ID A0A397HTK1_9EURO Unreviewed; 527 AA.
AC A0A397HTK1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Multicopper oxidase abr1 {ECO:0000313|EMBL:RHZ64906.1};
GN Name=ABR1 {ECO:0000313|EMBL:RHZ64906.1};
GN ORFNames=CDV56_103510 {ECO:0000313|EMBL:RHZ64906.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ64906.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ64906.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ64906.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
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:RHZ64906.1}.
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DR EMBL; NKHU02000020; RHZ64906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397HTK1; -.
DR STRING; 41047.A0A397HTK1; -.
DR VEuPathDB; FungiDB:CDV56_103510; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000215305; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:InterPro.
DR CDD; cd13877; CuRO_2_Fet3p_like; 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; IPR008972; Cupredoxin.
DR InterPro; IPR044130; CuRO_2_Fet3-like.
DR PANTHER; PTHR11709:SF361; IRON TRANSPORT MULTICOPPER OXIDASE FET3; 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; 2.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 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:UP000215305};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..527
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017402611"
FT DOMAIN 27..113
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 128..159
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 167..324
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 388..495
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 527 AA; 59216 MW; 85AEE13D53771EBB CRC64;
MLHSGAFFLF WLVGFTAAKD VHLDWNITWV WAAPDGFGRP MIGINDEWPC PLVNADLGDR
LIVDVYNGLG NQSTGIHWHG FHQYMTGTMD GSNQVTQCAL PPGSSMRYEF DVSFSLAIWL
ILLYSRGQVN QTGTYWYHSH EMGQYPDGLR GPLIVRDPSP PFEYDDEFTL TLTDHYHEQM
PFLLQQYEAD SVGAHAGVNE PLPAAALIND AVNATTIRVE PNKTYLVHLI CVGNWPGHVI
VFDDHEISVV EVDGIWVDTY PTGGKKIRLA TGQRISILLR TKDNADANYA IWDSMDVNMM
FFYENRTIPQ TFNPNATAWL VYDEEKELPP PPDIHELDPN NDFVDDLVYV PADHEPVLEP
VDHQIILSTG VTQRDGRSVY TVNGKTYVDQ EEPTMYTALA AGPDNSSDPS IYGQVNPFVL
AYGEVVEIVI NNHHGNLHPW HLHGHQFQVL QRTIPEGGYF NGYFANISST PVRRDTIMVQ
NHGHAVLRFR ADNPDKFGPS TPVKMRTDLY HECGSSTAMS NGMSPRG
//
