ARMT1_MACFA
ID ARMT1_MACFA Reviewed; 441 AA.
AC Q4R526;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Damage-control phosphatase ARMT1 {ECO:0000250|UniProtKB:Q04371};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q04371};
DE AltName: Full=Acidic residue methyltransferase 1 {ECO:0000250|UniProtKB:Q9H993};
DE AltName: Full=Protein-glutamate O-methyltransferase {ECO:0000250|UniProtKB:Q9H993};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H993};
DE AltName: Full=Sugar phosphate phosphatase ARMT1 {ECO:0000250|UniProtKB:Q04371};
GN Name=ARMT1 {ECO:0000250|UniProtKB:Q9H993};
GN ORFNames=QflA-10880 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metal-dependent phosphatase that shows phosphatase activity
CC against several substrates, including fructose-1-phosphate and
CC fructose-6-phosphate (By similarity). Its preference for fructose-1-
CC phosphate, a strong glycating agent that causes DNA damage rather than
CC a canonical yeast metabolite, suggests a damage-control function in
CC hexose phosphate metabolism (By similarity). Has also been shown to
CC have O-methyltransferase activity that methylates glutamate residues of
CC target proteins to form gamma-glutamyl methyl ester residues (By
CC similarity). Possibly methylates PCNA, suggesting it is involved in the
CC DNA damage response (By similarity). {ECO:0000250|UniProtKB:Q04371,
CC ECO:0000250|UniProtKB:Q9H993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate;
CC Xref=Rhea:RHEA:35603, ChEBI:CHEBI:15377, ChEBI:CHEBI:37721,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:138881;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate +
CC dihydroxyacetone; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; Evidence={ECO:0000250|UniProtKB:Q9H993};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- DOMAIN: Subfamily III proteins have a conserved RTxK motif about 40-50
CC residues from the C-terminus; the threonine may be replaced by serine
CC or cysteine. {ECO:0000250|UniProtKB:Q04371}.
CC -!- PTM: Automethylated. {ECO:0000250|UniProtKB:Q9H993}.
CC -!- SIMILARITY: Belongs to the damage-control phosphatase family. Sugar
CC phosphate phosphatase III subfamily. {ECO:0000305}.
CC -!- CAUTION: Human C6orf211 has been reportedly associated with a protein
CC carboxyl methyltransferase activity, but whether this protein indeed
CC has such an activity remains to be determined (By similarity). It has
CC been later shown to belong to a family of metal-dependent phosphatases
CC implicated in metabolite damage-control (By similarity).
CC {ECO:0000250|UniProtKB:Q9H993}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE01799.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB169718; BAE01799.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q4R526; -.
DR SMR; Q4R526; -.
DR STRING; 9541.XP_005552206.1; -.
DR eggNOG; KOG3870; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0097023; F:fructose 6-phosphate aldolase activity; IEA:RHEA.
DR GO; GO:0103026; F:fructose-1-phosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051998; F:protein carboxyl O-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:RHEA.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; ISS:UniProtKB.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR InterPro; IPR036075; ARMT-1-like_metal-bd_sf.
DR InterPro; IPR039763; ARMT1.
DR InterPro; IPR002791; ARMT1-like_metal-bd.
DR PANTHER; PTHR12260; PTHR12260; 1.
DR Pfam; PF01937; ARMT1-like_dom; 1.
DR SUPFAM; SSF111321; SSF111321; 1.
PE 2: Evidence at transcript level;
KW Acetylation; DNA damage; Hydrolase; Manganese; Metal-binding;
KW Methyltransferase; Nickel; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT CHAIN 2..441
FT /note="Damage-control phosphatase ARMT1"
FT /id="PRO_0000230796"
FT MOTIF 401..404
FT /note="Subfamily III RTxK motif"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 253..254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT BINDING 291
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 291
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT BINDING 367..371
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
SQ SEQUENCE 441 AA; 51207 MW; 351482D6BA80C860 CRC64;
MAVVPASLSG QDVGSFAYLT IKDRIPQILT KVIDTLHRHK SEFFENHGEE GVEAEKKAIS
LLSKLRNELQ TDKPIIPLVE KFVDTDIWNQ YLEYQQSLLN ESDGKSRWFY SPWLFVECYM
YRRIHEAIIQ SPPIDYFDVF KESKEQNFYE SQESVIALCT HLQQLIKTIE DLDENQLKDE
FFKLLQISLW GNKCDLSLSG GESSSQKTDV LNSLEDLKPF ILLNDMEHLW SLLSNCKKTR
EKASVTRVYI VLDNSGFELV TDLILANFLL SSELATEVHF YGKTIPWFVS DTTIHDFNWL
IEQVKHGNHK WMSKCGADWE EYVKMGKWVY HDHIFWTLPH EYCAMPQVAP DLYAELQKAH
LILFKGDLNY RKLTGDRKWE FSVPFHQALN GFHPAPLCTI RTLKAEIQVG LKPGQGEQLM
ASEPCWWTSG KYGIFQYDGP L
