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Database: UniProt/TrEMBL
Entry: C4Y128_CLAL4
LinkDB: C4Y128_CLAL4
Original site: C4Y128_CLAL4 
ID   C4Y128_CLAL4            Unreviewed;       250 AA.
AC   C4Y128;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Manganese/iron superoxide dismutase C-terminal domain-containing protein {ECO:0000259|Pfam:PF02777};
GN   ORFNames=CLUG_01910 {ECO:0000313|EMBL:EEQ37787.1};
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ37787.1, ECO:0000313|Proteomes:UP000007703};
RN   [1] {ECO:0000313|EMBL:EEQ37787.1, ECO:0000313|Proteomes:UP000007703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ37787.1,
RC   ECO:0000313|Proteomes:UP000007703};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408077; EEQ37787.1; -; Genomic_DNA.
DR   RefSeq; XP_002618451.1; XM_002618405.1.
DR   AlphaFoldDB; C4Y128; -.
DR   STRING; 306902.C4Y128; -.
DR   GeneID; 8499459; -.
DR   KEGG; clu:CLUG_01910; -.
DR   VEuPathDB; FungiDB:CLUG_01910; -.
DR   HOGENOM; CLU_057349_1_1_1; -.
DR   InParanoid; C4Y128; -.
DR   OMA; ASMAFNN; -.
DR   OrthoDB; 2055478at2759; -.
DR   Proteomes; UP000007703; 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; 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:UP000007703}.
FT   DOMAIN          122..175
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   DOMAIN          196..246
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
SQ   SEQUENCE   250 AA;  28784 MW;  94126032CDA09C50 CRC64;
     MFSTRLISSR RLLHSVPKLK NAAEFTEKGI AGLYSPQGFR TAWLDYQKYL TAQLSLRTVG
     TENETRTPYQ ILLSTAKQTT QQHTFHYASQ AHNNHFFFEQ LSDKETAQKT KPSRFLMERL
     ADQNITSLEE LRTAVNSRAN SVLGQGWVFL VEKEDKSVEL ITCHNDGTPY YWGKRQALDL
     NGAVDEASFD ALEAAKNAAH QLDFTLPLLA INFWDVAYYE DYGITGRAEY LDHVWDCINW
     DVVNRRMFQI
//
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