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Database: UniProt
Entry: G4F583_9GAMM
LinkDB: G4F583_9GAMM
Original site: G4F583_9GAMM 
ID   G4F583_9GAMM            Unreviewed;       617 AA.
AC   G4F583;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Copper-resistance protein, CopA family {ECO:0000313|EMBL:EHA16235.1};
GN   ORFNames=HAL1_07695 {ECO:0000313|EMBL:EHA16235.1};
OS   Halomonas sp. HAL1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA16235.1, ECO:0000313|Proteomes:UP000005692};
RN   [1] {ECO:0000313|EMBL:EHA16235.1, ECO:0000313|Proteomes:UP000005692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX   PubMed=22156396; DOI=10.1128/JB.06359-11;
RA   Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA   Wang G., Rensing C.;
RT   "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT   Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL   J. Bacteriol. 194:199-200(2012).
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:EHA16235.1}.
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DR   EMBL; AGIB01000031; EHA16235.1; -; Genomic_DNA.
DR   RefSeq; WP_008957452.1; NZ_CP130611.1.
DR   AlphaFoldDB; G4F583; -.
DR   PATRIC; fig|550984.5.peg.1498; -.
DR   Proteomes; UP000005692; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd13848; CuRO_1_CopA; 1.
DR   CDD; cd13874; CuRO_2_CopA; 1.
DR   CDD; cd13896; CuRO_3_CopA; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR   InterPro; IPR011707; Cu-oxidase-like_N.
DR   InterPro; IPR001117; Cu-oxidase_2nd.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR045087; Cu-oxidase_fam.
DR   InterPro; IPR006376; Cu-R_CopA.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR034284; CuRO_1_CopA.
DR   InterPro; IPR034282; CuRO_2_CopA.
DR   InterPro; IPR034279; CuRO_3_CopA.
DR   InterPro; IPR006311; TAT_signal.
DR   NCBIfam; TIGR01480; copper_res_A; 1.
DR   PANTHER; PTHR11709:SF218; FI03373P-RELATED; 1.
DR   PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 3.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          63..172
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          183..355
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          499..616
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   617 AA;  68600 MW;  AA634D2BBD8890B5 CRC64;
     MARSSIISHP LSRRQVLKGG AALGLGSAAA MGLTPAWANP WGRTNVYAQG VEEGPEVSLA
     IRRESIPIDG QEAHPISING TSPGPLIRLK EGQDAVLRVT NLLDESTSIH WHGLILPPEM
     DGVPGVSFAG IAPGETFTYR FPVRQNGTYW YHSHSGLQEQ LGHAGPLIID AAEREPIRYD
     REHVLLLTDW TFEDPMSVFR NLKTMEGYYN FQERTIADFF ADVREKGFSQ TAEMRGMWAK
     MRMSSRDIAD VTGSTYTYLL NGHSPQENWN ALFKAGERVR LRVINGSAMS YFDVRIPGLK
     MTVVAADGQP VQPVPVDEFR IGVAETYDVL VSPEDDRAYT IFAEAMDRSG YARATLAPRE
     GMQAEIPKRR QIADRGMEAM GAHGMGDMEG MDHSGMSNME GMDHSNMPGM SGDDAGMEGM
     DHSNMEGMDH SNMEGMDHSN VGGMSGEQAK VGENGILIAG EAQPGSRYDQ AGIGIDPNER
     RVLVYRDLKA FTPWPDRREP GRELELHLTG NMERYMWSFD GKKFSEVTGP IHFVKDERLR
     LILINDTMME HPIHLHGMWM ELENGQGELI PRKHTLNVKP GERVSALITA DAEGSWAFHC
     HLLYHMDAGM FRVVQVS
//
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