ID A0A498HD28_MALDO Unreviewed; 622 AA.
AC A0A498HD28;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=type II protein arginine methyltransferase {ECO:0000256|ARBA:ARBA00011935};
DE EC=2.1.1.320 {ECO:0000256|ARBA:ARBA00011935};
GN ORFNames=DVH24_037152 {ECO:0000313|EMBL:RXH69368.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH69368.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH69368.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH69368.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC Evidence={ECO:0000256|ARBA:ARBA00000778};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the NDUFAF7 family.
CC {ECO:0000256|ARBA:ARBA00005891}.
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:RXH69368.1}.
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DR EMBL; RDQH01000343; RXH69368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498HD28; -.
DR STRING; 3750.A0A498HD28; -.
DR Proteomes; UP000290289; Chromosome 17.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:EnsemblPlants.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:EnsemblPlants.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.50.12710; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003788; NDUFAF7.
DR InterPro; IPR038375; NDUFAF7_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12049:SF7; PROTEIN ARGININE METHYLTRANSFERASE NDUFAF7, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12049; UNCHARACTERIZED; 1.
DR Pfam; PF02636; Methyltransf_28; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 497..621
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 33..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 68575 MW; EDA2A4D8F70BA711 CRC64;
MLRRFLLQAS AARRRLPNSH FPPSYSAPLI PNRSVSSTSY SSSSQIPHSP FVEQLDDNPD
QTTQPTASIA VDRSGLYNPP EHSHEPTSDS ELVKHLKGII KFRGGPISVA EYMEEVLTNP
KAGFYMNRDV FGAGGDFITS PEVSQMFGEM VGVWAISLWE QMGQPDRVNL VELGPGRGTL
MADLLHGASK FKNFTESLHV HMVECSPTLQ KLQHQKLECV DEEVSDGKRT VSALAKTPVS
WHATLEDVPT GLPSIIIAHE FYDALPVHQF QKAARGWSEK MIDVAEDSTF RFVLSSQPTP
ATLYLAKRCK WAGNEEIAKL QHIEVCPKAM ELTQTIAERV ASDGGGALII DYGLNGVVSD
SLQAIRKHQF VNILDDPGSA DLSAYVDFAS IRHSAEEISG EVSVHGPITQ SQFLGSLGIN
FRAEALTQNC TEEQFESLRN GYWQLVGKGE APFWEGPDEK APIGMGTRYL AMAIVNRKQE
ISIDRERERM GSFLSSFIGG APADDSAAPG EEPGVTSFHS SARWQLHLNS HKESSQLLVI
DFSASWCGPC RFIEPAIHAM AAKFTDVQFA KIDVDELSEV AQEFGVQGMP TFVLLKKGKE
VDRVIGAKKD ELEKKVEKYR SL
//
