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Database: UniProt
Entry: E4NNU3_HALBP
LinkDB: E4NNU3_HALBP
Original site: E4NNU3_HALBP 
ID   E4NNU3_HALBP            Unreviewed;       229 AA.
AC   E4NNU3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Uncharacterized protein SCO1/SenC/PrrC {ECO:0000313|EMBL:ADQ67557.1};
GN   OrderedLocusNames=Hbor_19910 {ECO:0000313|EMBL:ADQ67557.1};
OS   Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS   KCTC 4070 / PR3).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halogeometricum.
OX   NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ67557.1, ECO:0000313|Proteomes:UP000006663};
RN   [1] {ECO:0000313|EMBL:ADQ67557.1, ECO:0000313|Proteomes:UP000006663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC   {ECO:0000313|Proteomes:UP000006663};
RX   PubMed=21304651; DOI=10.4056/sigs.23264;
RA   Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA   Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT   "Complete genome sequence of Halogeometricum borinquense type strain
RT   (PR3).";
RL   Stand. Genomic Sci. 1:150-159(2009).
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; CP001690; ADQ67557.1; -; Genomic_DNA.
DR   RefSeq; WP_013440625.1; NZ_AOHT01000051.1.
DR   AlphaFoldDB; E4NNU3; -.
DR   STRING; 469382.Hbor_19910; -.
DR   GeneID; 9993810; -.
DR   KEGG; hbo:Hbor_19910; -.
DR   eggNOG; arCOG00313; Archaea.
DR   HOGENOM; CLU_093041_0_0_2; -.
DR   OrthoDB; 27579at2157; -.
DR   Proteomes; UP000006663; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   PANTHER; PTHR12151:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006663}.
FT   BINDING         93
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         97
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         190
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        93..97
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   229 AA;  25559 MW;  B5355A9AF7D43557 CRC64;
     MNRRSFLRAA GVTGAAGLAG CLGGSPLGSG DSNPNVVLSE PDRDKQLESE DLPYPAWGQR
     VPDVTIPAPL SDEDVSVRDI EGPHFHTFFF TNCMTVCPLL ISSLRKVQVH SINEGYDDEV
     SFYPVSFDPA RDDAEAFRKE AKQMNIDMDA GNWHFLRPDG KSEARRIVDE TFGVFFEKQE
     NGDKPYMFAH TSVVLLVNGD GYVERAYRGT NPDEQKLIED LRRVRNASE
//
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