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Database: UniProt
Entry: A0A0R3SSB1_HYMDI
LinkDB: A0A0R3SSB1_HYMDI
Original site: A0A0R3SSB1_HYMDI 
ID   A0A0R3SSB1_HYMDI        Unreviewed;       490 AA.
AC   A0A0R3SSB1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-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   ORFNames=HDID_LOCUS8161 {ECO:0000313|EMBL:VDL60479.1},
GN   WMSIL1_LOCUS4197 {ECO:0000313|EMBL:VUZ44042.1};
OS   Hymenolepis diminuta (Rat tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX   NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000816301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HDID_0000816301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL60479.1, ECO:0000313|Proteomes:UP000274504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:VUZ44042.1, ECO:0000313|Proteomes:UP000321570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMS-il1 {ECO:0000313|EMBL:VUZ44042.1,
RC   ECO:0000313|Proteomes:UP000321570};
RA   Jastrzebski P J., Paukszto L., Jastrzebski P J.;
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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; UYSG01011037; VDL60479.1; -; Genomic_DNA.
DR   EMBL; CABIJS010000122; VUZ44042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3SSB1; -.
DR   STRING; 6216.A0A0R3SSB1; -.
DR   WBParaSite; HDID_0000816301-mRNA-1; HDID_0000816301-mRNA-1; HDID_0000816301.
DR   Proteomes; UP000046397; Unplaced.
DR   Proteomes; UP000274504; Unassembled WGS sequence.
DR   Proteomes; UP000321570; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0035173; F:histone kinase activity; IEA:UniProt.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR024604; GSG2_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR24419; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE; 1.
DR   PANTHER; PTHR24419:SF18; SERINE_THREONINE-PROTEIN KINASE HASPIN; 1.
DR   Pfam; PF12330; Haspin_kinase; 1.
DR   SMART; SM01331; DUF3635; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274504};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          175..490
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  56387 MW;  726DAE46F6785389 CRC64;
     MRLRSGSLVS KPSGDLHKTK KVGRYSLRGT KTPITRHRLR SFNGARMPSR VDTLKRPPDI
     SKWDDTSDVE DRENLNISTS SSKTKELDLS PIISPRRFRS LNKDQSAKIK RLDACKIEVD
     PDESLCHSIC PDESKTANES VLNQSFTADP RTKLLELCGQ TEVKPMSSFF DAECLENVTK
     IGEGVYGEVF QSNKSTVIKI FPIDGSIPVN GERQMESHRV FPEVFISKQL TELGFKYRQN
     RAVNFIQLRR CAIVNGKWPR ELVKAWKKYE ADNGSDNECL DFLPETQEWM VLEFDYAGKP
     LGTFRFTSYR EAHSVIEQIA LSLAAAESAL QFEHRDLHWL NILVKPTKQT KLRYRVNGLS
     YSVQTEGIQV CIIDFTVSRL CHEGNVVYVD MSNSPEIFEC EGDYQFEIYR MMRDMNGNNW
     RPFKPITNLY WVHYLMDKLI RESLFPRRDP DGKAVQSELA ALRDNVLSGD YDSTMSLVRN
     SFFFDSCRIE
//
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