ID A0A1S3JQ27_LINUN Unreviewed; 1185 AA.
AC A0A1S3JQ27;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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_013412059.1};
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_013412059.1};
RN [1] {ECO:0000313|RefSeq:XP_013412059.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013412059.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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_013412059.1; XM_013556605.1.
DR AlphaFoldDB; A0A1S3JQ27; -.
DR STRING; 7574.A0A1S3JQ27; -.
DR EnsemblMetazoa; XM_013556605.1; XP_013412059.1; LOC106174871.
DR GeneID; 106174871; -.
DR KEGG; lak:106174871; -.
DR InParanoid; A0A1S3JQ27; -.
DR OrthoDB; 4221785at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
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_013412059.1};
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 755..823
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 929..1130
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1041..1096
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 411..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 509..813
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 838..911
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1139..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1185 AA; 137006 MW; 4C43B67BA6F55CA7 CRC64;
MLLDAQGHLK LADFGTCMRM DKDGMVRSDT AVGTPDYISP EVLKSQGGDG YYGRECDWWS
VGVFLYEMLV GDTPFYADSL VGTYGKIMDH KNSLSFPEDI EISRDAKSLI RAFLTDRSER
LGQRGVEEIK GHPFFTRNDQ WTWDSIRKTV PPVVPELSCD VDTSNFDDIE PDETAQETFP
VPKAFAGNHL PFIGFTYNRA YHLLSEAKAS LDQVDTAAVP SQMSNDVAKK LRQLEDQYRA
ERSSKDELER KYRAAIQDLD RLTSDETALR RQCNDFERNM ALIKHDLKET QRKLEIESDN
RRKTESKLVE TERQLQAETG ARRQAMGNSQ HVNERVTQLE RQLTELNEKL KTEQETSSKL
RKTCTDMQQK CNSLESGYND LQSKYNEIQS VKSSLEKEIF HLQSIIEQER SARTQASEQS
SEVESRNRNL HSEVQRFKEK EAQMLKDKQK LSQDVINLEK SRANVELELK TYRMKYDQEV
LAHKETIAKF NADKKHILTS TEEASNEAIK EIQLSLEQEK SARLKAEAKL LDTEKRKSEL
TYDMGQVRQH LETLQRELRT EVDKAKTLAL QVEQETQKRI LVSNDIKQQQ QLVAQLRQNE
KQYEKEITGL KQDKRSMEEE MRKVKDEAHV NDLQMKEIQD QLEAEQYFST LYKTQVRELK
EEIEEKIRQY QDLETQIQLL DKERAALDAQ LELAMAKANS EEIARKLAED QLSDVEKQKT
MLELEIKELM TRHKADMSKK ESTIGVLEES KNQNSRNIDI LSKEKDELNK QIKKLMEDVQ
NMQSDTSSTD TELAQLKKQY EEEKIKKIQA VNKLAEIMNR KEFAGGGKKD KKVSATDLRK
KEKECRKLQQ DLNKEKEKFN EMVAKFQKDI TELQAALYEE GQQRQRLQME LDAKDSEIEQ
LQRNLTLMNS DTASVSSGNE LDMEDGFPES RLEGWLYLPN RQNIKRYGWK KQYVVVSTKK
ILFYNSENDK MNADPELVLD IDKLFHVRPV TQGDVIRADP KEIPKIFQIL YASEGENKKP
LEGLHEMPKP DDKSGVIHYK GHDFIVLHYR TPTTCDSCQK PTWHMIHPPP AMECKRCRCK
VHKDHFDKGE EFIGPCKVND GMQSAKDLLL LAATQDEQKL WVQRIKKKID KKGIGHHPGQ
SSQPRNAKQY SSFSSNAKLV QSPGSHGGTP VQRAATLPPN TLRPK
//