ID A0A0V0Y6D9_TRIPS Unreviewed; 1090 AA.
AC A0A0V0Y6D9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Protein-lysine N-methyltransferase T4E_1360 {ECO:0000256|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03188};
GN Name=BicD {ECO:0000313|EMBL:KRX95807.1};
GN ORFNames=T4E_1360 {ECO:0000313|EMBL:KRX95807.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX95807.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX95807.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX95807.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that methylates elongation factor 1-alpha.
CC {ECO:0000256|HAMAP-Rule:MF_03188}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03188}.
CC -!- SIMILARITY: Belongs to the BicD family.
CC {ECO:0000256|ARBA:ARBA00010061}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM4 family. {ECO:0000256|HAMAP-Rule:MF_03188}.
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:KRX95807.1}.
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DR EMBL; JYDU01000051; KRX95807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0Y6D9; -.
DR STRING; 6337.A0A0V0Y6D9; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IEA:InterPro.
DR GO; GO:0070840; F:dynein complex binding; IEA:InterPro.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 6.10.250.2470; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03188; Methyltr_EFM4; 1.
DR InterPro; IPR018477; BICD.
DR InterPro; IPR026635; Efm4/METTL10.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31233; BICAUDAL D FAMILY MEMBER; 1.
DR PANTHER; PTHR31233:SF6; PROTEIN BICAUDAL D; 1.
DR Pfam; PF09730; BicD; 2.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03188};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03188};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03188};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03188}.
FT DOMAIN 915..996
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 744..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..59
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 86..183
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 208..249
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 315..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 761..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1090 AA; 123740 MW; 7C328AD021BB28A9 CRC64;
MSSLEALKSE IDRLSHELDE ACNQKIQAAK YGLQVLEEKQ ALEAKYEALE SSYEVTKQEL
DIALSHFQLK HREVEKHGVQ HEESLLQETA NRESELLSKI TALEQDLRQA DQEISRTKSE
WQQLQEMNDI LKSEKENFEI CARNLKKEMD ELKHREQRLI CDYSELEEEN LNLQKQLDST
KRVQIDFDSM KFELEKLYEE MQVLRFQSDE ASELKEIAER QVEEALRSLQ QEREQRLALK
KEVDQLKNAE LFNSNMSNLA HSVFGMQTFV DNKVSSPAMF KQLQASMEEE VNEEDGESDN
FQPMDLFSEM HGAQVKKIEL ELSSANRQKE EMQKQLDEAN RLMDQIVDVV NSSVVEMMCL
ISGNDPESFK ALLKNDSSLV LTMQQRFLDI VNRLKTLVEN GKLLDGDADV DQQTTERIQA
MQDDMRSLLA HAAQYKAALM QAQNEVCGVS ETLVQFYHDI CTRSGLTPDP VMLEHMKNSD
MYKSNSNNSS FEINCDAECS VGESISLSGG CLALADGRSK VENLEGLVVS NSEKDQLIES
IVGGLKSDVR KLLAGLDVEI EQQTPIFQVI DTVREQVISL NRTVDSALRG CPSSGLVEKA
TKSVPTVAQR SCEELVQQNV QLRSMLSTKR EQIATLRALL KSNKQVAETA LGQLRVRYEN
EKRTVTETMG KLRQELKSLK EDAATFASVR AMFTARCSEY QAEVEDYQRQ LSAAEEEKKT
VNSLLRMAIQ QKLALTQRLE ELEMDRERSN MRRPIGSKAQ QGVGRVSQQQ PSLSSSSSTV
SAVSSNGPRD SKSQNLLPPS SSFSSSSTAS SAFRQLGVRH RRNAFCFPNL KSHLLMHWIS
LFCNIFIYQF LVDFVQKEKA SNQMMSTGSA VATKQFWENV YQVEMENFID TGHVGEACEL
RMIKWLEEHE NIIPKHSSIL DLGCGNASLL LNLAKQGYSN LTGIDYSVSA VQLAQAKANQ
ENLNQVHFQN LDLLNNSENL HNKFDVILDK GTFDVISLRE DADKAVPIYI SNLIRYYCRE
SNLPRLFFIA SCNNTRMELI NYFEMNFEIM DEEHFSTISF GGKTGTTLTC VIFSLKSNAS
NAHIYNPIRE
//
