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Database: UniProt
Entry: A0A1H9XK72_9MICO
LinkDB: A0A1H9XK72_9MICO
Original site: A0A1H9XK72_9MICO 
ID   A0A1H9XK72_9MICO        Unreviewed;       266 AA.
AC   A0A1H9XK72;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SES46043.1};
GN   ORFNames=SAMN05216199_3888 {ECO:0000313|EMBL:SES46043.1};
OS   Pedococcus cremeus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Pedococcus.
OX   NCBI_TaxID=587636 {ECO:0000313|EMBL:SES46043.1, ECO:0000313|Proteomes:UP000199019};
RN   [1] {ECO:0000313|Proteomes:UP000199019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6963 {ECO:0000313|Proteomes:UP000199019};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; FOHB01000008; SES46043.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9XK72; -.
DR   STRING; 587636.SAMN05216199_3888; -.
DR   OrthoDB; 4859715at2; -.
DR   Proteomes; UP000199019; Unassembled WGS sequence.
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; IPR036249; Thioredoxin-like_sf.
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:UP000199019};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..266
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011692326"
FT   BINDING         92
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         96
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         196
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        92..96
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   266 AA;  28740 MW;  83614D6F45C5C53B CRC64;
     MTHATGRRGP VVRARRASVA LGLCAAVLLS GCSNATPSQS RTPATPASGT VLDEALPDTI
     ANLPLSDQHG RHFTLASLRG KTVVLGDFLT LCQEVCPLTS VNLHDVAAAI QRDGRSGDVQ
     VIEATVDPGR DTVARLAAYE KLFGAARDWT LATGSRQGLD ALWTFLGVYQ QRAKEDVTPA
     PRDWWTGAAL TYDVHHQDVV YVIDPRGHAR WVDDGTPNTS GKRPSGRMFR FLNSEGMHNL
     TSPTDPSWTV RDVEEAVTYV SGKPLD
//
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