ID G7E203_MIXOS Unreviewed; 873 AA.
AC G7E203;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6 {ECO:0000256|ARBA:ARBA00021704};
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM6 {ECO:0000256|ARBA:ARBA00032319};
GN Name=Mo03513 {ECO:0000313|EMBL:GAA96840.1};
GN ORFNames=E5Q_03513 {ECO:0000313|EMBL:GAA96840.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA96840.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(2011).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TRM6/GCD10 family.
CC {ECO:0000256|ARBA:ARBA00008320}.
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:GAA96840.1}.
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DR EMBL; BABT02000108; GAA96840.1; -; Genomic_DNA.
DR RefSeq; XP_014567303.1; XM_014711817.1.
DR AlphaFoldDB; G7E203; -.
DR STRING; 764103.G7E203; -.
DR GeneID; 26268816; -.
DR eggNOG; KOG0053; Eukaryota.
DR eggNOG; KOG1416; Eukaryota.
DR HOGENOM; CLU_329018_0_0_1; -.
DR InParanoid; G7E203; -.
DR OrthoDB; 5482552at2759; -.
DR Proteomes; UP000009131; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR GO; GO:0030488; P:tRNA methylation; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR017423; TRM6.
DR PANTHER; PTHR12945; TRANSLATION INITIATION FACTOR EIF3-RELATED; 1.
DR PANTHER; PTHR12945:SF0; TRNA (ADENINE(58)-N(1))-METHYLTRANSFERASE NON-CATALYTIC SUBUNIT TRM6; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR Pfam; PF04189; Gcd10p; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000009131}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 96305 MW; 480FADDA7CBEF114 CRC64;
MDLSTRLLHA DDEHPRPNEA GVYTASELNG PVAPSISVST TFRWPGPLQP PLPEGDIDPS
ASNPLVYSRY STPSSERVEK VLDSLMGART VLYSSGLAAS FAAMLWANPT VIAIREGYHG
SHMAIDVFKR IKSNLILIDL DDFDAYTNET LCWLETPLNP TGEARDMAHY AKHCKAKGAK
LLVDSTFAPP PLQDPFRHGA DIVMHSATKY LNGHSDALLG VLAVKSQSDW ERLWSDRTFT
GPMPGSLECW LLLRSLRTLS LRVKRQAKTA TGLAHWLNTL TQDKASLVNQ VWHASLQAKQ
GQFDAFAAQQ LTGGPACFSI LLSSAEVAKW LPYTVKLFAP ATSLGGVESL MEHRITSDAK
ADPKLVRISV GLEDLEDLKA DILTALNEFN TTLDEVKPST SESDAQTIVP VKRPATDASD
VANASEAKKF KSTGKGKQPA IEPYRAEHRI IRAGEPFLIS LPSGLSKLIP KLSSGVSINL
GKYGQFKSDD LIGRPYGFTY EITHGGSLTV VQHVTLSEIE ERERENTNED IMPQTYVGLS
AEQVAELRAA DMTGKEIVDY QIAVHAEFDK KNRFSQEKYR RRKETKYLKM FTPVAPTLYN
ICAYHFVKDP PRFRDLRVDS MAQILNLADV RPHKRVLLID DTAGALAAGC VERMDGHGAL
VLIHDASSDI QLPVCDYMGF SVRQKSVICQ INWAATDPTH QPFELPTDVD IKKDTRDRGR
QKAVKRQAQY EANAQMRQQF FDGGFGCVII ATAYDPLDVL SRVSDKLAGS AQVVIYSPSL
EPLASASRLL RGDPQFIGIG VHQPFLRKYQ VLPGRTHPEM TGLPAGGYIL TAISVLAKRK
DENGTRKSTP EQIQEIGQNA AREQDAMQDK MQS
//
