ID B8MDT0_TALSN Unreviewed; 691 AA.
AC B8MDT0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Laccase, putative {ECO:0000313|EMBL:EED18309.1};
GN ORFNames=TSTA_120560 {ECO:0000313|EMBL:EED18309.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED18309.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; EQ962655; EED18309.1; -; Genomic_DNA.
DR RefSeq; XP_002482301.1; XM_002482256.1.
DR AlphaFoldDB; B8MDT0; -.
DR SMR; B8MDT0; -.
DR STRING; 441959.B8MDT0; -.
DR GeneID; 8100040; -.
DR VEuPathDB; FungiDB:TSTA_120560; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_7_2_1; -.
DR InParanoid; B8MDT0; -.
DR OMA; HGHHFYI; -.
DR OrthoDB; 449862at2759; -.
DR PhylomeDB; B8MDT0; -.
DR Proteomes; UP000001745; 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:UniProtKB-KW.
DR CDD; cd04206; CuRO_1_LCC_like; 1.
DR CDD; cd04205; CuRO_2_LCC_like; 1.
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; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
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:UP000001745};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 127..244
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 268..414
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 526..669
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 77338 MW; 29A5268D8542F467 CRC64;
MQRRLSKRQQ QQDATKSPDA TAQPVEQQQK TEANDKRRGS KTTLHTPSIL IALVCILPFL
ATVVLFVRYY YESNNDDSIN RLSNSLHDHE SISSTLKYDN RIHENGRLRP EDHIHRGAIT
QTLNWSVTAG QRRPDGVDKR IYLINDMFPG PSIEARSGDT LQILVHNNLE DEQISLHWHG
LNMRGANTMD GVIGVTQCGI QPGQSFWYNF TISETQSGTF WYHAHSAVQR ADGLYGSLVV
HRPDSTLVSP NERSEMVSDS VKYGYDKEIV LMIGDWYHRT ATDVASWYLW WGSMGYEPVP
DSLLVNGAGR FNCSRAVRAR PLDCIGSADE MPPLILDGNS SYRVRVVNTG SLTGIILGFA
PGTSIQVITI DGGNPVEMEA VDGGRSSVGI LFPGQRVDFV LRPLKGQTSW MTVKMDDSYV
SPYTLYKTAE LSVSSDFTIG NPALVPQQSF PIFQTPLPSD SLPSSPTAQS NNTNDIEEDD
IININTLPST RTLLSSLPPK SEQTHIVYTK VEKLSRLDNI PHGFFNRTTW KIQSDPPYPL
LGLPRNQWDK HQFAVSTGNK NGWVDLVVNN LDEGAHPFHL HGYNFYVVDI YESPEGSGRW
GSYNPWTSPS FNENIDPYDL TKAVLRDTVQ IPRRGYAVLR FKADNPGVWL FHCHVMWHLA
GGMAMVIDSG SGDDSVAHEP WLAEEGMECR V
//
