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Database: UniProt
Entry: A0A1U7R627_ALLSI
LinkDB: A0A1U7R627_ALLSI
Original site: A0A1U7R627_ALLSI 
ID   A0A1U7R627_ALLSI        Unreviewed;       646 AA.
AC   A0A1U7R627;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=MAP3K3 {ECO:0000313|RefSeq:XP_006017895.1};
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_006017895.1};
RN   [1] {ECO:0000313|RefSeq:XP_006017895.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   RefSeq; XP_006017895.1; XM_006017833.3.
DR   AlphaFoldDB; A0A1U7R627; -.
DR   GeneID; 102374958; -.
DR   CTD; 4215; -.
DR   OrthoDB; 145974at2759; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06405; PB1_Mekk2_3; 1.
DR   CDD; cd06625; STKc_MEKK3_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR034879; PB1_MEKK2/3.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR   PANTHER; PTHR48016:SF50; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 3; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51745; PB1; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_006017895.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
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:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          64..143
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   DOMAIN          382..642
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          9..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         411
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   646 AA;  72951 MW;  EBA8E91F772DD230 CRC64;
     MKDLVALQMG RRHRLPGLET MKNKDTTHSS KQKKHNASNP ALLSSPAITN QCASAVEEKK
     IPNDVRIKFE YNGERRIIPF VRPVRYEDVQ QKVKTAFGQP LDLHYMNNEL SIPLKNQDDL
     DKAIDLLDRS SNVKSLRILL LSQDRNHISP SPHSGLPKQV RIKTSQSVGD VNTTYQPPEP
     RSRHLSVSSQ NTGRSSPPPG YVPERQQRIA RQGSYTSINS EGEFIPETNE QCMLDPLSSA
     ENSISGSCQS LDRSADSPSF RKSRMSRAQS FPDNRQEFSD RENQIYDKAG KGGTYPRRYN
     VSMQHKDYND GRRTFPRIRR HQGNLFTLVP SSRSLSTNGE NLGLAVQYLD PRGRLRSADS
     ENALSVQERN IPTKSPSAPI NWRRGKLLGQ GAFGRVYLCY DVDTGRELAA KQVQFDPDSP
     ETSKEVSALE CEIQLLKNLQ HERIVQYYGC LRDRAEKTLT IFMEYMPGGS VKDQLKAYGA
     LTENVTRKYT RQILEGVSYL HSNMIVHRDI KGANILRDSA GNVKLGDFGA SKRLQTICMS
     GTGIRSVTGT PYWMSPEVIS GEGYGRKADV WSLGCTVVEM LTEKPPWAEY EAMAAIFKIA
     TQPTNPQLPS HISEHCRDFL KRIFVDARHR PSAEELLRHH FAQLLY
//
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