ID V5BFB5_TRYCR Unreviewed; 858 AA.
AC V5BFB5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:ESS64742.1};
GN ORFNames=TCDM_07107 {ECO:0000313|EMBL:ESS64742.1};
OS Trypanosoma cruzi Dm28c.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS64742.1, ECO:0000313|Proteomes:UP000017861};
RN [1] {ECO:0000313|EMBL:ESS64742.1, ECO:0000313|Proteomes:UP000017861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dm28c {ECO:0000313|EMBL:ESS64742.1,
RC ECO:0000313|Proteomes:UP000017861};
RX PubMed=24482508;
RA Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL Genome Announc. 2:e01114-13(2014).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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:ESS64742.1}.
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DR EMBL; AYLP01000081; ESS64742.1; -; Genomic_DNA.
DR AlphaFoldDB; V5BFB5; -.
DR EnsemblProtists; ESS64742; ESS64742; TCDM_07107.
DR VEuPathDB; TriTrypDB:TCDM_07107; -.
DR Proteomes; UP000017861; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd06093; PX_domain; 1.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024311; Lipocalin-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24351:SF248; PROTEIN KINASE; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF13924; Lipocalin_5; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ESS64742.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000017861};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 30..154
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 251..306
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 354..608
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 609..681
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 172..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 858 AA; 97929 MW; D6AFEDBBFD0FE60A CRC64;
MISKLFRLDP QRREKHEINP HDIKALRGMA ATHNITSVAV PQYRVRENYV EYVIECSKRS
VKWHVFRRYQ QFRALDQKLK QFCSMGSQYH CEYGVLPVLT GSHWAEVTNQ SIDLVEKRRR
YLEIYLEQLL VPKNLFYVAK TALYKFLHEG EVPVRCGTNV LRPLIGFAAV EPSRRPEESE
DDATTVEESP NPLDISAAGG NLPVTTTFCT TPERGVSNSV ESFSTNRSSG MEEYDDVPSR
EDTDNEDIHM PPASPLCLQC NAEFSSMLYP HRCFLCKQRF CRNCLRNVEL EEEVVRVCLQ
CYENHERHSK KKQTAKDATP ETPFSQFKGV TTAPEILQLH EGNQLRTDVS LSDFELVTTL
GRGTFGKVLK VIFRENGQVY ALKILNKCII HKRRMVEYIK EEKDIMASLP FHPYVVTCHF
AFQTDYHLFF VLDFLPGGEL YSHIYPKCTL SPVDVRLIIA EVVLALEHLH RYDIVHRDLK
PENIVFAADG HLKLTDFGLA RMNFSRHRRY SFVGSPEYLA PETIRGECQS RALDWWSVGV
MMYEMLVGST PFHAANNNDV CNNVLNRTLD LTAPCFTPEA ASLIRQLLQR QPKQRLRDAE
QIKAHPYFAS LNWSALENKS LPPPIRLNLE GNDTKYFKRE FTAEWAVIAR PQEVSRATLD
MLKKQFSNFV HVPDVGAGVS LPSPSSGKRA SLPQSIKADA DEVLTVQRLL GIWRLVRVEM
TTDDGKIAYP WGSEVCGLLA YFPNGIFTMQ FTLSRRPHTG SHFPEQATVD ELVEMCNSYV
ASFGRYQLKA ESNAIVHCPN GSLFPNPSWN QQKFFVEVSS EKSVGGVAAL KLCTPQYNLQ
EEQLLARTVL TWERADAC
//
