ID A0A095A0E1_SCHHA Unreviewed; 541 AA.
AC A0A095A0E1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=STK38L_1 {ECO:0000313|EMBL:KAH9585553.1};
GN ORFNames=MS3_00006767 {ECO:0000313|EMBL:KAH9585553.1}, MS3_09171
GN {ECO:0000313|EMBL:KGB40690.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB40690.1};
RN [1] {ECO:0000313|EMBL:KGB40690.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
RN [2] {ECO:0000313|EMBL:KAH9585553.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=31494670;
RA Stroehlein A.J., Korhonen P.K., Chong T.M., Lim Y.L., Chan K.G.,
RA Webster B., Rollinson D., Brindley P.J., Gasser R.B., Young N.D.;
RT "High-quality Schistosoma haematobium genome achieved by single-molecule
RT and long-range sequencing.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EMBL:KAH9585553.1}
RP NUCLEOTIDE SEQUENCE.
RA Stroehlein A.J.;
RT "Chromosome-level genome assembly for S. haematobium.";
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KAH9585553.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=35167626;
RA Stroehlein A.J., Korhonen P.K., Lee V.V., Ralph S.A., Mentink-Kane M.,
RA You H., McManus D.P., Tchuente L.T., Stothard J.R., Kaur P., Dudchenko O.,
RA Aiden E.L., Yang B., Yang H., Emery A.M., Webster B.L., Brindley P.J.,
RA Rollinson D., Chang B.C.H., Gasser R.B., Young N.D.;
RT "Chromosome-level genome of Schistosoma haematobium underpins genome-wide
RT explorations of molecular variation.";
RL PLoS Pathog. 18:0-0(2022).
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};
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DR EMBL; AMPZ03000004; KAH9585553.1; -; Genomic_DNA.
DR EMBL; KL251549; KGB40690.1; -; Genomic_DNA.
DR RefSeq; XP_012800450.1; XM_012944996.1.
DR AlphaFoldDB; A0A095A0E1; -.
DR STRING; 6185.A0A095A0E1; -.
DR EnsemblMetazoa; XM_035734268.1; XP_035589008.1; MS3_0020636.
DR Proteomes; UP000471633; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21780; MobB_Trc-like; 1.
DR CDD; cd05599; STKc_NDR_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF184; SERINE_THREONINE-PROTEIN KINASE TRICORNERED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGB40690.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000471633};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 142..433
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 434..502
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 34..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 541 AA; 62032 MW; 062F0690C26D50BF CRC64;
MSTASSHPYS NLSLTTNPLA TLVKPDIISM SKNSQVINGG GGDLTSSSST TSLNRTNPSI
NSLNVSSHTL DKVKVAKVTL EYYYDNLIVQ YRERQNRYKI LESMMESEGL TEEQKQIKRT
QHALKESEFL RLKRARLTVD DFLPLKIIGK GAFGEVRLVQ KQDNGYIYAM KILHKADMLQ
KDQVAHVRAE RDILVKADNP WVVKMFYSFQ DSVNLYLVME FLPGGDMMTL LMKRDTLTES
QTQFYIAETV LAIDSIHKMG FIHRDIKPDN LLLDAKGHIK LSDFGLCTGL KKAHRTDFYK
DLSQAKPSDF SSGRADSRRR AEGWNKKRRR LAYSTVGTPD YIAPEVFQHH GYTNSCDWWS
LGVIMYEMLI GYPPFCSATP QETYKKIMSW KEALFFPPEM PISNHSRNLI QSLCCGAETR
LSSIEDIRKQ PFFHAVDWEH IRERPAAIPV NIRSIDDTSN FDEFPNADLS WPNVTDPMKS
YQKNLAFINY TYKAFDGWTN NDRILDRQLY QQQKFQRHQT ALSSRSSILS DLTGIKNKSS
T
//