ID A0A1Q7VVY8_9CYAN Unreviewed; 313 AA.
AC A0A1Q7VVY8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
DE Flags: Fragment;
GN ORFNames=AUI36_33820 {ECO:0000313|EMBL:OLE22681.1};
OS Cyanobacteria bacterium 13_1_40CM_2_61_4.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1805101 {ECO:0000313|EMBL:OLE22681.1, ECO:0000313|Proteomes:UP000186010};
RN [1] {ECO:0000313|EMBL:OLE22681.1, ECO:0000313|Proteomes:UP000186010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE22681.1}.
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DR EMBL; MNHI01004438; OLE22681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7VVY8; -.
DR Proteomes; UP000186010; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:InterPro.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR CDD; cd01444; GlpE_ST; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR InterPro; IPR023695; Thiosulf_sulfurTrfase.
DR PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR SMART; SM00450; RHOD; 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 SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
FT DOMAIN 224..313
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT NON_TER 313
FT /evidence="ECO:0000313|EMBL:OLE22681.1"
SQ SEQUENCE 313 AA; 34764 MW; 0DF41535C1419FAE CRC64;
MQQEITPIAV RPWTLNGISE RMLVSHYENN YGGGVRTLNA VRADLAALDA GAPGYRLRAL
KREELTAMGS VTLHELYFGN LGGEGNKVPD QARTILEEHF GSVAAWRREF VGTARSLAGG
SGWVLLTYSR RQRRFWNQVA ANHTQAAVDA APVLVLDMYE HAYHMDFGAN ATAYIDAFMR
NIEWAAVIHR MDAVRADRSL PLEDPSDKAL PSRSVEELAA QLAKGEPVQV LDARPRHHIS
RTVDLMEGAI WRDPDRVDEW IGELAVDRPV AVYCAYGFHV GCSVTKTLRE RGFDARYIRG
GISAWYATGG SRA
//
