ID A0A0V1ABP8_9BILA Unreviewed; 719 AA.
AC A0A0V1ABP8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine/threonine-protein kinase N2 {ECO:0000313|EMBL:KRY22189.1};
DE Flags: Fragment;
GN Name=mif4gdb {ECO:0000313|EMBL:KRY22189.1};
GN ORFNames=T12_973 {ECO:0000313|EMBL:KRY22189.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY22189.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY22189.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY22189.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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=2.7.11.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000946};
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=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY22189.1}.
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 EMBL; JYDQ01000011; KRY22188.1; -; Genomic_DNA.
DR EMBL; JYDQ01000011; KRY22189.1; -; Genomic_DNA.
DR EMBL; JYDQ01000011; KRY22190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1ABP8; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd11622; HR1_PKN_1; 1.
DR CDD; cd11623; HR1_PKN_2; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 3.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037313; PKN_HR1_1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF210; SERINE_THREONINE-PROTEIN KINASE N; 1.
DR Pfam; PF02185; HR1; 2.
DR SMART; SM00742; Hr1; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF46585; HR1 repeat; 3.
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; PS51860; REM_1; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:KRY22189.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Transferase {ECO:0000313|EMBL:KRY22189.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 698..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..204
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 207..289
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 656..719
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT COILED 137..201
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY22189.1"
SQ SEQUENCE 719 AA; 80899 MW; DF970E4831E5DB8E CRC64;
LFFLSGLLRP FQGVTMAHSQ IPDQLRLLSK KYGLVVNQEP TSADENALQQ LVSKLKKLIR
SLIAREMRFK EGYENMRRAV KDKKQVDALK KNLRSISDKI EDLHSDLFTI EMYATGTADL
SSASSTSDFN DSLNISNAAI NQKLAGLTRE LERESKVKDG LEKFLQMCKD KKMLEGSRQM
LEDSKAKIEL LRMQIARLQQ LHSLNLSSPV EGASPVASPT EIQVDELLHR LRKEAAMHEG
AKNMVKILNQ AKTVEKKSLQ DALDSQLESR EKLDLIRLAL EKHCQQLPTH SPKRESVKTD
IVQSNPSLYR NRTEELPDDA AAANASSQLL LNRHCAASSL AVSGKLEVRL MGCQKLLVDI
PGRAADSSAA AAEPGFSQKK TRSVGSRANT YRLKDNLSEE IYAVLRVDGR KVAQTEPKPY
SQQAWDQRFS IDLERSRELE INVYWNDWRS MCAFTFLKLG NLIDSYQDGR VVQLEPQGTL
FADIRYLNPV ISRKPMLQRQ QKLFRVKAQK VLPVRPGQMH VAAWGRIIKQ FFPQMCQDVP
AHASSPPSGA MNGRASRLIT QRSDSSLLND SLPYVLSPAA ISETSTSSLY PSLKEFGDQD
RKYSFPSSST LIDDRLVQDV KKLEKETLNL KLSARNLNAS SGYRQSTNAT MTIDDFKLIS
VLGRGHFGKV ILSKYRPNNN YFALKILKKA DILSRDEVSV NVFFFVFLLW IGIFSLVSG
//
