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Database: UniProt
Entry: A0A3B4AL08_9GOBI
LinkDB: A0A3B4AL08_9GOBI
Original site: A0A3B4AL08_9GOBI 
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
//
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