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Database: UniProt
Entry: A0A2V1AM72_9ASCO
LinkDB: A0A2V1AM72_9ASCO
Original site: A0A2V1AM72_9ASCO 
ID   A0A2V1AM72_9ASCO        Unreviewed;       454 AA.
AC   A0A2V1AM72;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=UPF0020 domain-containing protein {ECO:0000259|Pfam:PF01170};
GN   ORFNames=CXQ85_003227 {ECO:0000313|EMBL:PVH19387.1};
OS   [Candida] haemuloni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH19387.1, ECO:0000313|Proteomes:UP000244309};
RN   [1] {ECO:0000313|EMBL:PVH19387.1, ECO:0000313|Proteomes:UP000244309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B11899 {ECO:0000313|EMBL:PVH19387.1,
RC   ECO:0000313|Proteomes:UP000244309};
RA   Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA   Litvintseva A.P.;
RT   "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT   Patient with Chronic Leg Ulcers in Israel.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic subunit of an S-adenosyl-L-methionine-dependent
CC       tRNA methyltransferase complex that mediates the methylation of the
CC       guanosine nucleotide at position 10 (m2G10) in tRNAs.
CC       {ECO:0000256|ARBA:ARBA00002425}.
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:PVH19387.1}.
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DR   EMBL; PKFO01000002; PVH19387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1AM72; -.
DR   STRING; 45357.A0A2V1AM72; -.
DR   EnsemblFungi; CXQ85_003227-t46_1; CXQ85_003227-t46_1-p1; CXQ85_003227.
DR   VEuPathDB; FungiDB:CXQ85_003227; -.
DR   OrthoDB; 5488599at2759; -.
DR   Proteomes; UP000244309; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR000241; RlmKL-like_Mtase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016691; tRNA_mtfrase_TRM11.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   PANTHER; PTHR13370:SF3; TRNA (GUANINE(10)-N2)-METHYLTRANSFERASE HOMOLOG; 1.
DR   Pfam; PF01170; UPF0020; 1.
DR   PIRSF; PIRSF017259; tRNA_mtfrase_TRM11; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
DR   PROSITE; PS51627; SAM_MT_TRM11; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244309};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022555};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          183..298
FT                   /note="UPF0020"
FT                   /evidence="ECO:0000259|Pfam:PF01170"
SQ   SEQUENCE   454 AA;  52012 MW;  B13A806AB881D677 CRC64;
     MKDYIISFAQ AFPNFRIAEL ESLAELNGIE VDFQNHNEKK PFLKVQLEDD EQAKKLIKRS
     ILAKGIYELW GEGKDLTELH ESIQKNSSDK FDTYKRNTFR FDFVSFMGAK TTEEKIQTID
     SFKYLGFEGK IRLKNPEVIF AVLEEYFVSG QERAEKPDYL WFGRQVETSA RSEGVVEQYD
     LKKRKYIGTT SFDAELALVS CNIAQVKPGK VVYDPFTGTG SFLVAGAYFG GYPMGTDIDA
     RSVRGKGPNN NLLSSFRQYG TASQFIDIWT MDFTNNALRE DFVIDTIVCD PPYGVREGLK
     VCGAKDPAKA AGREHNVVDG ELGFKRRDFI APKKPYHLAN LLDDLLEFSA ARMPVGGRLA
     FWMPTANDEF VEHHIPQHER LELLYVLEQE FNKWSRRLVV YVKRDESYKG KTYNGMRSEQ
     VTHFRDRYFK SFNERSKQTV SSQLGDLRIS GSGP
//
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