ID A0A0V0X784_9BILA Unreviewed; 573 AA.
AC A0A0V0X784;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=Pak1 {ECO:0000313|EMBL:KRX83899.1};
GN ORFNames=T06_11617 {ECO:0000313|EMBL:KRX83899.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX83899.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX83899.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX83899.1};
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:KRX83899.1}.
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DR EMBL; JYDK01000010; KRX83899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0X784; -.
DR STRING; 92179.A0A0V0X784; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR CDD; cd06614; STKc_PAK; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF10; SERINE_THREONINE-PROTEIN KINASE MAX-2; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:KRX83899.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transferase {ECO:0000313|EMBL:KRX83899.1}.
FT DOMAIN 28..41
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 254..506
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 137..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 573 AA; 64464 MW; BB55E2FAEE45CCCC CRC64;
MITILKSFFK TGSDVESGSS DAEDSVRISK PYNTKHEFHV GYNEQTGEFS GVPEPWLKLL
HTQISKADQK KNPRAVVHAL KFYATSIKRK QPTKFLIQKD SITQSDDDLI DVDPETCSPP
LSIRTDTEPI IQQAKFVHPE PQVKELEQRP TPPPLPPKPQ NRNIFAQQAK QRQINNEVTE
NLPAAVQPTL NEQSRSSSSS GQCQSGEQCR KISADDAETV AERKQSAAVL STRDSRILEE
LKSIVSPENP SEKYEFISKI GSGASGKVYL AKNPLTQQTV AIKCMDFKAQ QKKEMLLTEI
KVMKQYRHRN LVNYLESFLV EDDDLWVVME YLEGGCLTDV VTETILDERQ IASVLLECLK
ALHFLHSHSI IHRDIKSDNV LLGLDGSVKL TDFGFCAQLN PQRSKRSTMV GTPYWMAPEV
VNRKQYNHKV DIWSLGIMAL EMLDGEPPYL NEAPLKALYL IAQHGKPEIK QIDRLSASFV
DFLDRCLCVD VEERATAEQL LAHPFLTCAS PLSRLVPYIR AVKQMKLKAK TPTVDHHQHQ
QNNNTNTATV TTTTDTTIDS ATPQSAYSCD VHQ
//
