ID A0A1V6V981_9EURO Unreviewed; 827 AA.
AC A0A1V6V981;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=37S ribosomal protein Rsm22 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENCOP_c001G02632 {ECO:0000313|EMBL:OQE47235.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE47235.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE47235.1}.
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DR EMBL; MDDG01000001; OQE47235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6V981; -.
DR STRING; 36646.A0A1V6V981; -.
DR OrthoDB; 146346at2759; -.
DR Proteomes; UP000191500; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR InterPro; IPR015324; Ribosomal_Rsm22-like.
DR PANTHER; PTHR13184; 37S RIBOSOMAL PROTEIN S22; 1.
DR PANTHER; PTHR13184:SF5; METHYLTRANSFERASE LIKE; 1.
DR Pfam; PF09243; Rsm22; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT REGION 42..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..789
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..817
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 93034 MW; 0FAA1312DA02170B CRC64;
MLSRSSASGA SRSQSRELFR TFACPAGSRQ LRGPVNRLTS THQRTLVQKA SPLIASSSPT
HRRNTSDYAV SQCQPQRRFV SGPASADSPK QPSQPIKPDH INTLIDRIGE NEAQMAQILG
ELEIMGEEGG ADELIDLIDQ RDEHTPESWV HMIKQRFGDE IPEGLLDDAE LQIYARLYGE
PIIRQEVELM VEEEEEDMSL LREDGKGGWE EVDLEESAAE DEIQLVYDMD IPPEERETLA
MQRTREVAEQ LGGEIMLEEF ENEAVPDSAP RMHPLTLEGK FGTDPTTIHL PKDTVTGPIS
VILSEFSNKH ISETARRLFG GPGLPHSSTT APPRAQLPQL PVALNASQRQ MGEMEANAYL
AALYPGIFAS TLSVMVEIRK RLGVDWIRRL IAQDGGPNVL DASGGGAGIL AWRDIIRAEW
ELMVPDHPSG APIPFGRSTV LTGSDALRQR ASVLLDNTTF LPRLPDYVHV REKPTIDDSR
KAPKRKQYDI IIAPHSLLGL EEEYERKQHV ENLWSLLNPN GGILILLEKG RQKGFEAISG
AREMLLKRHI ASPGSTEYDN FLEDPDQREV IEKERGMIVA PCTNHSTCPM HNSSGATKGR
RDFCHFEQRY IRPPFLQRIM GAKDRNHEDL KFSYLAVQRG VDLRQDQAIR QDSEATDAAF
EGFEDPDDSD IPNKPAFRAL SLPRAIYPPM KRRGHVIFDL CTPAGKIERW TVPRSYSRQA
YRDARKSHWG DLWALGAKTR IPRNLNLGDK HGEGKKERLA RRAATKASEE EGDFENEGEE
EDEEYELHDS DVPDVPVKKR GQHIPSWKKH NDKKKIRQAS NKRSADE
//
