ID A0A161GXF2_9RHOB Unreviewed; 523 AA.
AC A0A161GXF2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Multicopper oxidase type 2 {ECO:0000313|EMBL:AMY72279.1};
GN ORFNames=AKL17_3p0123 {ECO:0000313|EMBL:AMY72279.1};
OS Frigidibacter mobilis.
OG Plasmid cai42_Plasmidc {ECO:0000313|Proteomes:UP000076128}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY72279.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY72279.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RC PLASMID=Plasmid cai42_Plasmidc {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012664; AMY72279.1; -; Genomic_DNA.
DR RefSeq; WP_066819290.1; NZ_CP012664.1.
DR AlphaFoldDB; A0A161GXF2; -.
DR KEGG; daa:AKL17_3p0123; -.
DR PATRIC; fig|1335048.3.peg.5246; -.
DR OrthoDB; 9757546at2; -.
DR Proteomes; UP000076128; Plasmid cai42_Plasmidc.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13865; CuRO_1_LCC_like_3; 1.
DR CDD; cd13887; CuRO_2_MCO_like_2; 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; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034279; CuRO_3_CopA.
DR InterPro; IPR006311; TAT_signal.
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};
KW Plasmid {ECO:0000313|EMBL:AMY72279.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..523
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007822931"
FT DOMAIN 63..148
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 261..351
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 406..520
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 177..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 55456 MW; 35A0A0E71886D545 CRC64;
MNTLSRRGFL AASAAAIGAA QMPRLAFAQS AAPISLAAAT RTLDIDGRAA TVFGLAGPGG
QGLTFDPGQR FRVDLTNDLD VGTIIHWHGQ IPPNAQDGVP DMPMPLLAPG ETRSYDFEAR
PGTHWMHSHV PTQEMQLLAA PLIVRSQEDL AADRQEVVMF LHDFSFKAPE EVLAEISGGH
GGGHGAGHGA GAEPEQSASM GGMGAMQGMD HGAMGHGATG GMPMGNMPGM GGMMGMSGMM
GMGGQMGGMA MDLNDYDWDA YLANDRTLSD PEVVQVERGG RIQLRVINAA AATVFWIETG
GAEARLVAVD GHAVQPVAGT RFGLAMGQRL DIEIDLPNEG GAWPILALRE GARERTGLIL
ATQGAEVRRL DAVAEAAAPA FDTDLAQEAR LIARDPLPDR QVDRSQMLML GGSMQPYLWT
INGAVWGQHQ PIIARSGERV VLSFHNMSMM AHPMHLHGHV FQVVGLNGRR VAGALRDTVH
VPPMSMVDVA LDAGEAARWM LHCHHMPHLA TGMMTEFAVT ASV
//
