GenomeNet

Database: UniProt
Entry: A0A9W9X8H5_9EURO
LinkDB: A0A9W9X8H5_9EURO
Original site: A0A9W9X8H5_9EURO 
ID   A0A9W9X8H5_9EURO        Unreviewed;       888 AA.
AC   A0A9W9X8H5;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   28-JAN-2026, entry version 8.
DE   RecName: Full=Cytochrome c oxidase assembly protein COX16, mitochondrial {ECO:0000256|ARBA:ARBA00015368};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE   AltName: Full=Cytochrome c oxidase assembly protein cox16, mitochondrial {ECO:0000256|ARBA:ARBA00019222};
GN   ORFNames=N7530_000635 {ECO:0000313|EMBL:KAJ5486335.1};
OS   Penicillium desertorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1303715 {ECO:0000313|EMBL:KAJ5486335.1, ECO:0000313|Proteomes:UP001147760};
RN   [1] {ECO:0000313|EMBL:KAJ5486335.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 17660 {ECO:0000313|EMBL:KAJ5486335.1};
RA   Petersen C.;
RL   Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAJ5486335.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 17660 {ECO:0000313|EMBL:KAJ5486335.1};
RX   PubMed=36726175;
RA   Petersen C., Sorensen T., Nielsen M.R., Sondergaard T.E., Sorensen J.L.,
RA   Fitzpatrick D.A., Frisvad J.C., Nielsen K.L.;
RT   "Comparative genomic study of the Penicillium genus elucidates a diverse
RT   pangenome and 15 lateral gene transfer events.";
RL   IMA Fungus 14:0-0(2023).
CC   -!- FUNCTION: Required for the assembly of the mitochondrial respiratory
CC       chain complex IV (CIV), also known as cytochrome c oxidase. May
CC       participate in merging the COX1 and COX2 assembly lines.
CC       {ECO:0000256|ARBA:ARBA00002490}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004434}.
CC   -!- SIMILARITY: Belongs to the COX16 family.
CC       {ECO:0000256|ARBA:ARBA00008370}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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:KAJ5486335.1}.
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; JAPWDO010000001; KAJ5486335.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9W9X8H5; -.
DR   OrthoDB; 6058203at2759; -.
DR   Proteomes; UP001147760; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd01446; DSP_MapKP; 1.
DR   CDD; cd18533; PTP_fungal; 1.
DR   FunFam; 3.90.190.10:FF:000142; Protein tyrosine phosphatase (Pyp1), putative; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR020164; Cyt_c_Oxase_assmbl_COX16.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR050348; Protein-Tyr_Phosphatase.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR19134:SF561; PROTEIN TYROSINE PHOSPHATASE 36E, ISOFORM A; 1.
DR   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF14138; COX16; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP001147760};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        36..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          335..451
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          589..882
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          764..873
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          200..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   888 AA;  98504 MW;  15BA56787170AF79 CRC64;
     MPVFQSKTFR RAATESSSLG ERLGAFYRAR LARHPFILFG LPFMAVIVAG SFALTPAAAL
     RYERYDRKVK QLSQDEAFDL GLKGPDGEEG IKRNPRRRIV GDEKEEYYRL MAKDLDQWEQ
     KRVERFKGEP DGRLPGTGVV EANLPVMTGP GRSPSSPWVQ SAQGGHHDGG VTQSFQSTMS
     PSTTGMMSSA AFTERSSPNY FGMAVQSPHN QQTSNPGLSM QKNWGTLPHS QPLPSPKLPM
     FSQESVSAGL KNLLKTETET SRIRRESALH GSSSPQTTSW SNPSPSHSLG NFSFEQPNEL
     RLPAGKNSTP TPQGATPASF PWVSAERCAE LLESSQSNTM LFDVRPFAHF RQANIKGSLN
     LCIPTTLLKR RSFDTQKLEG TFTDDADKRS FACWRKSDVI IVYDSAAADL KDAAPLLNLL
     NKFQAEDWKG DGLILQNGFR GFSGRFPHLI QQPQTQTTGP SSKRPSPMRI NLQSVAPVVG
     GCALPESSSA VNPFFGNIRQ NMDLLGGVGQ IPLKQPDQLT EAKRQQLPSW LRGASDTKDQ
     GHIISNKFLV LEKTELERMK QALTYEGPSA DTNGSPKKYR VAGIEKGTKN RYNDIYPFDH
     SRVRLEGIPS GACDYVNANH ISAELTNRKY IATQAPVPDT FDDFWRVVWE QDVRLLVSLT
     AEVERGQIKC HRYWESGKYG PFEVKAYSEK HINIESKGGP IDPTAGSPKA TDQHDGTNEN
     PVITVRNFSI CHTSFPFEPI RDITQLQYPY WPDFGTTSQP THLLHLIEQC NKVIRATSNS
     SFSREQAEPK GQRPVLVHCS AGCGRTGTFC TVDSVLDMLK RQRAQAAGGG GLDQNPSGSS
     EWIGDSNLDL IAKTVEDFRR QRPSMVQNLS QYALCYESVL EWLASEMD
//
DBGET integrated database retrieval system