ID A0A3Q0HJS1_ALLSI Unreviewed; 1343 AA.
AC A0A3Q0HJS1;
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=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LOC102368069 {ECO:0000313|RefSeq:XP_025070708.1};
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_025070708.1};
RN [1] {ECO:0000313|RefSeq:XP_025070708.1}
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=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR RefSeq; XP_025070708.1; XM_025214923.1.
DR KEGG; asn:102368069; -.
DR InParanoid; A0A3Q0HJS1; -.
DR OrthoDB; 988261at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00132; CRIB; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF22; SERINE_THREONINE-PROTEIN KINASE MRCK GAMMA; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_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:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_025070708.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..276
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 277..347
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 788..907
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 930..1200
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1270..1283
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 291..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 541..568
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 666..693
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 383..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1343 AA; 145057 MW; C901341785A854B8 CRC64;
MSEGVPIYLC SIKGITASGP LLYTSGLPLP SLSWCSPLTD PCLLGPSIPA TPFVEQVKEL
QLSRDDFEIL KVIGRGAYGE VAVVRLRGSD RVYAMKILHK WEMLKRAEAR ARFYLAEMVL
AIDSLHRLGY VHRDIKPDNV LLDAQGHVRL ADFGSCLRLG PDGMVGSAMA AGTPDYISPE
ALRVVEGGRG RYGPACDWWA LGVCAYELLF GETPFYAESL VETYGRIMAH EEHLHFPAEV
TDVSEEAKAL IRGLLCREEL RLGRGGLGDF QEHPFFRGVA WARLRDSPAP YVPPVAGPGD
TSNFDVDDDT LKEPESPPPS SQGTFPWHRL PFVGFTFMSG SSLARQGPSP PPGSSSSKDP
KRAPLPGTDR AELCLADVLS RSPTKDAETR SPKRDVDKVS QQLVETHEEG ETSGQLRALE
KQLEATRKER DEALKAQHGP PGAPPEPLHA RATVSHEGPA CEGMSQDDTA GTESKGFWVM
AQGRAGAASQ SHQGGPDWSL VGGAGPSEGP APTPCFGVPS TSEGPERGRG AAEQGDGAAE
TQQLRAQLEA LSAAKGRLEQ ELQVLQAQGE AQINDLLQWV SEEKESRGYL QATATRLAQE
LESLKQVGTP ASVRDPGVRA PPGAGGSAGV PAPSAAHPTP PGPTPLPAPG RTQASGLRPG
VSPRQLQELE AQNQALGQEL EKLKAELRAR TLEGTKHLIR SRSTENDTIS HGSSLEAPES
PRAQEDAQLR PEGRRSLRAQ TRPHSLHFCG VPLACGLICH VGCAGGALRC PPPPESPRQG
LGAGAGTGTA LEGVLSVPRP AGVRKGWQRV FAIVSDFRLF LFEAPEGRSS PGGVGATHVI
DLRAEQFSAE LVQASDVIHA NPKDLPCIFR VTALQLWVPR TCCSLLLLAE SAGEARRWVQ
ALGALPRALP PQLRPVLALK EAYDSGLPLL PHALATAILD RERIALGTED GLFVLHLRTN
DVVQVGDCRR VQGLLACPQA QVLAVLCGRH HSVRLFSWAE LGQPAAPGAK MTEVRGCQAL
AAGVLCRGTT PVLCLASKRQ VLCVQLVPGT PPYRRGRELQ APGYVQCLDV LGDRLCVGFP
GGFALYPLLN EGAPQPLPQP EEPRSRGLGQ QEALRAVEVS LGELILCFGG LGVYVDGRGR
RTRDQDLMWP APPLSCCYSA PYLTVFSENA LDVFDVRKAE WVQTVPLRKV RALNPEGSLL
LFGTEKTRLV YLRNQAADQD EIKIPEITDL SRRQLVRTSK RRFSFRISNE ERQQQRKEMM
RDPDARARLI SSPTNFSHVV HVGPGDGRHR LQDLPTAQAE KQQEAQLRPR SFSDPRQPLA
SRRISDQTSL PRSVSSSQGS SIS
//
