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Database: UniProt
Entry: A0A0A2LLP8_PENIT
LinkDB: A0A0A2LLP8_PENIT
Original site: A0A0A2LLP8_PENIT 
ID   A0A0A2LLP8_PENIT        Unreviewed;       513 AA.
AC   A0A0A2LLP8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Manganese/iron superoxide dismutase, C-terminal {ECO:0000313|EMBL:KGO77320.1};
GN   ORFNames=PITC_092800 {ECO:0000313|EMBL:KGO77320.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO77320.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO77320.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO77320.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO77320.1}.
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DR   EMBL; JQGA01000203; KGO77320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2LLP8; -.
DR   STRING; 40296.A0A0A2LLP8; -.
DR   HOGENOM; CLU_531094_0_0_1; -.
DR   OrthoDB; 2055478at2759; -.
DR   PhylomeDB; A0A0A2LLP8; -.
DR   Proteomes; UP000030104; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT   DOMAIN          437..487
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   REGION          39..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  56658 MW;  B35FD4570316DF3E CRC64;
     MHNIAPEEER WDQLGPDLPS CISHSSFRVR RKQKVIKRAA TAPKTAPGKK PAAMAPTGKD
     GHDVDVFEHA VGVADFSDEG DATAVMVARG VVEVVAIVDD DALLIEVLDT DDVAVLVEEL
     GADNDDVLGT SVALAGVAKR AARIAAFGKT VAQARCLDNT LGVDPVGHEE EHASELLERR
     SKELYACPGR MLAIRVKSNR TNGRDLVILV VLPLVMFNRF ARPQSALRAA SSFSPKPTSA
     FSRFQTRALH RIPQLQHDAH YKEHGVPEFL SPEAFDFSWT QYQTLLVNKL NLLTQDTVDA
     DAKPGELLVK YSKRPEMASV FNYASMAHNN HFFFNCLSPT ATTVPEKFAK DIVDTCSSVE
     SLKLDFLATA SSMFGPGFVW LAKNLEREGM MHIFCTYSAG SPYPAAHSRR QPVDMATHTP
     ETQLGNQFAG SMGAHAQNQK SLAPGAVDVQ PILCVNTWEH AWMMDYGIAG KDEYLERWWD
     RINWDVVFDN YNAVGSMKNS RSSINRHRSM SML
//
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