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TM10C_BOVIN
ID   TM10C_BOVIN             Reviewed;         426 AA.
AC   Q2KI45;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=tRNA methyltransferase 10 homolog C {ECO:0000305};
DE   AltName: Full=Mitochondrial ribonuclease P protein 1 {ECO:0000250|UniProtKB:Q7L0Y3};
DE            Short=Mitochondrial RNase P protein 1 {ECO:0000250|UniProtKB:Q7L0Y3};
DE   AltName: Full=RNA (guanine-9-)-methyltransferase domain-containing protein 1 {ECO:0000250|UniProtKB:Q7L0Y3};
DE   AltName: Full=mRNA methyladenosine-N(1)-methyltransferase {ECO:0000250|UniProtKB:Q7L0Y3};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q7L0Y3};
DE   AltName: Full=tRNA (adenine(9)-N(1))-methyltransferase {ECO:0000250|UniProtKB:Q7L0Y3};
DE            EC=2.1.1.218 {ECO:0000250|UniProtKB:Q7L0Y3};
DE   AltName: Full=tRNA (guanine(9)-N(1))-methyltransferase {ECO:0000250|UniProtKB:Q7L0Y3};
DE            EC=2.1.1.221 {ECO:0000250|UniProtKB:Q7L0Y3};
DE   Flags: Precursor;
GN   Name=TRMT10C {ECO:0000250|UniProtKB:Q7L0Y3};
GN   Synonyms=MRPP1 {ECO:0000250|UniProtKB:Q7L0Y3},
GN   RG9MTD1 {ECO:0000250|UniProtKB:Q7L0Y3};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mitochondrial tRNA N(1)-methyltransferase involved in
CC       mitochondrial tRNA maturation. Component of mitochondrial ribonuclease
CC       P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3,
CC       which cleaves tRNA molecules in their 5'-ends. Together with
CC       HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P,
CC       named MRPP1-MRPP2 subcomplex, which displays functions that are
CC       independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex
CC       catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at
CC       position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting
CC       as the catalytic N(1)-methyltransferase subunit. The MRPP1-MRPP2
CC       subcomplex also acts as a tRNA maturation platform: following 5'-end
CC       cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2
CC       subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2,
CC       retains the tRNA product after ELAC2 processing and presents the
CC       nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1
CC       enzyme. In addition to tRNA N(1)-methyltransferase activity,
CC       TRMT10C/MRPP1 also acts as a mRNA N(1)-methyltransferase by mediating
CC       methylation of adenosine residues at the N(1) position of MT-ND5 mRNA.
CC       Associates with mitochondrial DNA complexes at the nucleoids to
CC       initiate RNA processing and ribosome assembly.
CC       {ECO:0000250|UniProtKB:Q7L0Y3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43148, Rhea:RHEA-COMP:10363, Rhea:RHEA-COMP:10364,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.218;
CC         Evidence={ECO:0000250|UniProtKB:Q7L0Y3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC         Evidence={ECO:0000250|UniProtKB:Q7L0Y3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(1)-
CC         methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:55392, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12415,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74491;
CC         Evidence={ECO:0000250|UniProtKB:Q7L0Y3};
CC   -!- SUBUNIT: Component of mitochondrial ribonuclease P, a complex composed
CC       of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3. Interacts with
CC       HSD17B10/MRPP2; forming the MRPP1-MRPP2 subcomplex of the mitochondrial
CC       ribonuclease P complex. Interacts with GRSF1.
CC       {ECO:0000250|UniProtKB:Q7L0Y3}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC       {ECO:0000250|UniProtKB:Q7L0Y3}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI12775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC112774; AAI12775.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001039788.1; NM_001046323.2.
DR   RefSeq; XP_005201287.1; XM_005201230.3.
DR   RefSeq; XP_005201288.1; XM_005201231.3.
DR   RefSeq; XP_005201289.1; XM_005201232.3.
DR   AlphaFoldDB; Q2KI45; -.
DR   SMR; Q2KI45; -.
DR   STRING; 9913.ENSBTAP00000033017; -.
DR   PaxDb; Q2KI45; -.
DR   PRIDE; Q2KI45; -.
DR   GeneID; 532418; -.
DR   KEGG; bta:532418; -.
DR   CTD; 54931; -.
DR   eggNOG; KOG2967; Eukaryota.
DR   HOGENOM; CLU_034384_3_1_1; -.
DR   InParanoid; Q2KI45; -.
DR   OrthoDB; 1569668at2759; -.
DR   TreeFam; TF319795; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0061953; F:mRNA (adenine-N1-)-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR   GO; GO:0000964; P:mitochondrial RNA 5'-end processing; ISS:UniProtKB.
DR   GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; ISS:UniProtKB.
DR   GO; GO:0090646; P:mitochondrial tRNA processing; ISS:UniProtKB.
DR   GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR   GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR   Gene3D; 3.40.1280.30; -; 1.
DR   InterPro; IPR028564; MT_TRM10-typ.
DR   InterPro; IPR038459; MT_TRM10-typ_sf.
DR   InterPro; IPR025812; TRM10C.
DR   InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR   InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR   PANTHER; PTHR13563; PTHR13563; 1.
DR   PANTHER; PTHR13563:SF5; PTHR13563:SF5; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   PROSITE; PS51675; SAM_MT_TRM10; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Methyltransferase; Mitochondrion; Mitochondrion nucleoid;
KW   Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW   Transit peptide; tRNA processing.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..426
FT                   /note="tRNA methyltransferase 10 homolog C"
FT                   /id="PRO_0000311308"
FT   DOMAIN          193..385
FT                   /note="SAM-dependent MTase TRM10-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT   COILED          138..166
FT                   /evidence="ECO:0000255"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UFY8"
SQ   SEQUENCE   426 AA;  49785 MW;  120F0F431992C822 CRC64;
     MPVLLKMSVS ITFLRPFARV LVPFTLHRKR RVLYSTIMQR YMSSKIPAAS YPNKESTPPS
     EELELDRWKI TMKSSVQEED VSTATSSEDE DPLAATRELV EMWRLLGKEV PEHFSEEELK
     TLMECVSKSS KRKYLKYLYI KEKMKKARQI KKEMKKAEKE EPKKDQLPET IKEDKQQNFL
     FLRLWDRNMD IAMGWKGAQA MQFGQPLVFD MAYDDHMKPK ELQNAVSQLL ESEGCNRRNV
     DPFHIYFCNL KTGGAYYKEL VKRYGEKWNK LLLTATEKSH VDLFPKDSII YLTADSPNVM
     TTFKHDKIYI VGSFVDKNMQ PGTSLAKAKR LKLATECLPL DKYLQWDTGT KNLTLDQMMR
     ILLCLKNTGS WEEALKFVPS RKHAGYLEIS QHSQEFLNRM KKSKTFNSFP RGSINRHRKS
     SLKENI
 
 
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