ID M7X136_RHOT1 Unreviewed; 340 AA.
AC M7X136;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Superoxide dismutase, Fe-Mn family {ECO:0000313|EMBL:EMS23795.1};
GN ORFNames=RHTO_06854 {ECO:0000313|EMBL:EMS23795.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS23795.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS23795.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS23795.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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}.
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DR EMBL; KB722646; EMS23795.1; -; Genomic_DNA.
DR RefSeq; XP_016274914.1; XM_016420513.1.
DR AlphaFoldDB; M7X136; -.
DR GeneID; 27370867; -.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_057349_2_0_1; -.
DR OrthoDB; 2055478at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
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; 1.
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; 1.
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;
FT DOMAIN 278..328
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT REGION 207..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 36561 MW; F8448FCC77929E0F CRC64;
MASIRTLPSF SRQLARSRSP AVASFLPSQR RLVHHRVPPA FDVEKGLRPF LGPENLRTVA
VDWQDGVLAR LNELTRGTEY ENMSVLQTLK QSAMNPAHAL IFNYASEALN NSFFLSNLPT
PNSNFSQQIA ATASLGSFPA LISHFSAHVS GLHPSSGAYV WLVTDPHGNL GVVGTYAGGT
VLVRERAQMG PGGYASKDLR VLGEKVEVKD GEAPPVPAGE TASAAGGAAT TGAAAAAGSA
WQTVQPGSQR QASQTPVGDS LLKDGALDPS KILFGAKQHH ASSIGQSIHP LVCISTHPHC
YFEDYGLWGR DEYVQKWWGA VDWHKVEQAY DQFRIKQQGI
//
