.
DR   Bgee; ENSACLG00000027238; Expressed in liver and 7 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06624; STKc_ASK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR046872; DRHyd-ASK.
DR   InterPro; IPR046873; HisK-N-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR043969; MAP3K_PH.
DR   InterPro; IPR025136; MAP3K_TRAF-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR11584:SF332; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 5; 1.
DR   PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF19039; ASK_PH; 1.
DR   Pfam; PF20309; DRHyd-ASK; 1.
DR   Pfam; PF20302; HisK-N-like; 1.
DR   Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          674..932
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1175..1237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1279..1310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1211..1234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         703
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1370 AA;  153805 MW;  99AF48AEAF4EA382 CRC64;
     MNQDQDGISL AVPSFGAGPG RENLSGENTS VNSSGGGGAC GIPAAGTFWH DSGAGGGGLS
     PISGSCPLDT GGLLSTGKSC KSRPVTVAYV VNGEASQQNN HESMALQCLK DACESVGSKL
     ETVNFGKLDF GETAVLDRFY NADIAVVEMT DAFRQPSLFY HLGVRESFSM ANNIILYCDT
     NSDALQSLQE IICQKNTTCS ANYTFIPYMV TPQNKVYCCE GSLMKGLTEL MQPSFEMLLG
     PICMPLLDRF IQLLKVSQAN SHQYFRETIL NEIRRARELY TGLELAAELS RIQQRLDNVE
     CLSVDVVINL LLTYRDIQDY ESIVKLVETL EKLPTFDPMA HPHVKFHYAF ALNRRNLPGD
     RQKALDIMLP LVEGEEQVAS DMYCLVGRIY KDTFLESDFT NTQSRDNGAL WFKKGFESEP
     TLHSGINYAV LLLAAGHQFD TSFELRKVGV KLSSLLGKKG SLDKLQSYWD VGFFLGASIL
     ASDSTLVIQA SEKLFKLKAP IWYLRSLVET ILIFQHFNKP SVEQPSYKQE LVDFWMDFLV
     EATKKDVSSV RFPVLILEPT KVYQPSYLSI NKDVDDNTVS IWHVAPDDKN KGIHEWNFSA
     TSVRGVSISK FDERSAFLYV LHNAEDFQIY FCTEMHCKRF CDLVNSITEE AWKCPEEGEC
     DTDTLEYDYE YDEHGERVVL GKGTFGVVYA GRDLSNQVRL AIKEIPERDS RYSQPLHEEI
     ALHKHLKHKN IVQYLGSISE NGFIKIFMEQ VPGGSLSALL RSKWGPLKNN EPTIGFYTRQ
     ILEGLKYLHD NQIAHRDIKG DNVLINTYSG VLKISDFGTS KRLAGINPCT ETFTGTLQYM
     APEIIDKGPR GYGKPADIWS LGCTIIEMAT GKPPFYELGE PQAAMFKVGM FKIHPEIPES
     MSPEAKAFIL RCFEPDPDRR ATALDLLTDE FLTVTSRKKK SKGSFTALTP GSEYLRSISL
     PVPVVVEDTS SSSEYGSVSP DNDLNTNPFI FKPSIKCYSE KDVKGQRSLF LSIPVENFED
     HSAPPSPDEK DSGFFMLRKD SERRATLHRI LTEDQAKVVA NLMEALAQGS EEMKLKHQHI
     STLVVSLADF VRMADRKIIA NTLSQLKLEL DFDSTAISQL QIMLFGFQDA VNKVLRNHNI
     KPHWMFALDN IIRKAVQTAI TILVPELRPH FSLASESDAA DQEDIDDDGE PDRTSTHQSR
     APPGAAHDDT VATSGVSTLS STVSHESHNA QRSVSMELGR MKLETSRLLE QLLEKEREYQ
     SILQQVLDER EQEIRLLKLR TEPEDTPTSS HDLEGQRSQP AERRDDPELT SWLTRYGADQ
     DAIDRILNEE YTLYDILHDV TRDDLKSLRL RGGVLCKLWK AITDYRQKLF
//
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