ID A0A9D3XUK3_9SAUR Unreviewed; 1320 AA.
AC A0A9D3XUK3;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 02-APR-2025, entry version 10.
DE RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN ORFNames=KIL84_018530 {ECO:0000313|EMBL:KAH1185781.1};
OS Mauremys mutica (yellowpond turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Geoemydidae; Geoemydinae; Mauremys.
OX NCBI_TaxID=74926 {ECO:0000313|EMBL:KAH1185781.1, ECO:0000313|Proteomes:UP000827986};
RN [1] {ECO:0000313|EMBL:KAH1185781.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MM-2020 {ECO:0000313|EMBL:KAH1185781.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAH1185781.1};
RA Gong S., Gao Y.;
RT "The genome of Mauremys mutica provides insights into the evolution of
RT semi-aquatic lifestyle.";
RL Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048329};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00047559};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAH1185781.1}.
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DR EMBL; JAHDVG010000463; KAH1185781.1; -; Genomic_DNA.
DR OrthoDB; 275301at2759; -.
DR Proteomes; UP000827986; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033554; P:cellular response to stress; IEA:TreeGrafter.
DR CDD; cd06624; STKc_ASK; 1.
DR FunFam; 1.10.510.10:FF:000054; Mitogen-activated protein kinase kinase kinase 5; 1.
DR FunFam; 3.30.200.20:FF:000067; Mitogen-activated protein kinase kinase kinase 5; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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:SF363; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 15; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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}; Reference proteome {ECO:0000313|Proteomes:UP000827986};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 640..896
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1175..1209
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..43
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..943
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 669
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1320 AA; 148434 MW; 07E2630E01806869 CRC64;
MEGSGGAAAE QPHFLSGEAE QQPGAEAGAE AAGPGAEGSA PAPRQRSLRA VYVLNDSPKA
GAGARSPEAG ALQCLVRACE AQGAQLATVN FGELDFGETA VLDAFYDADV AVVDMSDVSR
QPSLFYHLGV RESFDMANNV ILYHDTDADT ALSLKDMVSQ KNTASSGNYY FIPYIVTPGA
DYFCCESDAL RRASEYMQPS WDNILGPLCV PLMDRFICLL KDIHVTSCAY CKETLLNDIR
KARDKYQGDE LAKELARIKL RMDNTEVLTS DIVINLLLSY RDIQDYNAMV KLVETLEMLP
TCDLADQHNI KFHYAFALNR RNNTGDRGKA LQVMLQVLQT CDHPAPDMFC LCGRIYKDIF
LDSDCKDTSS RDIAIEWYRK GFELQSSLYS GINLAILLIV AGQQFETSME LRKIGVRLNS
LLGRKGSLEK MNNYWDVGQF FSVSMLASDI GKAVQAAEKL FKLKPPVWYL RSLVQNLLLI
QRFKKLIIEH SPRQERLNFW LDIIFEATKE TTNGLRFPVL VIEPTKVYQP AYVSINNEAE
ESTVSLWHVS PTEVKQIHEW NFTASSIRGI SISKFDERCC FLYVHDNSDD FQIYFSTEDQ
CSRFCGLVKE ILTDAVGSAL ELEGEIDGDT LEYEYDYDEN GDRVILGKGT YGIVYAGRDL
SNQVRIAIKE IPERDSRYSQ PLHEEIALHK YLKHRNIVQY LGSVSEDGYI KIFMEQVPGG
SLSALLRSKW GPMKEPTIKF YTKQILEGLK YLHENLIVHR DIKGDNVLVN TYSGVVKISD
FGTSKRLAGI NPCTETFTGT LQYMAPEIID KGPRGYGAPA DIWSLGCTII EMATGKPPFH
ELGEPQAAMF KVGMFKIHPE IPESLSAEAK AFILLCFEPD PNKRVTASDL LKDLFLKQVN
KGKKNRIAFK PLDYNRSTSL PLPVHGEQAG SSSSEHGSVS PDSDVQHELF FEKTKRSVSE
NPAKHPISHL SVPDENSALE DRSASPSLED RDSGLFLLRK DSERRAILYK ILKEEQNKVA
SNLQECLTQN SEELQLSVTH IKQIIGILRD FIRSPEHRVM ASTISKLKVD LDFDSTSINQ
IHLVLFGFQD AVNKVLRNHL IRPHWMFAMD NIIRRAVQAA VTILIPELQA HFEPASETEG
VEKDADEVED DCLPVEQNGN EEPVVTSGVS TLSSVVSHES QQQHLNLQLA KLKQETNRLL
EVLIQKEREY QTLLQQTLEQ KTQEFHLLQL QSKPAEFRRP PGAPVQNVDL ELLDWLRQQG
ADSGAIERFA EEDYTLNDVL NDITKDDLRY LRLCGGLLCR IWNAILNHRK MANKPSETNS
//
