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Database: UniProt
Entry: H3AL83_LATCH
LinkDB: H3AL83_LATCH
Original site: H3AL83_LATCH 
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}.
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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
//
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