GenomeNet

Database: UniProt
Entry: A0A1B9IF68_9TREE
LinkDB: A0A1B9IF68_9TREE
Original site: A0A1B9IF68_9TREE 
ID   A0A1B9IF68_9TREE        Unreviewed;       640 AA.
AC   A0A1B9IF68;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Acidic laccase {ECO:0000313|EMBL:OCF53950.1};
GN   ORFNames=L486_08555 {ECO:0000313|EMBL:OCF53950.1};
OS   Kwoniella mangroviensis CBS 10435.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1331196 {ECO:0000313|EMBL:OCF53950.1, ECO:0000313|Proteomes:UP000092583};
RN   [1] {ECO:0000313|EMBL:OCF53950.1, ECO:0000313|Proteomes:UP000092583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10435 {ECO:0000313|EMBL:OCF53950.1,
RC   ECO:0000313|Proteomes:UP000092583};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Kwoniella mangroviensis CBS10435.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10435 {ECO:0000313|Proteomes:UP000092583};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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; KV700104; OCF53950.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B9IF68; -.
DR   SMR; A0A1B9IF68; -.
DR   STRING; 1331196.A0A1B9IF68; -.
DR   Proteomes; UP000092583; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:InterPro.
DR   CDD; cd13851; CuRO_1_Fet3p; 1.
DR   CDD; cd13877; CuRO_2_Fet3p_like; 1.
DR   CDD; cd13899; CuRO_3_Fet3p; 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   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; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092583};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..640
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008628644"
FT   TRANSMEM        582..604
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..148
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          160..325
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          393..522
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   640 AA;  71195 MW;  A09DDB578A90F2AB CRC64;
     MARLSSLLSA VTIAATVVKA ATIEHWWNIT YAQANPDGLQ ERRVIGVNNS WPPPMLTATQ
     GDVLIIHATN GLGDDSVGTS LHTHGMFFNG SNWADGAVGT TQCPIPNGYT MDYMIDTSRQ
     TGTYWIHGHH EGQNTDGLRA PFVISPQNAT GRSDNVTWDE EYTLVVGDWY HDEYPDLIKD
     EFLIWTNPTG AEPVPKSAVC YVAKNGSYIH SNADLMQGVG VSDNATIAFE AGKTYKIHIV
     NTGTLGMFWI RMDQHQMKII EMDGVEHEPY PVDVLTVSVA QRYSIIVEAL NTTGTNYAMM
     IMQDTDMYDA VPDELQLNNT IQIVYDSNAP KADPVEVGID DIVTFNDTEL VPILKNELLQ
     PDVKFELNAY FDTYDDGTNR ASFNNVTFQM PMVPSMFTAL TMGDDAYNTA VYGAQTNAFV
     YKHMQVVELT VFNWDAGFHP FHFHGHEFQI VHKSFDVTSN DTTVNPPINE NQENPARRDT
     IVIPPTGSVT LRWRADNPGA WMFHCHIDWH LSSGLAAIFL EAVDAFQATN TTDNSVPQQV
     FDQCNYWKTP TSGNIVGKFS TTDFKGQPYG PFPLKMGWTS KAIGALAGCI ITVLLGIATI
     VWYASGELDE REVEEEVKYK LEAKKNKVPL WKKVLPNKSG
//
DBGET integrated database retrieval system