ID U6G984_EIMAC Unreviewed; 1032 AA.
AC U6G984;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glycine hydroxymethyltransferase, putative {ECO:0000313|EMBL:CDI76821.1};
GN ORFNames=EAH_00019840 {ECO:0000313|EMBL:CDI76821.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI76821.1};
RN [1] {ECO:0000313|EMBL:CDI76821.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI76821.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI76821.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI76821.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00008941}.
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DR EMBL; HG670470; CDI76821.1; -; Genomic_DNA.
DR RefSeq; XP_013252707.1; XM_013397253.1.
DR AlphaFoldDB; U6G984; -.
DR EnsemblProtists; CDI76821; CDI76821; EAH_00019840.
DR GeneID; 25270054; -.
DR VEuPathDB; ToxoDB:EAH_00019840; -.
DR OrthoDB; 1699at2759; -.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR InterPro; IPR044571; P4KG1-8.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR PANTHER; PTHR45800; PHOSPHATIDYLINOSITOL 4-KINASE GAMMA; 1.
DR PANTHER; PTHR45800:SF11; PI3K_PI4K CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:CDI76821.1};
KW Transferase {ECO:0000313|EMBL:CDI76821.1}.
FT DOMAIN 153..481
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|Pfam:PF00454"
FT REGION 648..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 112434 MW; 618D5D640B98A904 CRC64;
MPAVEGPAAA GGAGGGGGVM MLPSHPLYYF STHNALRGAD GDDLHFRVCF EELHGSRSCE
LDVYPFYDVQ MVKDVRLIFR GCELPNWRPM TVFFENPVKR LLWAVRGGSA QASIRPFARS
QTFRSKELLR ILEEVRLGFR RNVAPKLTMD GTGGTYILFD GRRRPVAVFK PEDEEAFAPC
NPRGYEGRLG QQGLRGGVLS GEGAGREFAA YLLDASYGGF AGVPATMMVE ACHPAFCSRG
QIEVDGDVMM STYVRSESSP SVSWKVGSFQ AFVEAKECVG NFDARLFSVG DVHRIAIFDL
RVMNLDRNDS NILVAPVVGY QKEPSAGGSS RSLRASGGVV KQIESKLLRS VSAVGSCGTQ
LCVADKAAVA GAETAASAAS GVLTPDGKPT KWSNRRFRLI PIDHGMILTD VLDVATLDLV
WFDWPQSKEP YSESELRLIY SFDVDKDLER LSRRVALRDN CLRTLRLATK LLQICARHHL
TVRETATIAV RDDFDIPSPL EHLIRRSLEI SYLALDSTSL MSTNRLGFGI MDLAELQGDP
GKQQGLRRTS FEAKLKKAFR KKKRGGDEGP VEETAVDANG ICSRCGGFVA VSGAAAVSTA
VITSVSCRVP STLDPDGEVD SEEFEERPLL RSCTTIEAWS DARSPVGAHA EVDVSEPRAS
RNTAAAALDR ATVQPAGSRL HSVENVRGRL PSGSAEDERQ TAGGTAPCRC GDRIERRSSS
SLGDSADSDS DLTSNSLSTS SNDGTQSSWT SSHSDDDSSK AASEVGARLA PPTFGSFQAP
GAAGGPLRHL PSAALFRYPS GEPRFSGRQK RRTSRSRRRK APTETETKTD DAAPAVPSPP
RNEPAVFGNR HTKGTVRRLN GTARGTGCRP KKQPSATQST WSLTDSSGRV ILLDWRDGRL
EKLFFEVYES LLRQHILHNH PQWFTYPYNG EAIERSERRQ QSFRREESGS LVTPLVATPT
VHVNSQQIHA TNTHRRLSSE ASDDASASAA DRHLTHKHLR SVQQPQPQSP AQLEDRAPAA
SRQTRFNISS DA
//