ID A0A0V1CPP5_TRIBR Unreviewed; 1100 AA.
AC A0A0V1CPP5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Protein-lysine N-methyltransferase T03_5640 {ECO:0000256|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03188};
GN Name=Bicd1 {ECO:0000313|EMBL:KRY50707.1};
GN ORFNames=T03_5640 {ECO:0000313|EMBL:KRY50707.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY50707.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY50707.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY50707.1};
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:KRY50707.1}.
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DR EMBL; JYDI01000143; KRY50707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CPP5; -.
DR STRING; 45882.A0A0V1CPP5; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03188};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03188};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03188};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 826..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 916..1005
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 746..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..186
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 211..252
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 317..347
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 763..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 124366 MW; 80576AFC1660CE12 CRC64;
MSSLEALKSE IDRLSHELDE ACNQKIQAAK YGLQVLEEKQ ALETKYEALE SSYEVTKQEL
DIVKEALSHF QLKHREVEKH GVQHEESLLQ ETANRESELL SKITALEQDL RQADQEISRT
KSEWQQLQEM NDILKSEKEN FEICARNLRK EMDELKHREQ RLICDYSELE EENLNLQKQL
DSTKRVQIDF DSMKFELEKL YEEMQVLRFQ SDEASELKEI AERQVEEALR SLQQEREQRL
ALKKEVDQLK NAELFNSNMS NLAQSVFGMQ ILVDDKVSSP AMFKQLQASM EEANEEDGES
DHFQPMDLFS EMHGAQVKKL ELELSSANQK REEMQKQLDE ANGLVDQIVD VVNSSVADVM
CLICGNAPES FKGLLFKDDN SLILTMQQRF LDIVSRLKTL VENGKLLASD AVVDQQTTER
IQTMEDDLRS LLAHAAQSKA CLMQAQNEMC SVSETLAQFY HDVCSRSGLT PDPVMLEHSK
SSDLYKSNNS SFEISYDAEC SSVDESISLS GGCLAIADGR GKVENLEARV VSTSEKNRLV
ESIVGGLKSD FRELLAGLDV EIEQQAPLFQ VIDTVRDQVT SLSRTVDSAL RGCSSSGVVE
KATKSVPTTA QRSSEELVQQ NVQLRSMLST KREQIATLRA LLKSNKQVAE TALGQLRVRY
QNEKRTVTET MGKLRQELKS LKEDAATFAS VRAMFTARCC EYQAEVEDYQ RQLSAAEEEK
KTLNSLLRMA IQQKLALTQR LEELEMDRER SNMRRPIGSK AQQGVGRVSQ QPSSSTASAV
SSNGPRDSKS QNSLPPSSSS ASSAGSAFRQ LVFKSQITPT DQQQLLLHWI LICAIFRASV
SFLFFLLVLT QCGEKASNQM MSTGSAVATK QFWENVYQVE MENFVDNGHV GEVWFGKACE
LRMVKWLEER ENIIPKHSSI LDLGCGNASL LLNLAKRGYS NLTGIDYSDS AIQLAQAKAN
REKLNQIHFQ NLDLMINSEN LHNKFDVILD KGTFDVISLR EDAEKAVPVY ISNVTHYYCR
KSNLPRLFFI ASCNNTRTEL INYFETNFEI MDEEHFSTIN FGGKTGTTLT CVIFSLKNNA
IIVSCFLKLF KFDLGHNSNI
//
