ID A0A498SM03_ACAVI Unreviewed; 531 AA.
AC A0A498SM03;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=NAV_LOCUS5808 {ECO:0000313|EMBL:VBB31017.1};
OS Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX NCBI_TaxID=6277 {ECO:0000313|EMBL:VBB31017.1, ECO:0000313|Proteomes:UP000276991};
RN [1] {ECO:0000313|EMBL:VBB31017.1, ECO:0000313|Proteomes:UP000276991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) 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};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; UPTC01001076; VBB31017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498SM03; -.
DR STRING; 6277.A0A498SM03; -.
DR Proteomes; UP000276991; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR48012:SF16; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000276991}.
FT DOMAIN 57..333
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 531 AA; 60668 MW; 82C75888CDCCD9DB CRC64;
MAESEMRRME EFGESSRIQQ DVEYGESQIQ QDVESEESSQ VQPVVQELPW PANKEGYRLE
EIIGSGATST IYRAFCMERE AICAIKRVDI EKHNLTQLGK EIKDLMACRH PNIISYHTSF
QVGKTMWIVM RLLDCGSLRQ IMDRQITAMG GRYELTRGVL PQPIIATILK ETLIALDYIH
RSQLVHGDVK TSNILISSAG NVQLADFGPS IWLESEERTK KSMSGTLCYL APEIAVLEMD
DSERAFTYTF SVDIWSLGIT TLEMATGYPP YHNKIATMTL KLIRGSNPPS LDTYEVCNYR
EYGKQYRHFL SLCLKKNAKQ RWSAKKLLTH PFVAGKAKNA EFLANALLRT PPAGSSSGGQ
SSSRRLPPIT DNFEIEPANV EWDFDVEEEQ RRVNRINKTH IHMPATIPPS AEISMCMNLT
TKTSSFQYVN IIECIENQAR SERILMAEKL FHSCKYSIEE QVFQLVEKRK LEARYMVIVV
ANLCKVATAA QRQNLEGKYF AFIIEKRKTL VTVLEISINI WRYITDHRVP H
//
