ID A0A0K0JIU3_BRUMA Unreviewed; 932 AA.
AC A0A0K0JIU3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Bm5417 {ECO:0000313|EMBL:CRZ22392.1, ECO:0000313|WBParaSite:Bm5417.1};
GN ORFNames=Bm5417 {ECO:0000313|EMBL:CRZ22392.1,
GN ECO:0000313|WBParaSite:Bm5417.1, ECO:0000313|WormBase:Bm5417},
GN BM_Bm5417 {ECO:0000313|EMBL:CRZ22392.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CRZ22392.1};
RN [1] {ECO:0000313|EMBL:CRZ22392.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ22392.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CRZ22392.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ22392.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm5417.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2019) to UniProtKB.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369}.
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DR EMBL; LN856386; CRZ22392.1; -; Genomic_DNA.
DR EnsemblMetazoa; Bm5417.1; Bm5417.1; WBGene00225678.
DR WBParaSite; Bm5417.1; Bm5417.1; WBGene00225678.
DR WormBase; Bm5417; BM39024; WBGene00225678; -.
DR OrthoDB; 55859at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11579:SF9; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE DOMAIN-CONTAINING PROTEIN 1-LIKE PROTEIN; 1.
DR Pfam; PF01135; PCMT; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006672}.
FT REGION 377..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..405
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..815
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 105080 MW; 57008B46B6940776 CRC64;
MGLAASSGHD NDDLIDKLID ANIVVTHRVE IALRLVDRRR FFPVEGRYIA YKDLAWKSDF
GSPGRIHISA PCIYGNVLEC LDLQEGNSFL NVGSGTGYLS TVAGYLLGSN GTNHGVEIHS
NIVDYARSLV VETLNCPETQ CYDWAIPQFS CGNGLHLSPS HYSKYDRVYC GAAVPPSYRR
ILWELLKVNG ILVMPYEDQL LQVRRQSANV FDVKIITSVS FSDFIPPTEE ETSKELYSNA
PSFRMVPTLQ FLCALSIRKI IRAAVASNHK IHIRNFVGQQ PHRIRENHVV VQFRDGEQPV
AQQFHFENRH PPLREILAIV GADFIGDDEN DVNDDVGEAE PGRRRRLVRD RFRMVWFRHH
LRAHIANRVV RRRRPLDGEA EAEAQEEDAG IEDDQNSDVE ITDENENSEY SGSGSLSATT
SDPTDTSVDT TESCNDNTSA TGRSKKRSLE EYDGESSLSV KRRNDDDKGF TDKGTMEIGL
VNDYKTQNIP NENVPDENGS NDESAITTIA QETLTQPEGN ANQKSEENLP EQSEHFEEAK
NSNNLKFVER TVENSEGSVS HWAEVVEQLR DLREREAEDN RIIVVGSISK HNGNSFHSSL
RDQSIDSCEV QNGITRSNDF GNSNHDEKYE QESSKSANLS VQIQNSKMHN EANDEKWVNN
LTNTNIHSTE PDEMENTLRA DREFFPSSKD FDTKDDELMW QNNKLYKNKS ETSSAERYNS
NNCENLVSNS SDKSEILSTS NNELEQDKSH LITNVEGGNS DNDGDNDDYG DDGDDVDDDD
DDNDDDSDDD SDDTDDEEDG SADSNSSDPE DQEDNPEYNN GNHFYPVNSR DENDLYLAVH
ETARNITAAI NDQAFNHNRG NGGEAMNNNS SSRRRSNARD ELQADEKKRE QARLEERGRQ
LSDIRKFAAL FESRVMDLPL NSALKKYIKC LC
//
