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Database: UniProt
Entry: E3ECK9_PAEPS
LinkDB: E3ECK9_PAEPS
Original site: E3ECK9_PAEPS 
ID   E3ECK9_PAEPS            Unreviewed;       459 AA.
AC   E3ECK9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN   Name=sodF {ECO:0000313|EMBL:ADO54781.1};
GN   ORFNames=PPSC2_03965 {ECO:0000313|EMBL:ADO54781.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO54781.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO54781.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO54781.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(2011).
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714}.
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DR   EMBL; CP002213; ADO54781.1; -; Genomic_DNA.
DR   RefSeq; WP_013369417.1; NC_014622.2.
DR   AlphaFoldDB; E3ECK9; -.
DR   STRING; 1406.LK13_16770; -.
DR   KEGG; ppm:PPSC2_03965; -.
DR   PATRIC; fig|886882.15.peg.788; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_5_2_9; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000006868; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   Gene3D; 1.20.1260.120; Protein of unknown function DUF2935; 1.
DR   InterPro; IPR021328; CotB-like.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR   Pfam; PF11155; DUF2935; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF158430; Bacillus cereus metalloprotein-like; 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.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT   DOMAIN          258..338
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          345..447
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   REGION          74..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   459 AA;  52143 MW;  62F32FC3129246EC CRC64;
     MLSTYGSFLP LRVLEEIRHW KQQESWHVEV IKSATEGLEP AYVRLLDDWR TVFEQTERAA
     IELLEEQRSA LDPVEQAWQH QEKKASSAPQ AHTHQLDESS AHSRGSDASA TGEKPLSESG
     LNSQPASQEL NRRLDDLLQT ANRQSQEYVR QLGLLTEHSH ALRQQPKSAG VVIHAAHESQ
     YFLISTTPFQ EPGSIARATG LYHVAAEGED YPEQAFRERH ASMRGEGSGA TKGVQSGQTQ
     PSAAEKSLVG RPVPIGGHRL PPLPYPYNAL EPYIDEKTMR IHHNKHHLSY VNDLNKAEKK
     LEEARKTGDF DLVKHWEREL AFNGAGHYLH TLFWTIMSPQ GGGNPSGPLA EQIKKDFGSY
     DAFKKQFSSA AEKVEGGGWA ILVWSPRSGR LEILQAEKHQ NLTQWESIPL LAIDVWEHAY
     YLKHQAERNK YIEDWWHVVN WPEVEARYAQ ASKLRWQPF
//
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