ID A0A3B4AL08_9GOBI Unreviewed; 1696 AA.
AC A0A3B4AL08;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000017823.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000017823.1}
RP IDENTIFICATION.
RG Ensembl;
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=2.7.11.1;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}.
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 STRING; 409849.ENSPMGP00000017823; -.
DR Ensembl; ENSPMGT00000019019.1; ENSPMGP00000017823.1; ENSPMGG00000014581.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
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:SF31; SERINE/THREONINE-PROTEIN KINASE MRCK ALPHA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 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; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 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.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 77..343
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 344..414
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 975..1025
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1045..1165
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1191..1463
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1535..1548
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 629..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 705..824
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 890..945
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1574..1637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1660..1690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1696 AA; 192544 MW; D665E96AB67801D8 CRC64;
MSGEVRLKKL EKLILDGPVQ SIGQCLSVET LLDILVCLYD ECNNSPLRRE KNIIEFLDWA
KPFTSKVKQM RLHKEDFEIL KVIGRGAFGE VAVVKVKHTD KVFAMKILNK WEMLKRAETA
CFREERDVLV NGDCQWITTL HYAFQDDNNL YLVMDYYVGG DLLTLLSKFE DRLPEEMAKF
YLAEMVLAID SVHQLHYVHR DIKPDNILLD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT
PDYISPEILQ AMEDGKGKYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
FQFPQQVTDV SEDAKDLIKR LICSREHRLG QNGIEDFKQH PFFSGIDWDN ILTCEAPYIP
EVSSPTDTSN FDVDDDCLKN SETMPPPSHT AFSGHHLPFV GFTYTSKCIL SDRGCLRQLS
GEPGKAGHEK VDLEVQRGLE DSLAVEAYER RIRRLEQEKL ELSRKLQEST QTVQALQHPS
GDSPINLNKE VEIRSLKSEI DILKKQIADS GQLEKQLEDV TLARRDLEDS SKHIKTLEKQ
MRSMTQERDD LHKDLIDANE KLKVQSKELK EAHTQRKVAL KEFSELNEKL TDLRSAKQRL
SRQLRDKEEE IESQTQKVEA LRLEVRKAER SKKEMESQAE EQGAEAQKER KLRERNEQYS
RQLEEELEAL KLKQPGPAAT SPSADQSQEV GRLRGDLEKK TLHFEEELSR REAQHSSELK
ALKKELRDAE SQHLALQKEI LVLKDKLDKT RRESQCEREE FETEYKQKYE RERVLLMDEN
KKLSSELDKL TSMFEKLNSS NRQLEDEMRE LADKKESVAH WEAQITEIIQ WVSDEKDARG
YLQALATKMT EELEGLRNTS LGARATDMPW KMRRFAKLDM SARLELQSAL DAEIRAKQSI
QDELNKSKAN NISTECKLQE VEVKNQELLA EIDRLKKETE ELRLRRGVKH QDSQNSFLAF
LNAPTSALDQ FDPKAHQFVV KTFNTPTKCN QCTSLMVGLI RQGCTCEVCN FSCHVTCADK
APAVCPVPQD QTKGPLGIDP QRGIGTAYEG TVRVPKPTGV KKGWQRAMAV VCDFKLFLYE
LGEGKATQPS VVVSQVIDMR DEEFSVSSVL ASDVIHASRK DIPCIFRVTA SQLSPSSSNK
TSILILADSD QERNKWVGLL NELHRILKKN KLKERFVYVP KEAYDSTLPL IKTTQSATII
DHERVALGNE EGLFVVHVTK DEIIRVGDNK KVHHIDLMAQ EQLLAVISGR NRHVRLFPTQ
ALDGRETDSF KLAETKGCTS VVSGPVRNGA LTCLCVAMKR QIICYEVHTS KMRHRRLREL
QAPGQVQWMG LLSERLYVGY QSGFTRYSVH GDVSPVSLLH PEDHTLSFIP QQSLDALCAV
EISGKELLLC FSAIGVYVDS QGRRSRQQEL MWPAVPNAAC YNAPYLSVYS ENAVDVFDVN
TMEWIQTIPL KKVRPLNVDG SLNLLGLETV RLIYFRNKMA EGDELVVPET SDNSRKQMVR
SMNNKRRYSF RVPEEERLQQ RREMLRDPEM RNKLISNPTN FNHVAHMGPG DGIQILKDLP
MNVRVQENRA GFSGSVSIPS ITKNRGEPGR SMSASSGLGI RSSSQNGSAL RRELSGGSYG
SKRQTMTSPS ESSLSSGGGM DCGDAPLSQF DREDSDSPRH STASNSSTFS SPPSPASPHK
TKSLSLESTD RMGWDT
//