ID A0A397JR25_9GLOM Unreviewed; 551 AA.
AC A0A397JR25;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Multicopper oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Glove_22g130 {ECO:0000313|EMBL:RHZ88476.1};
OS Diversispora epigaea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ88476.1, ECO:0000313|Proteomes:UP000266861};
RN [1] {ECO:0000313|EMBL:RHZ88476.1, ECO:0000313|Proteomes:UP000266861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT104 {ECO:0000313|EMBL:RHZ88476.1,
RC ECO:0000313|Proteomes:UP000266861};
RA Sun X., Fei Z., Harrison M.;
RT "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL Submitted (AUG-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:RHZ88476.1}.
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; PQFF01000020; RHZ88476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397JR25; -.
DR STRING; 1348612.A0A397JR25; -.
DR Proteomes; UP000266861; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 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; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000266861};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..169
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 180..343
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 421..533
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 551 AA; 63461 MW; F98315813F666ECF CRC64;
MNSFSSIIVL IVINLLFIIV PLFTNDVGAT ALPYHDKNNK RFPSKPQVYE YKFHLSKVEL
APDGFTKLVS AVNGQYPGPP IQVNRGDRLI VHVVNCLGEP TSMHWHGIFQ RGTPWFDGVV
GQTQHVIPDK YTFTYDFTID LQSGSYWYHS HHRGQYMDGV LGPLIVYDEF DKILYGYDED
LIVLITDWYH DNSADLFKWF LSPASKGAEP IPNNALINGK NDYNCDWAAK GSKCVNNSEL
ANFVFKKDCK YRMRVINTSG FSAFVFSIDN HDFEIIEVEG TKTIPYRINQ LSINVAQRYS
VIVDAKQPIS NYWMRVEFQQ ECLPDEFAYN LTIDNKAIIH YEEASLENPT TNSWTDKVEE
CVDLEQNKLK PLLPNIPPNC DTRIVYEIEF KEDSNGVNRP YVNGSSYVSD EEYPTLKKVF
DGVHEFAKTE NIYQIHKKDE VIDVVFINKD DGEHPFHLHG HVFWILGWGE KDEKLVYEKL
NTLNPIQRDT STIPAEGWIA LRFIANNPGV WACHCHMEWH LGAGLLVQFV ELPEIIKTLN
PPKSWWDLFS K
//
