ID H3AL83_LATCH Unreviewed; 482 AA.
AC H3AL83;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Zgc:152951 {ECO:0000313|Ensembl:ENSLACP00000010404.1};
GN Name=ZGC:152951 {ECO:0000313|Ensembl:ENSLACP00000010404.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000010404.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000010404.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins. {ECO:0000256|ARBA:ARBA00002549}.
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; AFYH01199416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01199417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01199418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01199419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01199420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01199421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AL83; -.
DR STRING; 7897.ENSLACP00000010404; -.
DR Ensembl; ENSLACT00000010483.1; ENSLACP00000010404.1; ENSLACG00000009166.1.
DR eggNOG; ENOG502QS72; Eukaryota.
DR GeneTree; ENSGT00390000016088; -.
DR HOGENOM; CLU_012751_1_1_1; -.
DR InParanoid; H3AL83; -.
DR OMA; IVVSQCH; -.
DR TreeFam; TF315258; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000009166; Expressed in pelvic fin and 5 other cell types or tissues.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04371; DEP; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR006869; DUF547.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR34386; GLUTAREDOXIN; 1.
DR PANTHER; PTHR34386:SF1; GLUTAREDOXIN-LIKE PROTEIN NRDH; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF04784; DUF547; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SMART; SM00049; DEP; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 152..206
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
SQ SEQUENCE 482 AA; 54114 MW; EB260137C396FA01 CRC64;
LSFSLPKCDT MERFAGRVTV YSVVGCPHCN SAKAFLKGLG LPYCEVDVEK DSTVRQKVKE
LTGRSTVPQI FFNKTHIGGN DDLQNLVSNN GFFSPQIKKK KKNKPSDLMI PSIPCFTDVK
GERDNFAELI LEFKSSGIIK SHGSFLKVHK LTFSGSELIE WLVDKKGFEK DQALNTGKEL
MQKKFFSDVS GKGDFQDGHT LYRLIEHDCL TALNSGKTAE CSPVLAAELS EALRRLILKL
YGEHLSPDGK TVDYKAMENS QTFQEYCELA TQLQRLELKS MTREEKLAFF INVYNALVIH
GHIKMGPPKN LWQRYKFFNG VSYLIGGEVF TLQDIENGVL RGNRKGVGQL TKPFSQGDQR
LQVALPEAEP LIHFALNCGA KGCPAIRSYS AKTVDAQLKT AGEAFLEGDD GCHVNSCKNE
IRLSQIFKWY KVDFGDTNEK LLQWVAEHMA DSPKKKELKE LLGKGNHKVV FLPYDWSSNS
KD
//