ID A0A397VR44_9GLOM Unreviewed; 602 AA.
AC A0A397VR44;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:RIB24408.1};
GN ORFNames=C2G38_2139263 {ECO:0000313|EMBL:RIB24408.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB24408.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB24408.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB24408.1,
RC ECO:0000313|Proteomes:UP000266673};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-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:RIB24408.1}.
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DR EMBL; QKWP01000218; RIB24408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397VR44; -.
DR STRING; 44941.A0A397VR44; -.
DR Proteomes; UP000266673; 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; cd13910; CuRO_3_MCO_like_4; 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; PTHR11709:SF515; ADR239WP; 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; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 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 Reference proteome {ECO:0000313|Proteomes:UP000266673};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..602
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017303601"
FT DOMAIN 49..161
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 170..337
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 415..532
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 602 AA; 69259 MW; CDAE1F7F7EA5C401 CRC64;
MILSKSLSLW TILCILALLN SLAFILASPI KKHAYVPETK TFYLHLYKAK LSPDGFERVV
WTVNGTYPGP TLVVTKGDRL IIHIINNLGE PTSIHFHGFF QRGTNWYDGV PGQTQCPIPN
NTTFIYNFTI PDQSGTFWYH SHYLAQYVDG VLGAIIVKDP NDPYQNDYDE EIVVLLSDWY
HNESSTLISY YLSPASEGKE PQPDNGLIDG RNNYHCEWAL ASHKCIDKAG LSKFNFVPGK
RYRLRVINTS AFSNFIFSID EHEMDLIEVE GMMTKRHKIH RLIINVAQRY SVIVTADKLV
SNFWMRADLQ TDCFDDSSDQ IVHLNPYVKA IVHYEGANNL DPTTKGWADN PNYHDHCVDL
NTSDIKPLFL ENVPAKADQI IYLNASFEND DFNINRGLIN GSTYVIDIYN PTINQVLFEN
KHSFPPNQNV FGQFNTSQVI DIVVYNDDDG EHPFHLHGHT FWVLGSGEVN TEPDYSKLNI
YDPIRRDTAT IPAEGWIVIR FVADNPGIWA FHCHIEWHVE AGLVAQFVEL PNELRELKPP
DDWEQLCIKS TNPYNLLKPQ SEPKIFINDM RNIDILIKNL GWNWGEMEFN WNYLLVYFLN
LF
//
