ID S7ZE25_PENO1 Unreviewed; 411 AA.
AC S7ZE25;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=tRNA (guanine(9)-N1)-methyltransferase {ECO:0000256|ARBA:ARBA00020451};
DE EC=2.1.1.221 {ECO:0000256|ARBA:ARBA00012797};
DE AltName: Full=tRNA methyltransferase 10 {ECO:0000256|ARBA:ARBA00032166};
DE AltName: Full=tRNA(m1G9)-methyltransferase {ECO:0000256|ARBA:ARBA00031792};
GN ORFNames=PDE_01876 {ECO:0000313|EMBL:EPS26936.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS26936.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS26936.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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:0000256|ARBA:ARBA00000855};
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DR EMBL; KB644409; EPS26936.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZE25; -.
DR STRING; 933388.S7ZE25; -.
DR eggNOG; KOG2967; Eukaryota.
DR HOGENOM; CLU_034384_0_0_1; -.
DR OrthoDB; 2908056at2759; -.
DR PhylomeDB; S7ZE25; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0052905; F:tRNA (guanosine(9)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd18089; SPOUT_Trm10-like; 1.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; TRNA (GUANINE-9-) METHYLTRANSFERASE; 1.
DR PANTHER; PTHR13563:SF13; TRNA METHYLTRANSFERASE 10 HOMOLOG A; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 144..361
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000259|PROSITE:PS51675"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 46114 MW; CEC173FDE0296213 CRC64;
MDEEERPRKV AKLEHSEASI ETELGPAMTG AVPIVDEPSQ ATSSNAQPEQ SQLTLSNETS
GLPIQSSEGT AQENDQDSAP KLSKNQLRKL RKRELWEAGR EQRKEKRKEQ MARKKERRQR
MVDEAREAGG EEAVQALRKQ WETTRSKSKR STLLPLSIVI DCGYDDLMNP HERISLAGQL
TRSYSENSRA MWRSHLMFSS FNKQLKERFD NVLSPYRNWK GIRIIQEDFV HAAEIAKEQM
TSPKGGKLVG PFADEADAKP EDGEVIYLSS DSDNVLTELK PYCTYIIGGL VDKNRHKAVC
YKSAVSKGLK TAKLPIGDYI QMTSRQVLTT NHVVDIMLKW LELGDWGEAF MQVLPPRKGG
KLKGQQGSDG AVDEASDDEP EAEQTLEEIA NQMEADAEID DENGHNSGPD L
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