ID A0A2U9C219_SCOMX Unreviewed; 454 AA.
AC A0A2U9C219;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase {ECO:0000256|RuleBase:RU362022};
DE EC=2.1.1.100 {ECO:0000256|RuleBase:RU362022};
GN ORFNames=SMAX5B_000532 {ECO:0000313|EMBL:AWP09172.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP09172.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP09172.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the post-translational methylation of isoprenylated
CC C-terminal cysteine residues. {ECO:0000256|ARBA:ARBA00023572}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-
CC adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-
CC cysteine methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:21672, Rhea:RHEA-COMP:12125, Rhea:RHEA-COMP:12126,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90510,
CC ChEBI:CHEBI:90511; EC=2.1.1.100;
CC Evidence={ECO:0000256|ARBA:ARBA00001450,
CC ECO:0000256|RuleBase:RU362022};
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000256|ARBA:ARBA00011133}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU362022}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU362022}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. Isoprenylcysteine carboxyl methyltransferase family.
CC {ECO:0000256|RuleBase:RU362022}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL22 family.
CC {ECO:0000256|ARBA:ARBA00007817}.
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DR EMBL; CP026253; AWP09172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9C219; -.
DR STRING; 52904.ENSSMAP00000004583; -.
DR Proteomes; UP000246464; Chromosome 11.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 1.20.120.1630; -; 1.
DR Gene3D; 3.30.1360.210; -; 1.
DR InterPro; IPR007269; ICMT_MeTrfase.
DR InterPro; IPR025770; PPMT_MeTrfase.
DR InterPro; IPR002671; Ribosomal_eL22.
DR InterPro; IPR038526; Ribosomal_eL22_sf.
DR PANTHER; PTHR10064; 60S RIBOSOMAL PROTEIN L22; 1.
DR PANTHER; PTHR10064:SF2; 60S RIBOSOMAL PROTEIN L22; 1.
DR Pfam; PF04140; ICMT; 1.
DR Pfam; PF01776; Ribosomal_L22e; 1.
DR PROSITE; PS51564; SAM_ICMT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU362022};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362022};
KW Methyltransferase {ECO:0000256|RuleBase:RU362022};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU362022};
KW Transferase {ECO:0000256|RuleBase:RU362022};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362022};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362022}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT TRANSMEM 49..67
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT TRANSMEM 198..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
SQ SEQUENCE 454 AA; 51312 MW; 6C0DA6B0E4FA1A7F CRC64;
MAGSKLGLEG RVSVKSFILG LSVLVVPLIR TWFGHLDWVF DYLTDTPGKI VICVHVAVLN
GLLLLLYRGP LYKVAVRACF LGVTFGCGLI ISFSETTWTH FGWYLCSLSF FHYSEYLVTA
IINPRSLSLD SFLLNHSVEY TLAAISSWLE FTAEKMVVPG VPVRVSVYPL VAVRACFLGV
TFGCGLIISF SETTWTHFGW YLCSLSFFHY SEYLVTAIIN PRSLSLDSFL LNHSVEYTLA
AISSWLEFTA EKMVVPELKQ LSWLSCAGLL MVMCGDGLRK AAMLTAGSNF NHIVQNEKAQ
SHVLVTDGVY AYFRHPSYVG WFYWSIGTQK KQSTGKGGKK KKQLLKFTLD CTHPVEDGIM
DAANFEQFLQ ERIKVNGKAG NLGDGVVSIE RSKSKITVSS EVPFSKRYLK YLTKKYLKKN
NLRDWLRVVA NTKESYELRY FQINQDEEEE EEED
//
