ID A0A2A2JWK3_9BILA Unreviewed; 436 AA.
AC A0A2A2JWK3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase {ECO:0000256|ARBA:ARBA00023656, ECO:0000256|RuleBase:RU362022};
DE EC=2.1.1.100 {ECO:0000256|ARBA:ARBA00012151, ECO:0000256|RuleBase:RU362022};
DE Flags: Fragment;
GN ORFNames=WR25_19451 {ECO:0000313|EMBL:PAV66033.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV66033.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV66033.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV66033.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU362022}; Multi-pass membrane protein
CC {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|ARBA:ARBA00009140, ECO:0000256|RuleBase:RU362022}.
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:PAV66033.1}.
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DR EMBL; LIAE01010173; PAV66033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JWK3; -.
DR STRING; 2018661.A0A2A2JWK3; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:UniProt.
DR GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd19049; LGIC_TM_anion; 1.
DR Gene3D; 1.20.120.1630; -; 1.
DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR007269; ICMT_MeTrfase.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR025770; PPMT_MeTrfase.
DR PANTHER; PTHR12714; PROTEIN-S ISOPRENYLCYSTEINE O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR12714:SF9; PROTEIN-S-ISOPRENYLCYSTEINE O-METHYLTRANSFERASE; 1.
DR Pfam; PF04140; ICMT; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR PROSITE; PS51564; SAM_ICMT; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU362022};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362022};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU362022};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU362022};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT TRANSMEM 203..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT TRANSMEM 230..252
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT TRANSMEM 287..308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT TRANSMEM 355..378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362022"
FT DOMAIN 22..130
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAV66033.1"
SQ SEQUENCE 436 AA; 50535 MW; 19F3C562D9C5FD2D CRC64;
NYSCLEARFY MRRDVGYHIA NTYVPTTICV VFSWISVWLP EEFVEGRIFV SLTVFLTLSA
ENNSAKEELP KVSYVKAIDI WFGFTSTFVF VTMLQALTVI SFEHQSKLMR EKAEKQMDQY
SKLHMTKAFL LHRYYHKQAR NLDTFCKLIH DVELKLCCLW FLSSTICSIV GLIFLPFQWI
LSLLVVEFIA SYMLGSTRGS RPLCTLQATV LGAVLGLTVA SSFSTDYEPL QIFCRYVSLF
VIFHFSEYFF TAISNRRSLQ PDSFLLNHST AYWVAAITSW VEFWVETYFF PSIKCSSISS
VGVFLVLVGE CLRKLAMLHA GSGFTHRLAQ TKRPDHRLTT TGVYALIRHP GYSGWFLWSV
STQLVLCNPI CIFAYAYVSW LFFEERILDE EKDLLRFFGQ QYADYQRKVW VGLPFIKGYR
SSEPRSPAQM RLNFDD
//
