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Database: UniProt
Entry: A0A3Q0FMP8_ALLSI
LinkDB: A0A3Q0FMP8_ALLSI
Original site: A0A3Q0FMP8_ALLSI 
ID   A0A3Q0FMP8_ALLSI        Unreviewed;       718 AA.
AC   A0A3Q0FMP8;
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=calcium/calmodulin-dependent protein kinase {ECO:0000256|ARBA:ARBA00012434};
DE            EC=2.7.11.17 {ECO:0000256|ARBA:ARBA00012434};
GN   Name=CAMK2B {ECO:0000313|RefSeq:XP_025047465.1};
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_025047465.1};
RN   [1] {ECO:0000313|RefSeq:XP_025047465.1}
RP   IDENTIFICATION.
RG   RefSeq;
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=2.7.11.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000902};
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=2.7.11.17; Evidence={ECO:0000256|ARBA:ARBA00000517};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. CaMK subfamily. {ECO:0000256|ARBA:ARBA00005354}.
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DR   RefSeq; XP_025047465.1; XM_025191680.1.
DR   AlphaFoldDB; A0A3Q0FMP8; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14086; STKc_CaMKII; 1.
DR   Gene3D; 3.10.450.50; -; 1.
DR   Gene3D; 6.10.140.620; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24347:SF403; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT BETA; 1.
DR   PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Kinase {ECO:0000313|RefSeq:XP_025047465.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   Transferase {ECO:0000313|RefSeq:XP_025047465.1}.
FT   DOMAIN          69..327
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..578
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   718 AA;  77948 MW;  3BFD94D4D7ED280B CRC64;
     MGTSRRLPQP CREVTPLHAS LSPPSSRADG FSLNPPSGFP VHKPGSGRTV PPQPAGPDAD
     GHWVPASRWW HVLKAGRGAF SVVRRCVKLC SGHEYAAKII NTKKLSARDH QKLEREARIC
     RLLKHSNIVR LHDSISEEGF HYLVFDLVTG GELFEDIVAR EYYSEADASH CIQQILEAVL
     HCHQMGVVHR DLKPENLLLA SKCKGAAVKL ADFGLAIEVQ GDQQAWFGFA GTPGYLSPEV
     LRKEAYGKPV DIWACGVILY ILLVGYPPFW DEDQHKLYQQ IKAGAYDFPS PEWDTVTPEA
     KNLINQMLTI NPAKRITAHE ALKHPWVCQR STVASMMHRQ ETVECLKKFN ARRKLKGAIL
     TTMLATRNFS VGRQTTAPAT MSAAASGATM GLVEQAKSLL NKKADGVKPQ TNSTKGSAGV
     TSPKGTLPPA ALEPQTTVIH NPVDGIKESS DSTNTTIEDE DTKAKGPNIE SPMELGPTTE
     VPSPPPPAPA VAAAAAAVST RFSDLLSTVK RSSGSPDTEG PQPATSQPCP TPAATNPLSP
     QSARFSDLLS TVKRGAGSPD AEGPPPAASQ PCLPPAATNP PALQSRKQEI IKITEQLIEA
     VNNGDFEAYA KICDPGLTSF EPEALGNLVE GMDFHRFYFE NLLSKNNKPI HTTILNPHVH
     VIGDDAACIA YIRLTQYIDG QGRPRTSQSE ETRVWHRRDG KWQNVHFHCS GAPVAPLQ
//
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