ID A0A0V1HB06_9BILA Unreviewed; 770 AA.
AC A0A0V1HB06;
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 TNNI3K {ECO:0000313|EMBL:KRZ07955.1};
DE Flags: Fragment;
GN Name=TNNI3K {ECO:0000313|EMBL:KRZ07955.1};
GN ORFNames=T11_6265 {ECO:0000313|EMBL:KRZ07955.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ07955.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ07955.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ07955.1};
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 -!- 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:KRZ07955.1}.
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; JYDP01000094; KRZ07955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HB06; -.
DR STRING; 268475.A0A0V1HB06; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR23257:SF975; DUAL SPECIFICITY PROTEIN KINASE SPLA-RELATED; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRZ07955.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 85..117
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 118..150
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 151..174
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 225..249
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 451..706
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 712..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478
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:KRZ07955.1"
SQ SEQUENCE 770 AA; 86524 MW; 247F46A4A8F70A6F CRC64;
LISHLQMGNY MKRPKHSLSD ELYDKISKGY RLSLELLERG LLNDIDFTSD SLLSQLLIAC
YENDVDRLKS MLENLNLDVN SISWRKMSLL HIAVLCEKYE IVKSLLEKEA DVHQIDWASF
TPLHLASYFG FTEIVRLLLL FSSNPNSLTG VQDTPLHLAA LNGHYETVEL LLSKPELCVV
WPNQEKSTVF HYCAQFGHLE IMKLLLDDVQ RYDIISACVH EGNLYGDTPL HNACYSNQFE
IVKLLISRSG FDCLSKENMF SETPLHAACT AGKSVDLIGY LLKQPGVNVN CQGRDGHTRK
SVIAHLVDLS SPCTLFQHCI VPVTMGADMD ISANSQILRN FKYANSGVFG DSDVDFENTA
KGPISVVSQT PIAWAYEQGF DNIVNLLKDV KRSEYSRSST SECSYNSLND YASVTLPSPM
GKLKSVTKEK AEVLQLRNLL GNQYHIQMSD IDLQESVGSG SFGKVYKCVL NNRTVAVKRY
RSWSVGSKSD VKMFCREVSI MSRLNHPNIL QFIGACLDDP SQFALVTEFA QDGSLFSALH
EEKRFFDAEF KFSICFDVAS AMNYLHKRSY PIIHRDLNPH NILLKGNRAL VADFGESRFV
DSRDTDMTRQ PGNLRWMAPE IFLQSGSYTT KADVFSYALC VWEIYTGDIP FVHLKPATAA
AEMAYRNNRP LLSDAIPVKI QSLINKAWHS SVQYRPEFSV IMNELIGTKE QNKEDASSLP
VEGDSTSNSQ SEDSAVLLSI SRFNDLLKLV DKNGYVVDPS QSVSGHRPEN
//
