ID A9A1W0_NITMS Unreviewed; 315 AA.
AC A9A1W0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 13-SEP-2023, entry version 60.
DE SubName: Full=Blue (Type 1) copper domain protein {ECO:0000313|EMBL:ABX12081.1};
GN OrderedLocusNames=Nmar_0185 {ECO:0000313|EMBL:ABX12081.1};
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX12081.1, ECO:0000313|Proteomes:UP000000792};
RN [1] {ECO:0000313|EMBL:ABX12081.1, ECO:0000313|Proteomes:UP000000792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1 {ECO:0000313|EMBL:ABX12081.1,
RC ECO:0000313|Proteomes:UP000000792};
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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DR EMBL; CP000866; ABX12081.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A1W0; -.
DR STRING; 436308.Nmar_0185; -.
DR EnsemblBacteria; ABX12081; ABX12081; Nmar_0185.
DR KEGG; nmr:Nmar_0185; -.
DR eggNOG; arCOG02926; Archaea.
DR eggNOG; arCOG03700; Archaea.
DR HOGENOM; CLU_862224_0_0_2; -.
DR InParanoid; A9A1W0; -.
DR OrthoDB; 4392at2157; -.
DR Proteomes; UP000000792; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 2.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR36507; BLL1555 PROTEIN; 1.
DR PANTHER; PTHR36507:SF1; CELL SURFACE LIPOPROTEIN; 1.
DR Pfam; PF00127; Copper-bind; 1.
DR SUPFAM; SSF49503; Cupredoxins; 2.
DR PROSITE; PS00196; COPPER_BLUE; 1.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 4: Predicted;
KW Copper {ECO:0000256|ARBA:ARBA00023008}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000792};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 239..315
FT /note="Blue (type 1) copper"
FT /evidence="ECO:0000259|Pfam:PF00127"
SQ SEQUENCE 315 AA; 33051 MW; C685566A5F273C3E CRC64;
MTENQYYLTT PARTGKMMAI MLGICIVGGA IFFSLWDYWI SEPAPVVAMM GGDSTPTAVA
VHTGATITSD LSFIESSDFI TLAFNALPGE PGNNPTINME VGDKVIFNVV NDGVSFHSFG
VTADTEGFGG IFPGSEVASP ANPLKSGEGG TSEFIAGEEG VFYYICTVPG HREQGMVGKI
IVGDAEVPEE VVEAVPEPMA TEPAEEKAPV STEPVAYDGP ISLPEGSGVP GCQETNECYI
PYHVTAPAGT EIVWSNDDTA AHTVTSGSPA DGPDGIFDSS ILAGGLTFSV TLDEPGEYPY
YCIVHPWMVG NITIE
//
