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Database: UniProt
Entry: A0A0N5A1Q9_PARTI
LinkDB: A0A0N5A1Q9_PARTI
Original site: A0A0N5A1Q9_PARTI 
ID   A0A0N5A1Q9_PARTI        Unreviewed;       585 AA.
AC   A0A0N5A1Q9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Protein kinase domain-containing protein {ECO:0000313|WBParaSite:PTRK_0001555800.1};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001555800.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001555800.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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DR   AlphaFoldDB; A0A0N5A1Q9; -.
DR   STRING; 131310.A0A0N5A1Q9; -.
DR   WBParaSite; PTRK_0001555800.1; PTRK_0001555800.1; PTRK_0001555800.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0005925; C:focal adhesion; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR036137; Focal_adhe_kin_target_dom_sf.
DR   InterPro; IPR005189; Focal_adhesion_kin_target_dom.
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   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418:SF367; INACTIVE TYROSINE-PROTEIN KINASE KIN-32; 1.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   Pfam; PF03623; Focal_AT; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF68993; FAT domain of focal adhesion kinase; 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; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}.
FT   DOMAIN          64..323
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   585 AA;  68655 MW;  5B47D7010FD4FE0E CRC64;
     MQHGSVWNVK NILFRSPNSI DLETKNLLNM KRIINFPLDT ASSSSTSSPL TIRREDLQID
     RKKILLEELL GEGHFGNVYK GSFTDNYKKH HNVAIKVCKS NTEEKEINNF ISEAYLMHNF
     RHPHIIRLIG ICEDNPVWIV MELSPLGELR QYLIRQKYTI DLHTQIMFSY QLSTALKYLH
     DKKFVHRDIA ARNVLVSSPK CVKLSDFGLS RNLQDEDYYT SENSKLLPIK WMSPESINFR
     KFDSTTDVWM FGVCIWEILC YGQKPWQGIR NHEVIVKIEQ GIRLEIPQSC PLIIYDLLYD
     IWNYEGEKRP SMEDIKDNLQ GFLLQLEKGI PYNKMEFVVK RRESIKMSNN NHDNRQSYIS
     CKPIGSIKLD TTQVEPTFLI KALEQQRLQS EEDERWLNEF ENGDFIKDDR DVDSGKNSES
     SGCGYQLDRE HDMIYKTVTE LVDCITNFNQ NYKKTLPNDD FVRNVKYITN ALKNLFHEST
     KNLVLLEDDD RKNVEKAETL LGDNMREMAK AMSHVVEPYI DNCDVLEESR LEVLKITHML
     AINSKHFLES FDNARLKTRF QRRRKRYESH LKNQGISTTE KISFC
//
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