ID J4D9H7_THEOR Unreviewed; 855 AA.
AC J4D9H7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Phospholipase {ECO:0000313|EMBL:BAM41390.1};
GN ORFNames=TOT_030000652 {ECO:0000313|EMBL:BAM41390.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41390.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM41390.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM41390.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
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DR EMBL; AP011948; BAM41390.1; -; Genomic_DNA.
DR RefSeq; XP_009691691.1; XM_009693396.1.
DR AlphaFoldDB; J4D9H7; -.
DR STRING; 869250.J4D9H7; -.
DR EnsemblProtists; BAM41390; BAM41390; TOT_030000652.
DR GeneID; 20715814; -.
DR KEGG; tot:TOT_030000652; -.
DR VEuPathDB; PiroplasmaDB:TOT_030000652; -.
DR eggNOG; ENOG502TN48; Eukaryota.
DR OrthoDB; 232510at2759; -.
DR Proteomes; UP000003786; Chromosome 3.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR007480; DUF529.
DR InterPro; IPR022742; Hydrolase_4.
DR PANTHER; PTHR11614:SF87; MONOGLYCERIDE LIPASE; 1.
DR PANTHER; PTHR11614; PHOSPHOLIPASE-RELATED; 1.
DR Pfam; PF04385; FAINT; 2.
DR Pfam; PF12146; Hydrolase_4; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000003786}.
FT DOMAIN 502..555
FT /note="Serine aminopeptidase S33"
FT /evidence="ECO:0000259|Pfam:PF12146"
FT DOMAIN 660..834
FT /note="Serine aminopeptidase S33"
FT /evidence="ECO:0000259|Pfam:PF12146"
FT REGION 575..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 97117 MW; DAC591F5D65E909F CRC64;
MAPLFKRKRR QRGEEEITAG PGENRVVSLN VAETKSSDFE VRKRLIFDFL LVTFTPAPGA
IVDKVVLKDT IFWQKGHGMD ECNCVRTYAK KGNIMFVELI VNKGNAPTFE YFYRDYFKWT
STDAEKFALS FSKQVDLFYV RATPKLNING KMNPTFFYIN KSMEAPVWVI TPKPGIWVDR
VVDGIVDIWE KNYKSEICTN AVVLHRKKKP VYVYLLVNEL ELASQEVFFK KDGITWPRVT
KEEFVEAAKA LGCNPETFMN ELTLDLSNAG KNFTVEVLDV DTASTQVITP LTGYKVRKVV
DGEQVIWKDE RSFATNASKL TYTNRGTYEH KHTLLNLYVR QGEKTSVLHF AKLSGVWSRV
DSAKYARMYS QTDDPINTHK HLGVDASGGR KMYMSHFRNK DGLNIHTFHA PVENSKGSMV
LVHGAFGHFC SDYISYSRKF CLDYEHYSPL AELEDFANAN YDTMDSLKMV TRALEERKDC
FEHRRLDGLD MFDTGSRFEY KRSFVEALNN MGYSVYGLDL PSHGHSEGVT TTRFYTNSFL
DYVEDLLQFI NIVKRGKFSD TTQTYEDFTW KDKSYRPKAP SECTRRSGES SIEHMGSLGS
MSSRSQAPEE AQGDASATHG SGEHTQTSPK ASEDKMETRP NSPAHVTKGN LAEYVAAASM
TEPEWVDEKL YLVGYSMGSN ICIRTINEYY RRTKSSKKLI DGLVCLSGMY QLAAISNPVV
QRLAAIFISI LSFFAPKSPN PIEKLFDFTM TFDSLCRLRD PMYATKKSCN KTLLMIAKAT
FDLTKNLSYF PDDLPMLMLN SVKDELVNIE GARKMNKLIK NSKLVELKGT VHGLPLSPYV
TVVTPVLKDW LSGSL
//
