GenomeNet

Database: UniProt
Entry: A0A1S3JQ27_LINUN
LinkDB: A0A1S3JQ27_LINUN
Original site: A0A1S3JQ27_LINUN 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system