ID A0A0V0RFB9_9BILA Unreviewed; 1112 AA.
AC A0A0V0RFB9;
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 T07_11728 {ECO:0000256|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03188};
GN Name=Bicd1 {ECO:0000313|EMBL:KRX13180.1};
GN ORFNames=T07_11728 {ECO:0000313|EMBL:KRX13180.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX13180.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX13180.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX13180.1};
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:KRX13180.1}.
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DR EMBL; JYDL01000218; KRX13180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0RFB9; -.
DR STRING; 6336.A0A0V0RFB9; -.
DR Proteomes; UP000054630; 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:UP000054630};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03188};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03188}.
FT DOMAIN 929..1025
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 757..819
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..344
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 774..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1112 AA; 125891 MW; AEA71F3F40F6AE63 CRC64;
MSSLEALKSE IDRLSHELDE ACNQKIQAAK YGLQVLEEKQ ALETKYEALE SSYEVTKQEL
DIVKEALSHF QLKHREVEKH GVQHEESLLQ ETANRESELL SKITALEQDL RQADQEISRT
KSEWQQLQEI NDILKSEKEN FEICARNLRK EMDELKHREQ RLICDYSELE EENLNLQKQL
DSTKRVQIDF DSMKFELEKL YEEMQVLRFQ SDEASELKEI AERQVEEALR SLQQEREQRL
ALKKEVDQLK NAELFNSNMS NLAQSVFGMQ ILGDDKVSSP AMFKQLQASM EEASEEDGES
DHFQPMDLFS EMHGAQVKKL ELELSSANRQ REEIQKQLDV CMRLLNCILF EEANRLVDQI
VDVVNSSVAD VMCLICGNVP ESFKGLFKDD NSLILTMQQR FLDIVSRLKT LVENGKLLAS
DAVVDQQTTE RIQTMEDDLR SLVAHAAQSK ACLMQAQNEM CSVSETLAQF YHDVCSRSGL
TPDPVMLEHT KSSDLYKSNN SSFEISYDAE CSSVDESISL SGGCLAIADG RGKVENLEAR
VVSTSEKNQL VESIVGDLKS DFRKLLAGLD VEIEQQAPLF QVIDTVRDQV TSLSRTVDSA
LRGCSSSEVV EKATKSVPTT AQRSSEELVQ QNVQLRSMLS TKREQIATLR TLLKSNKQVA
ETALGQLRVR YQNEKRTVTE TMGKLRQELK SLKEDAATFA SVRAMFTARC CEYQAEVEDY
QRQLSAAEEE KKTLNSLLRM AIQQKLALTQ RLEELEMDRE RSNMRRPIGS KAQQGVGRVS
QQPSSSTASA VSSNGPRDSK SQNSLPPSSS SSASSAGSAF RQLGVRHRRN AFQISNHTDR
STIAVALDII LCNISYFFLL VLTQCGEKAS NQMMSTGSAV ATKQFWENVY QVEMENFVDS
GHVGEVWFGK ACELRMVKWL EERENIIPKH SSILDLGCGN ASLLLNLAKR GYSNLTGIDY
SDSAIQLAQA KANREKLNQI HFQNFDLMIN SENLHNKFDV ILDKGTFDVI SLREDAEKAI
PVYISNVTHY YCRKSNLPRL FFIASCNNTR TELINYFETN FEIMDEEHFS TINFGGKTGT
TLTCMIQTSI PDRSCLRIGR KSNLQATSSN HR
//
