ID J7MF35_THEOR Unreviewed; 934 AA.
AC J7MF35;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=[phosphatase 2A protein]-leucine-carboxy methyltransferase {ECO:0000256|ARBA:ARBA00012834};
DE EC=2.1.1.233 {ECO:0000256|ARBA:ARBA00012834};
DE AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1 {ECO:0000256|ARBA:ARBA00032526};
GN ORFNames=TOT_040000771 {ECO:0000313|EMBL:BAM42404.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM42404.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM42404.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM42404.1,
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-
CC methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl
CC ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48544, Rhea:RHEA-
CC COMP:12134, Rhea:RHEA-COMP:12135, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90516, ChEBI:CHEBI:90517;
CC EC=2.1.1.233; Evidence={ECO:0000256|ARBA:ARBA00000724};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC -!- SIMILARITY: Belongs to the SSRP1 family.
CC {ECO:0000256|ARBA:ARBA00010060}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000256|ARBA:ARBA00010703}.
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DR EMBL; AP011949; BAM42404.1; -; Genomic_DNA.
DR RefSeq; XP_009692705.1; XM_009694410.1.
DR AlphaFoldDB; J7MF35; -.
DR STRING; 869250.J7MF35; -.
DR EnsemblProtists; BAM42404; BAM42404; TOT_040000771.
DR GeneID; 20716814; -.
DR KEGG; tot:TOT_040000771; -.
DR VEuPathDB; PiroplasmaDB:TOT_040000771; -.
DR eggNOG; KOG0526; Eukaryota.
DR eggNOG; KOG2918; Eukaryota.
DR OrthoDB; 5472060at2759; -.
DR Proteomes; UP000003786; Chromosome 4.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:InterPro.
DR CDD; cd13231; PH2_SSRP1-like; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR016651; PPM1.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR048993; SSRP1-like_PH1.
DR InterPro; IPR000969; SSRP1/POB3.
DR PANTHER; PTHR13600; LEUCINE CARBOXYL METHYLTRANSFERASE; 1.
DR PANTHER; PTHR13600:SF21; LEUCINE CARBOXYL METHYLTRANSFERASE 1; 1.
DR Pfam; PF04072; LCM; 2.
DR Pfam; PF21103; PH1_SSRP1-like; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 97..215
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
SQ SEQUENCE 934 AA; 108861 MW; DD274F8D46A0847E CRC64;
MRQGQTRYSY IVMQFEADHE TKVDLNLQEN DMKQFKLDKT LEGKASYIEA YSHTSTRATF
VNECPLGKTY NVISRLFGSL VNRSIVVPGD FKSEKGDSAI SCTYKATSGH LFPLNRSFLF
IVKPVIFIRW VLLPTLAIKL APVPVDWAAL TNAMLFEDIV SVEFSRTGVT TQNRFFAILV
SMRGAIEYEF TNIDKSEYKF LYDYLISKQV KVVNAEDTER HERQTFASGV CISQCTFVAW
KQAHERNVQT AMASEVLDVD RKEVKRTGKL TVSRKRAAVE LGYYEDEFVH VFGETYNQIP
IVSLTYVHRV FSSRMISDLF VESFNGKPVQ FVNLGGGLDT LCFYLLKKHP NVICFDTDLE
TQVKLKCELM AGHQIFTDLL PDLKLENGFY SSSRYKMFPL DLTRIEDFQR LLDAGFSKDL
PTLFFAECVF MYIDPDVLNE VGHDGYFTKA LVEKYKEHKL KLSAFQRYRT PEDIKQRFKD
LGWELVSATR GTTFWNLLPE SERKRVLNLQ SFNEFEGLGL HYGYGFCCVA SNKYDNPALH
KTIFTDGMKA NEESELHLED IDYHLKRTSP SFNKQFFDRF FSELWIKVCV ELGYYDDEFI
EFFADPATQS SLLSIVHHIR TVSIRMVADL FVESFNGKPV QFVNLGGGLD TLCFYLLKKH
PNVICFDTDL ETQVKLKCEL MAGHQIFTDL LPDLKLENGF YSSSRYKMFP LDLTRIEDFQ
RLLDAGFSKD LPTMYIAEFS SMYVEAEPMN KFLKFLNEFS NDDSVYFFTE AHFVSNSLGC
AVYRTLESQI KRYEDLSWKL KLVSYNDFYN HNFETEEKKR ILKLEDFKEM DELGTACSHM
ISGLCYKSDR NLSKVLNLFR TYDNHTNLNY YDMPYGINFS KPDFDKALFR HPELREINRR
RDHDRRNKQL FRKTIAQKAW ELPFSKIWIY IISK
//
