ID A0A0V0V308_9BILA Unreviewed; 1020 AA.
AC A0A0V0V308;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=T09_11297 {ECO:0000313|EMBL:KRX57890.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX57890.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX57890.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX57890.1};
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:KRX57890.1}.
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DR EMBL; JYDN01000094; KRX57890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0V308; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 PANTHER; PTHR47167; SERINE/THREONINE-PROTEIN KINASE TAO1-LIKE PROTEIN; 1.
DR PANTHER; PTHR47167:SF4; SERINE_THREONINE-PROTEIN KINASE TAO; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KRX57890.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 28..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 360..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 471..583
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 362..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 118274 MW; 81C4F6843CD86533 CRC64;
MPIALKPGSL KDPEIAALFR TEDPESYFAD LREIGHGSFV GFGYSWPRMC SHQKDVIWWE
AKWNDIVKEV KFLKNLRHEN IVEFKACFLK DHTCWLVMEY CVGSASDILE VHKKPLREQE
ISAICQQVLH GLRYLHSLGR IHRDVKAGNI LLTDSGVVKL ADFGSASLVC PAQSFVGTPY
WMAPEVILAM DEGRYNDRAD VWSLGITCIE LAEKKPPFFN MNAMSALYHI AQNDSPSLPV
GSWSSDFHDF VDQCLIKDPA LRFSTETCLL HPFISSARPA SILFDLIQRT KLLVRDLDHF
QYRKLRKLIV DDDLCAESAS SRSDSYTSTQ SLCGAMRSSI TSVSSLKKAQ RSLVPIVPLA
DDSTTSPLSR TPPLSGSVDT DTDTDVTPPR PSLTPTAKTA SMEMNHEQQQ QQQHQHQQQE
QQQQLSIVGP RRRKEEILAW RRSRFATIRP TVTIAREQTE YAAENNMHEQ MSGYKRMRRE
HQKELKQLEE KFNSEMDNLK MKLDREYENL LLQFHKEMDK LHVTHRQELD KRLKTNEELE
RKLRKAIVQQ QEVEMKALQM QLKKEYKVNK ERLKQELKME NSSKSFVEGN LKTSKQNHLH
VQAEAENRLI ADHKFYLDFE IRKLKRRRLL HYHQLEQDLI REELGVRGRQ LQSAHTLLRR
HHELTRDLEM RQLNSLQNLR CQHLQKQHAS ELQNQQAYMK RVQDELRKKH AMQVKQQPKE
LKQKELQIRR QFRQAVKTQT RQYKLLQLQL TQDLPKDEQR EVVARLKDEQ KRKLALLAEQ
YEGSIGEMME KQTVQLETWQ EEEARQTKDK LNEELELLMA FQSKQRMQMD QHHEREKGRL
NEKVSLRLAV LENKMDDEVT QFERERQDRL NQLQTRQNQE LDVFDQASIH LGFSLIALSA
SSSSTSTASG SSSSATAVAN KPGVINSASI QDAIHQQPTT DNSFQAVTAH HHHQHLSSSS
SSNNNNNNNN NSRNNNNSNN NNSNNNNNQC ISPSLHPSAS SGKQRYELLE EDYRKKWAIS
//
