ID A0A429X1H1_9BACI Unreviewed; 507 AA.
AC A0A429X1H1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Copper oxidase {ECO:0000313|EMBL:RST56980.1};
GN ORFNames=D5F11_025145 {ECO:0000313|EMBL:RST56980.1};
OS Siminovitchia terrae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Siminovitchia.
OX NCBI_TaxID=1914933 {ECO:0000313|EMBL:RST56980.1, ECO:0000313|Proteomes:UP000287296};
RN [1] {ECO:0000313|EMBL:RST56980.1, ECO:0000313|Proteomes:UP000287296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29736 {ECO:0000313|EMBL:RST56980.1,
RC ECO:0000313|Proteomes:UP000287296};
RA Sun L., Chen Z.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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:RST56980.1}.
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DR EMBL; QYTW02000048; RST56980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429X1H1; -.
DR OrthoDB; 9757546at2; -.
DR Proteomes; UP000287296; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd04232; CuRO_1_CueO_FtsP; 1.
DR CDD; cd13867; CuRO_2_CueO_FtsP; 1.
DR CDD; cd13890; CuRO_3_CueO_FtsP; 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; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR48267:SF1; BILIRUBIN OXIDASE; 1.
DR PANTHER; PTHR48267; CUPREDOXIN SUPERFAMILY PROTEIN; 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; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..507
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019083223"
FT DOMAIN 98..211
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 236..333
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 387..506
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 507 AA; 56864 MW; 2293FAA9F3718D21 CRC64;
MKRILLTGAS LLLILAGCTN AATDKHSGEQ SKEHMQMQHD ENMDMDHENM EDMEDMEGHM
DHDDIPSLKA SKGTQELSLP PLLKKQQGSD FDYEVVAQEG TTQFFDGTQT KTYGYNGNLL
GPTVRLKKGE TVKVKVRNEL NEPTTFHWHG LEIPGSEDGG PQDEIQPGKS KIVTLKADQP
AATLWYHPHP HELTSEQVFK GLGGMLYVEG TDQDSADLPK NYGVDDIPLI FQDRIFDEDH
QLNYDELMNS DGTIGDVSLV NGTLHPKLTV TQPVMRFRIL NGSNARNYTF RLSNGASFTQ
IASDGGLLDE PVEMNELTLS ASERSEILID FSKLDSDEPV AITDEKGNVL LPFDLDFESK
ATKNSTVSWI ADEPFLTKEE KDLPVSKEIE LFGMMDKVTI NGQKFDPNRI DFKQEKGVSE
VWEIYNKPDH MGGMIHPFHI HGTQFKIISR DGKGPAPNEQ GLKDSVLIEP GERVKLLVTF
PEKGIYMYHC HILEHEDNGM MGQVEVY
//
