ID G9KR99_MUSPF Unreviewed; 90 AA. AC G9KR99; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-DEC-2022, entry version 34. DE RecName: Full=sulfiredoxin {ECO:0000256|ARBA:ARBA00013055}; DE EC=1.8.98.2 {ECO:0000256|ARBA:ARBA00013055}; DE Flags: Fragment; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae; OC Mustela. OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES07428.1}; RN [1] {ECO:0000313|EMBL:AES07428.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lungs {ECO:0000313|EMBL:AES07428.1}; RX PubMed=23236062; DOI=10.1128/JVI.02476-12; RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F., RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M., RA Farooqui A., Kelvin D.J.; RT "Sequencing, annotation, and characterization of the influenza ferret RT infectome."; RL J. Virol. 87:1957-1966(2013). CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-dithiol + ATP + S-hydroxy-S-oxy-L-cysteinyl- CC [peroxiredoxin] = [protein]-disulfide + ADP + phosphate + S-hydroxy- CC L-cysteinyl-[peroxiredoxin]; Xref=Rhea:RHEA:17545, Rhea:RHEA- CC COMP:10593, Rhea:RHEA-COMP:10594, Rhea:RHEA-COMP:13681, Rhea:RHEA- CC COMP:17976, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:50058, ChEBI:CHEBI:61973, ChEBI:CHEBI:61974, CC ChEBI:CHEBI:456216; EC=1.8.98.2; CC Evidence={ECO:0000256|ARBA:ARBA00034024}; CC -!- SIMILARITY: Belongs to the sulfiredoxin family. CC {ECO:0000256|ARBA:ARBA00009609}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JP018830; AES07428.1; -; mRNA. DR AlphaFoldDB; G9KR99; -. DR HOGENOM; CLU_124532_1_0_1; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0032542; F:sulfiredoxin activity; IEA:UniProtKB-EC. DR InterPro; IPR003115; ParB/Sulfiredoxin_dom. DR InterPro; IPR036086; ParB/Sulfiredoxin_sf. DR InterPro; IPR016692; Sulfiredoxin. DR PANTHER; PTHR21348; UNCHARACTERIZED; 1. DR Pfam; PF02195; ParBc; 1. DR PIRSF; PIRSF017267; Sulfiredoxin; 1. DR SUPFAM; SSF110849; ParB/Sulfiredoxin; 1. PE 2: Evidence at transcript level; KW Antioxidant {ECO:0000256|ARBA:ARBA00022862}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR017267- KW 1}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR017267-2}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRSR:PIRSR017267-1}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. FT DOMAIN 6..84 FT /note="ParB" FT /evidence="ECO:0000259|Pfam:PF02195" FT BINDING 52..55 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR017267-1" FT DISULFID 53 FT /note="Interchain" FT /evidence="ECO:0000256|PIRSR:PIRSR017267-2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AES07428.1" FT NON_TER 90 FT /evidence="ECO:0000313|EMBL:AES07428.1" SQ SEQUENCE 90 AA; 9918 MW; 9036F769380D9646 CRC64; SVLIRPLPSV LDPAKVQSLV DTIREDPDSV PPIDVLWIKG AQGGDYFYSF GGCHRYAAYQ QLQRETIPAK LVQSTLSDLR VYLGASTPDL //