ID A0A1S3JY35_LINUN Unreviewed; 1061 AA.
AC A0A1S3JY35;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LOC106177175 {ECO:0000313|RefSeq:XP_013415325.1};
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_013415325.1};
RN [1] {ECO:0000313|RefSeq:XP_013415325.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013415325.1};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR RefSeq; XP_013415325.1; XM_013559871.1.
DR AlphaFoldDB; A0A1S3JY35; -.
DR EnsemblMetazoa; XM_013559871.1; XP_013415325.1; LOC106177175.
DR GeneID; 106177175; -.
DR OrthoDB; 2904475at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06608; STKc_myosinIII_N_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_013415325.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777,
KW ECO:0000313|RefSeq:XP_013415325.1}.
FT DOMAIN 1..237
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 739..1035
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 257..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 120127 MW; 0F49CB2AE53A084E CRC64;
MSVTPDEEEE IKLEINVLKK YSHHRNIATY YGAFIKKMPP GKDDQHDQLW LVMEYCGAGS
ITDLVKATKG GALKEEWIAY VCREILRGLS HLHANKVIHR DIKGQNVLLT DNAEVKLVDF
GVSAQLDKTI GRRNTFIGTP YWMAPEVIAC DENPDATYDN RSDLWSLGIT AIEMAEGKPP
LCDMHPMRAL FLILKNQPPR LKSKKWSKRF QNFIEVTLYK DYTQRPNTEQ LLKHAFIRDQ
PTERQVRIQL KDHIDRAKKN RKTTDHDTDY EMYEEEEDEE ENALAGEPSS IIQIGPREST
LKRNFQRIQE NEGRLTPSPY AVPQRQQQQQ QFFPNPQLQQ QQMLRQQQQQ QQQQQQQQRA
HQIQQAQFAQ RPQIQRPNQP QMGVMHQQQQ QPSSSHHQGQ HQSQPPQQAK QFPVQSRVIV
VPTPQQQQQT PQQQQQGAHA DLSRQASAQQ RARPEVKHVQ SEPSLKLSKS QEDLDRLAAQ
LKGIAAGNER VTSDIPEVVD DDSDEEPEVI GVSSRAGGDG TLLASEPARP LPAGGYNRDT
LETLESMIIH DDVPSTQSSP EKQPSSSKNQ DREGDDGTLV VRRNQSDTRL VEERQRQHQQ
RAASKQHNDV KRTESNQSNQ SSPGNLGTPE QARANSSNVL PDLLPQQPGN TRERGGSAPQ
RPQDKTVSEE DDEDINVKIT FKAKGRSFTA FGFGAGSSSQ TSTLTPPRRG SSVNVNVTPT
TVDITSDTPE IRKYKKRFSS DILCAALWGV NLLIGTENGL MLLDRSGQGK VYQLISRRRF
SQMEVLEGQN ILVTISGKKN RLRVYYLSWL KTKILKSDGV SSLQTEKRNG WTNVGELDGA
VHFKIVKYER IKFLVIALQH SVEIYAWAPK PYHKFMAFKS FGDLADKPVI VDLTVEEGQR
LKVIYGSHRG FHAIDLDTST VFDLYIPSMY NRGQNQAPLT PHTIVILPES NGMQLLLCYD
NEGVYVDANG KIAKNMVLQW GELPTSVAYI STGQIMGWGH KAIEIRAAET GHLDGVFMHK
KAQKLKFLCE RNDKVFFSSI RSGSTCQIYF MTLNKPGLTN W
//
