ID A0A0K9NGT6_ZOSMR Unreviewed; 169 AA.
AC A0A0K9NGT6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Monothiol glutaredoxin-S15, mitochondrial {ECO:0000313|EMBL:KMZ55986.1};
GN ORFNames=ZOSMA_9G00890 {ECO:0000313|EMBL:KMZ55986.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ55986.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- FUNCTION: May only reduce GSH-thiol disulfides, but not protein
CC disulfides. {ECO:0000256|ARBA:ARBA00002426}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
CC {ECO:0000256|ARBA:ARBA00008983}.
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:KMZ55986.1}.
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DR EMBL; LFYR01002228; KMZ55986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NGT6; -.
DR STRING; 29655.A0A0K9NGT6; -.
DR OMA; CAFSKRM; -.
DR OrthoDB; 1038at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03028; GRX_PICOT_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR00365; Grx4 family monothiol glutaredoxin; 1.
DR PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10293:SF16; GLUTAREDOXIN-RELATED PROTEIN 5, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987}.
FT DOMAIN 73..137
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 169 AA; 18305 MW; 8F3BC3AB6A3147B6 CRC64;
MARSLANTVL KGIIGSHHRA ATCRTLCQQG TIAYYSVSSD AGTHDDFKSI SKLADSDISL
KDVVEKDVKE NPVMIYMKGI PEAPACGFSS LAVRVLKAHG VPIASRNILE DQELKSGVKA
FSHWPTFPQI FINGEFIGGS DIILNMHQSG ELTEKLKGAT TSNTVKRDD
//