ID A0A1S3JNX0_LINUN Unreviewed; 1183 AA.
AC A0A1S3JNX0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=LOC106174871 {ECO:0000313|RefSeq:XP_013412060.1};
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_013412060.1};
RN [1] {ECO:0000313|RefSeq:XP_013412060.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013412060.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR RefSeq; XP_013412060.1; XM_013556606.1.
DR AlphaFoldDB; A0A1S3JNX0; -.
DR EnsemblMetazoa; XM_013556606.1; XP_013412060.1; LOC106174871.
DR GeneID; 106174871; -.
DR OrthoDB; 4221785at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR CDD; cd20813; C1_ROCK; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR CDD; cd22250; ROCK_SBD; 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; 1.20.5.730; Single helix bin; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF73; RHO-ASSOCIATED PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR SMART; SM00109; C1; 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; SSF103652; G protein-binding domain; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 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; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01206}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_013412060.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 1..135
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 139..207
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 753..821
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 927..1128
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1039..1094
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 409..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 507..811
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 836..909
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1137..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1183 AA; 136791 MW; 56E0518469A84B8A CRC64;
MLLDAQGHLK LADFGTCMRM DKDGMVRSDT AVGTPDYISP EVLKSQGGDG YYGRECDWWS
VGVFLYEMLV GDTPFYADSL VGTYGKIMDH KNSLSFPEDI EISRDAKSLI RAFLTDRSER
LGQRGVEEIK GHPFFTRNDQ WTWDSIRKTV PPVVPELSCD VDTSNFDDIE PDETAQETFP
VPKAFAGNHL PFIGFTYNRA YHLLSEAKAS LDQTAAVPSQ MSNDVAKKLR QLEDQYRAER
SSKDELERKY RAAIQDLDRL TSDETALRRQ CNDFERNMAL IKHDLKETQR KLEIESDNRR
KTESKLVETE RQLQAETGAR RQAMGNSQHV NERVTQLERQ LTELNEKLKT EQETSSKLRK
TCTDMQQKCN SLESGYNDLQ SKYNEIQSVK SSLEKEIFHL QSIIEQERSA RTQASEQSSE
VESRNRNLHS EVQRFKEKEA QMLKDKQKLS QDVINLEKSR ANVELELKTY RMKYDQEVLA
HKETIAKFNA DKKHILTSTE EASNEAIKEI QLSLEQEKSA RLKAEAKLLD TEKRKSELTY
DMGQVRQHLE TLQRELRTEV DKAKTLALQV EQETQKRILV SNDIKQQQQL VAQLRQNEKQ
YEKEITGLKQ DKRSMEEEMR KVKDEAHVND LQMKEIQDQL EAEQYFSTLY KTQVRELKEE
IEEKIRQYQD LETQIQLLDK ERAALDAQLE LAMAKANSEE IARKLAEDQL SDVEKQKTML
ELEIKELMTR HKADMSKKES TIGVLEESKN QNSRNIDILS KEKDELNKQI KKLMEDVQNM
QSDTSSTDTE LAQLKKQYEE EKIKKIQAVN KLAEIMNRKE FAGGGKKDKK VSATDLRKKE
KECRKLQQDL NKEKEKFNEM VAKFQKDITE LQAALYEEGQ QRQRLQMELD AKDSEIEQLQ
RNLTLMNSDT ASVSSGNELD MEDGFPESRL EGWLYLPNRQ NIKRYGWKKQ YVVVSTKKIL
FYNSENDKMN ADPELVLDID KLFHVRPVTQ GDVIRADPKE IPKIFQILYA SEGENKKPLE
GLHEMPKPDD KSGVIHYKGH DFIVLHYRTP TTCDSCQKPT WHMIHPPPAM ECKRCRCKVH
KDHFDKGEEF IGPCKVNDGM QSAKDLLLLA ATQDEQKLWV QRIKKKIDKK GIGHHPGQSS
QPRNAKQYSS FSSNAKLVQS PGSHGGTPVQ RAATLPPNTL RPK
//
