ID A0A1S3JW34_LINUN Unreviewed; 1788 AA.
AC A0A1S3JW34;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=LOC106176436 {ECO:0000313|RefSeq:XP_013414271.1,
GN ECO:0000313|RefSeq:XP_013414272.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013414271.1};
RN [1] {ECO:0000313|RefSeq:XP_013414271.1, ECO:0000313|RefSeq:XP_013414272.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013414271.1,
RC ECO:0000313|RefSeq:XP_013414272.1};
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 -!- 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 RefSeq; XP_013414271.1; XM_013558817.2.
DR RefSeq; XP_013414272.1; XM_013558818.2.
DR EnsemblMetazoa; XM_013558817.2; XP_013414271.1; LOC106176436.
DR EnsemblMetazoa; XM_013558818.2; XP_013414272.1; LOC106176436.
DR GeneID; 106176436; -.
DR OrthoDB; 988261at2759; -.
DR Proteomes; UP000085678; Unplaced.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20809; C1_MRCK; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR CDD; cd05597; STKc_DMPK_like; 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:SF66; SERINE_THREONINE-PROTEIN KINASE GENGHIS KHAN; 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; PF00786; PBD; 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; 2.
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 PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 2.
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, ECO:0000313|RefSeq:XP_013414271.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000085678};
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 345..415
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1057..1107
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1127..1246
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1272..1545
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1607..1620
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 1640..1653
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 623..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 887..942
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 974..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1788
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 1788 AA; 203176 MW; 98311A5C2E46865A CRC64;
MTAIDRIKKL ETLYLGGVGN SDMLALSMET LLDVLVVLYD ECCGSTLRRE KSVSEFVEFA
KPVVARIKQL RLQRDDFEIL KVIGRGAFGE VAVVKLKNTD TVYAMKILNK WEMLKRAETA
CFKEERDVLV KGDRRWITNL HYAFQDDDYL YLVMDYYCGG DLLTLLSKFE DRLPEDMAKF
YIAEMVLAID SLHRLRYVHR DIKPDNVLLD RSGHIVLADF GSCLRLMNDG TVQSNVAVGT
PDYISPEILR AMEDGHGRYG AECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKNR
FEFPADINDV SEEAKDLMRR LICSQDQRLG QNGIEDFINH PWFEGRIDWE NIRQSEPPYI
PDVSSPTDTS NFDVEDTDFK QSESVPPTSH SVFTGHHLPF VGFTFTSNSR MSDLEALADG
FSQETSEEKT SSVSTQAYER RIQRLEQENK ELDRKLKDAT RVIQSQFGNE APGSPSQSAD
RELQHLRTEV VRLQAQVKET QRDLDETLAI KQELETMEGD KNTKLKALEK SSKNLSQEKS
ELQQELESLQ ERYRTQTKEL KDAIGQRKLA IEELTNITER LEDTRSGKQK LQRQLRDKEE
ELEDSRLKLD NLKQDLRKAE KAKRDLQTQL DESTAEASKQ SKLRERSESY AKELEQEIET
MKQKSLGRTP STSNLETTQE INRLKAELEK KEVQYEEMIA RLKQKHSTAI QDLHYQIQDI
DNKKTEKERE VQTLKEKIDL TKKENISNYQ ENINDIKRKN EREKTLLEQE NLRLTKEVEK
LSRDVQKNQN DKRQIEEELR DLSEKRDSVA HWEAQISEII QWVSDEKDAR GYLQALASKM
TDELEGLKMQ GVGVTGERSW TKRRSQRVDK MELLSLQSQL QSEIQAKQSI SEDLTQTKAK
SVELEKQVLE AQAMCREWEY EVNQLRAENK ELKARLEGEE LKESLNFKDF TVVGDHDRPS
SQVSFRTFLE QQTRRLGSST SDVSEDDIDN YSIGSRGSRG SRNSDLSRPV NRDRVSLQDS
SDKDEKQPAT INNAHPVDEP KRTLPIQVIK PSNQPRSHRF AVRTFSTPVK CNHCTSLMVG
LQRQGTVCEV CHYACHVLCT ERAPQVCPVP PDQTKRPLGI DPAKGIGTAY EGYVRIPKPG
GIKKGWMRQF VVVCDFKLFL YDINPEKTSQ ASVQVNQVLD MRDEEFSVSS VLQSDVIHAN
RRDITCIFRV TTSQLHPPGS KHAVLMLAEN ESDKQRWVGA LNELHKILRK NKIPDKSVFQ
AKEVYDSSLS LLRNTLSGAI LDHDTLLLGT EEGLHCIDLT RDEISRIGDK KSVFQIEVVQ
RDQLVIVISG KQRHIRLIPM AAVESAESVE SVKINETRGC TTICTGLISQ GSVNCLCVAI
KRTVVIYELT RTKQRHKRVR EILVPGNVQY IEMMNERLCV GYPSSFAIYT IQGEGAPVCL
VNSEDTTLQF LLSSPVDAYL AVELSHKEYL LVFATLAIYV DNTGKRSRLQ EIMIPAQPHS
FSYNAPYLTC YAEEAAFVFD TRSEEWIQTI CLKKLRPLCR DGAIGLPLVS DTPRLVYIHQ
KSEEEDRIAI PDMLNGKGRS LNRSKRRFSF KEEKLTKQVP DRRSRMISAP INFAHVAHVG
KEETVTMIHR SASDRRSKLI SAPTNFSHIA HMGPDQGMKM LIDLPTSSGQ GLDDAQVQRV
KSMFQPNFGA NVLAMQEAAH VRGSGGSGSS GSGSGSRPNS MQPQYNGSAV RHESPSGSSQ
GSPYLASSSV ASASPDSSSL SSQEQFGGNS ANQMPSPIQE MRIYSTPV
//
