ID A0A5C5G8B0_9BASI Unreviewed; 794 AA.
AC A0A5C5G8B0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Large ribosomal subunit protein eL42 {ECO:0000256|ARBA:ARBA00035236};
DE AltName: Full=60S ribosomal protein L41 {ECO:0000256|ARBA:ARBA00029633};
DE AltName: Full=60S ribosomal protein L44 {ECO:0000256|ARBA:ARBA00035340};
GN ORFNames=DMC30DRAFT_345221 {ECO:0000313|EMBL:TNY24644.1};
OS Rhodotorula diobovata.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5288 {ECO:0000313|EMBL:TNY24644.1, ECO:0000313|Proteomes:UP000311382};
RN [1] {ECO:0000313|EMBL:TNY24644.1, ECO:0000313|Proteomes:UP000311382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-FST 08-225 {ECO:0000313|EMBL:TNY24644.1,
RC ECO:0000313|Proteomes:UP000311382};
RA Fakankun I.U., Fristensky B., Levin D.B.;
RT "Rhodosporidium diobovatum UCD-FST 08-225 genome sequencing, assembly, and
RT annotation.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family.
CC {ECO:0000256|ARBA:ARBA00009364, ECO:0000256|RuleBase:RU000666}.
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:TNY24644.1}.
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DR EMBL; SOZI01000001; TNY24644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C5G8B0; -.
DR STRING; 5288.A0A5C5G8B0; -.
DR Proteomes; UP000311382; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR Gene3D; 3.10.450.80; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000552; Ribosomal_eL44.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025795; tRNA_(uracil-5-)_MeTrfase.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF00935; Ribosomal_L44; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR PROSITE; PS01172; RIBOSOMAL_L44E; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS51622; SAM_MT_RNA_M5U_2; 1.
DR PROSITE; PS01230; TRMA_1; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000311382};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU000666};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU000666};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01024}.
FT REGION 148..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 737
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 737
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 607
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 639
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 660
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 710
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 794 AA; 87520 MW; 8EC1861A605B0F65 CRC64;
MVNVPKTRRT YCKGKQCRKH TPHKVTQYKT GKASLFAQGK RRYDRKQSGY GGQTKPVFHK
KAKTTKKVVL RLECTVCKYK MQMSLKRCKH FELGGDKKQK GQALQDGRRA VGLSWAPRRM
LVRAARSLVC FPRPLQLQLQ LSRAARPAMS APAPAAPPKR PLSTSPPPAA AAPPAAPAAA
ADHPDSKRVK LAVEDPVSVP PVLVEQPVPP SASATASASE PAPAAAAAVP SKAKQPRKPR
QRKGKAPKPG GAEEAGAFDV IALLGQERVD ELRRLQEDEA RDWVAEAERE WGRGAEGKDL
EVEVVGWTDH GDGLALLTPS GPGSDGKPTR LVSIPFALQG ERVRIHVHRH EPDYFMSHAD
LLDILEPSPR RQADVSELPG RVLDDKTRSR LDAVRAKFGN RVQCQYFGEC SGCQYQPLAY
DEQLEMKREV VRRAFANFSG LDPSLVPAVG PTLPSPLEYG YRTKLTPHFQ VPPSKNPNRN
RRKPKGGAAQ DQPPQGEDKE WEVTIGFEQK GRKRIVDIEE CVIATGVINR AMVGERAKVK
ADISAYKRGA TILLRDSLPP RPEGTDVRPP CYSPSSEEHI CVTDHHETVR EQVGEVEFLQ
KAGSFFQNNA SILPSLMDAV KAAIGPKPAD SKRYLVDAYC GSGLFAISLA DLFDRVEGIE
IDKASIVWAR KNALYNHAEG RGEVGFRDGK AEDIFGSIEF PRDQTTVLID PPRKGCDDAF
LRQLLALNPA TVIYVSCNVR SQARDIGWLL EHSRRDEDKS GSGKRGYWIE SLRAADLFAQ
THHAEGVAIL RREV
//
