ID   SPK1_CAEBR              Reviewed;        1132 AA.
AC   Q61IS6; A8XAC9;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Serine/threonine-protein kinase spk-1;
DE            EC=2.7.11.1;
GN   Name=spk-1; ORFNames=CBG10087;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Required for embryogenesis and germline development in both
CC       adult hermaphrodites and males. SR-protein kinase (SRPK) that binds
CC       directly to and phosphorylates RS domains (By similarity).
CC       {ECO:0000250}.
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:0000250|UniProtKB:Q03563};
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:0000250|UniProtKB:Q03563};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; HE601459; CAP29597.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q61IS6; -.
DR   SMR; Q61IS6; -.
DR   STRING; 6238.CBG10087; -.
DR   WormBase; CBG10087a; CBP42578; WBGene00031566; Cbr-spk-1.
DR   eggNOG; KOG1290; Eukaryota.
DR   HOGENOM; CLU_000288_81_0_1; -.
DR   InParanoid; Q61IS6; -.
DR   OMA; AWDTQEK; -.
DR   OrthoDB; 290680at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1132
FT                   /note="Serine/threonine-protein kinase spk-1"
FT                   /id="PRO_0000086671"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          495..1044
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          240..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1066..1121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..436
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        628
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         501..509
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         524
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1132 AA;  126200 MW;  B137D4FAEED24704 CRC64;
     MLSILHSLSW MAHWINPTAT IAPSTPPQAG EKNANVKNGT VQTNGVNHTE RLAGRAPNLL
     HPAIDYPGIT SYEAGGSLIL TDIFPTVLFM FVVLFCRWFN GFAPRQERFQ RLEYEAILRR
     RRFRVQSEES EELEDHEAYS ETDICTQLIA SSANVACNIN VDLVNQNRFY FFVKQNNEDE
     TAVPSDVPPP ETSIKNEDTE VNLVFASAED NGYISSTFEV SETSLMVTSE VYEVEKVSVN
     EDQSSRPVNV IVNESDDEQS LRSQDGSRCS DEAMNSCMSA SEDEDVESQE DSYHVNDATE
     DSVSSIKTQE DEPIEEELAS CHSDEDDHQN EVLGDEEASK YDNLPVEMRS AKEGDESEGT
     IDSSVSSSTS STPDDDEDDS ATSYDSDDIE IQMFEYDLGT VCASASISIP RPSIIPKKNK
     KAEVNANEER MDDVSVSPGR SDSPGGGGGH SDSFQDPLDP GEQLGSDDEE QEDPRDYKRG
     GYHPVNIGDV FNSRYHVIRK LGWGHFSTVW LAWDTQEKRF TAMKIVKSAE HYTEAALDEI
     KLLLSVRGAD PEDTGCHKVV QLLDEFTVTG INGQHVAMVF EVLGCNLLKL IIRSNYRGLH
     LEQVRKICKQ ILEALRYMHE KCGIIHTDIK PENVLITMSR EEIKIMAQHA VVARKMNMKM
     SGSAVSTAPD HLVKMAQENM TKNKKKKMKK KAKKQREKLE AELAGLEGLK MDANGLQEAY
     NNAPQNGIRM RPPSLLFNGP IPQLLQGSSC VNTPSSPRSV PPPPALYPQA GGVCNQTYHL
     SQVILNEQVE LESFNTSQVE DVNIEDAVNG NGNGTNNKIE LKSPDRFDRT TLTPFSDPES
     KIGELASPSS EFLSSPMSML PPGGVLPAPP VGPNIADPYC DIDVKIADLG NACWVNHHYT
     DDIQTRQYRA LEVLIGSGYG PPADIWSTAC MAFELATGDY LFEPHQGDNY SRDEDHLAHI
     SELLGQISPS IYKKGKHWRE FFHKNGNLLH IHNLKPWSLY EVLRQKYEWS HEDAQQFESF
     LRPMLDFDQE KRATANDALK HPFLLPFGGK APRDPEVLQR LYPDGQVPEA LDGNQEVYRD
     ENDSNSASER SANRSAGSDD EEEFHMDRPG PSGVINEPAD VSEIESFQLN LQ