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Database: UniProt
Entry: A0A3Q0GB70_ALLSI
LinkDB: A0A3Q0GB70_ALLSI
Original site: A0A3Q0GB70_ALLSI 
ID   A0A3Q0GB70_ALLSI        Unreviewed;      1031 AA.
AC   A0A3Q0GB70;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE            EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN   Name=MAP3K15 {ECO:0000313|RefSeq:XP_025056911.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025056911.1};
RN   [1] {ECO:0000313|RefSeq:XP_025056911.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_025056911.1; XM_025201126.1.
DR   AlphaFoldDB; A0A3Q0GB70; -.
DR   Proteomes; UP000189705; Unplaced.
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: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; 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; 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|SAM:Coils};
KW   Kinase {ECO:0000313|RefSeq:XP_025056911.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|RefSeq:XP_025056911.1}.
FT   DOMAIN          350..606
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          634..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          900..931
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        634..650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         379
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1031 AA;  116971 MW;  FD0211EB90B4D921 CRC64;
     MLLCFWNEGA EKYTGGGVCC SGILFGVLFL RNNAGDREKA LQVMLQVFQT CDQPAPDMFC
     LCGRIYKDMF LDSDCKDTSS RDSAIEWYRK GFELQSSLYS GINLAVLLLV AGQRFETSME
     LRKIGVRLNS LLGRKGSLEK MNNYWDVGQF FSVSMLANDV GKAVQAAEKL FKLKPPVWYL
     RSLVQNLLLI QRFKKLTIEH SPRQERLNFW LDIIFEATEE TTNGLRFPVL VIEPTKVYQP
     AYVSINNEDD ERSLSLWHVS PTEVKQIHEW NFTASSIRGI SISKFDERCC FLYVHDNSDD
     FQIYFSTESQ CSRFCALVKE MLTDAVGSSL ELEGEIDGDT LEYEYDYDEN GDKVILGKGT
     YGVVYAGRDL SNQVRIAIKE IPEKDIRYSQ PLHEEIALHK YLKHRNIVQY LGSVSEDGYI
     KIFMEQVPGG SLSVLLRSKW GPMKEPTIKF YTKQILEGLK YLHENQIVHR DIKGDNVLVN
     TYSGVVKISD FGTSKRLAGI NPCTETFTGT LQYMAPEIID KGPRGYGAPA DIWSLGCTII
     EMSTGKPPFH ELGEPQAAMF KVGMFKIHPE IPESLSAEAR AFILLCFEPD PHKRVAASDL
     LKDPFLKQVT KGKKNRISFK PSDYNRSVSL PVQVPGEQAG SSSSEHGSVS PDSDVQHDMF
     FEKTKRSVSE IQTKHNISNL LSVPDESSVS EDRSGSSSLE DKDSGLFLLR KDSERRAILY
     KILKEEQNKV ASNLQECITQ SSEELQLSVP HIKQIIGILR DFIHSPEHRV MASTISKLKM
     DLDFDSTSIN QIHLVLFGFQ DAVNKVLRNH LIRPHWMFAM DNIIRRAVQA AVTILIPELR
     AHFEPASETE GVDKDGEEVE NNYQPAEQNG NEEPAVASGV NTISSVAYYD SKQRQLSLEL
     GKIKQETNRL LENLVQKERE YQSLLRQTLE QRTLELHLLQ LKSKPAEFQE PLSDVSQNVD
     PELINWLNEQ GVDSDAIKKF AEEDYTLNDV LNNIGKEDLR YLKLRGGLVC RIWNAILSHR
     QMGDKLTDTE D
//
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