ID A0A369JM91_HYPMA Unreviewed; 383 AA.
AC A0A369JM91;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Putative 37S ribosomal protein S26A, mitochondrial {ECO:0000313|EMBL:RDB20524.1};
GN ORFNames=Hypma_012429 {ECO:0000313|EMBL:RDB20524.1};
OS Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB20524.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB20524.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB20524.1,
RC ECO:0000313|Proteomes:UP000076154};
RA Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA Jeong J., Song E.-S.;
RT "Whole genome sequencing of Hypsizygus marmoreus.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC mitochondrial genome-encoded proteins, including at least some of the
CC essential transmembrane subunits of the mitochondrial respiratory
CC chain. The mitoribosomes are attached to the mitochondrial inner
CC membrane and translation products are cotranslationally integrated into
CC the membrane. {ECO:0000256|ARBA:ARBA00037226}.
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:RDB20524.1}.
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DR EMBL; LUEZ02000062; RDB20524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369JM91; -.
DR STRING; 39966.A0A369JM91; -.
DR InParanoid; A0A369JM91; -.
DR OrthoDB; 2055478at2759; -.
DR Proteomes; UP000076154; Unassembled WGS sequence.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:InterPro.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 2.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR Pfam; PF02777; Sod_Fe_C; 2.
DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076154};
KW Ribonucleoprotein {ECO:0000313|EMBL:RDB20524.1};
KW Ribosomal protein {ECO:0000313|EMBL:RDB20524.1}.
FT DOMAIN 133..179
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT DOMAIN 329..372
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT REGION 206..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 42213 MW; E12700C5657A6F7B CRC64;
MSSIGLRLAS SKVSRTSSAV SHLKSRWGTR NVHKRRALPY SIEDGLGEFL PPAALKTVAV
EYQEGLLQRL NEEVRGTPEQ NITVTQTVIN TAPHRDRALA FNYASLALNN SFFLDQLKPP
PKPELNHQAA ISTDLGSAIR MQHGSIAQLK SSFSAAATGM FTNGWVWFVV DQNGNTGVIP
TFGPGTLLIR SRTYMAHSKN LVLGEGLGQW DRGNPYNVNE QEAEEPFEED EEDEEDEEDE
ELITPPPRSP TAHAAPPGVN PSSPVSGVSG VNTPTPPSGL LPKFMHTSAR LSNSFDLEIG
QKMPSSLYEG DPEPRTAPMT KTDMLNLGET LYPLFCISVH EHAWMAAGYG VWGKEEWLKK
FWTVLDWRKV SQSYSKAVAQ RSL
//
