ID A0A2A9LZK3_9APIC Unreviewed; 873 AA.
AC A0A2A9LZK3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Histone arginine methyltransferase PRMT3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BESB_030430 {ECO:0000313|EMBL:PFH31169.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH31169.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH31169.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH31169.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) 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:PFH31169.1}.
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DR EMBL; NWUJ01000016; PFH31169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9LZK3; -.
DR STRING; 94643.A0A2A9LZK3; -.
DR VEuPathDB; ToxoDB:BESB_030430; -.
DR OrthoDB; 205250at2759; -.
DR Proteomes; UP000224006; Chromosome xiii.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006:SF122; ARGININE METHYLTRANSFERASE 8; 1.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR Pfam; PF06325; PrmA; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015};
KW Reference proteome {ECO:0000313|Proteomes:UP000224006};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015}.
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 95299 MW; ABFC86BD8824872E CRC64;
MQLLEHPSHE SAPREKQAIK SRTRTREKGR SHAGLSRYAR LDRATHQYKG VFFFVESVFP
ARVVVGSRGA SLASNGEGDA SPVAESFTRA SFSSSCCTSA DSRVAFLAQR LAMTSCASAN
NGACPPQADC ASGGQPEAGR LFASREAFLE RRRYFESLGL IDAGDDLCRA NKEKTEKSDS
EDDAETAREA GARAERRTRH VAKRRDVDGA QDDGEASLLA PCLCLFCSFA SADLRCMHSH
LEELHGLNFF EPHGRWHPRR LLAGADAGAA SASSSPSSAS SSGSREDAPA AAAFAELPPL
TSYYRIALIN FLRNLAPAAP QERLQAWRAG SVETQPTEFE AVTRAFAALN RDAACWRDEK
FLQPAWAEDR LLWEEVCSDS EEDEEEEGEE EEEGEEEEEA ETRGWGVKCG RAGQEGGSDD
EIRGASVTQE DRNYFAGYAE LPIHREMICD TARTEAYRDF ILQNRDLFEG KVVLDAGCGT
SILSLFCAQA GARKVIGVDG ATGVARVAEK IVKMNHFTHV VQIVTGKMED FVLVWADEAR
HTVKAIPRET FSPSSWEKVR VDIIVSEWMG YCLLFESMLY TVLHARDEYL KPDGLLVPSR
AVMGAFAADC LPEIEAQLGK RFAEPVYGLD FSLLCLPDAA ALRSADVALI KPHRLLSSPT
PFCLLNLYAV SAADVQTLRA PFSIDLTQRP VHLAALPATT SSVCTTMVIY FDCFFERLRE
GELPGEAAPV VFFAAGSPVA ASWYASGDAK PVAEATAGGL CLSTSPLRQD THWKQTMLHL
RGHDGQGMEV LPQWVATEIA QRGEETSSEA ETSARVAASR APLSKLEGYI SMNPDPQRSR
SLAVTVEMRQ LPYRDESGEV AIAPCVINTF SVA
//
