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Database: UniProt
Entry: A0A9W9XUV8_9EURO
LinkDB: A0A9W9XUV8_9EURO
Original site: A0A9W9XUV8_9EURO 
ID   A0A9W9XUV8_9EURO        Unreviewed;       893 AA.
AC   A0A9W9XUV8;
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=N7463_005990 {ECO:0000313|EMBL:KAJ5503116.1};
OS   Penicillium fimorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1882269 {ECO:0000313|EMBL:KAJ5503116.1, ECO:0000313|Proteomes:UP001149954};
RN   [1] {ECO:0000313|EMBL:KAJ5503116.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 29495 {ECO:0000313|EMBL:KAJ5503116.1};
RA   Petersen C.;
RL   Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAJ5503116.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 29495 {ECO:0000313|EMBL:KAJ5503116.1};
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:KAJ5503116.1}.
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DR   EMBL; JAPWDS010000003; KAJ5503116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9W9XUV8; -.
DR   OrthoDB; 6058203at2759; -.
DR   Proteomes; UP001149954; 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:UP001149954};
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          334..450
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          588..887
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          764..878
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          150..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..283
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  99095 MW;  3D16134077B49634 CRC64;
     MPVFQSKTFR RAATESSSLG ERLGAFYRAR LARHPFILFG LPFMAVIVAG SFALTPAAAL
     RYERYDRKVK QLSQDEAFDL GLKGPDGEEG IKRNPRRRII GDEKEEYYRL MAKDLDQWEQ
     KRVERFKGEP DGRLPGTGVV EANLPAMTGP GRSPSSPWVQ SAQGGHHDGV TQSFQSAISP
     STTGMKSSAA FAEMSSPNYF GMAVQTPNNQ QISNPGLSMQ KNWGTLPNTQ PLPSPKLPVF
     CQESVSAGLK NLLKTEPETS RIRRESALHG SSSPQTTSWS TPSPSHPLGN FSFAQPNGLK
     LPASKTLAPI PQGATPASFP WVSAERCAEL LESSQSNTML FDVRPFAHFR QANIKGSLNL
     CIPTTLLKRR SFDTQKLEGT FTDDTDKQNF ARWRKCDVII VYDSTAADLK DAAPLLSLLN
     KFQAEDWKGD GLILQNGFRG FSGRFPHLIQ QSQTQTTGPS SKRPSPMRIN LQSVAPVVGG
     CALPESSSAV NPFFGNIRQN MDLLGGVGQI PLKQPDQLTE AKRQQLPSWL RGASDIKDQG
     HIVSNKFLIL EKTELERMKQ ALTYEGPSAD TNDDPKKYRV AGIEKGTKNR YNDIYPFDHS
     RVRLEGIPSG ACDYVNATHI SAELSNRKYI ATQAPVPDTF DDFWRVVWEQ DVRLIVSLTA
     EVERGQVKCH PYWESGKYGP FEVKAYSEKH ISIESGGESI NPTAGSPKAS TDRPDGTNEN
     PVITVRNFSI CHTSFPFQPL RDITQLQYPY WPDFGTTSQP THLLHLIEQC NKVIRATSNS
     SFSSQQAEPK GQRPVLVHCS AGCGRTGTFC TVDSVLDMLK RQRAQAQRVQ AVGGGDLDQN
     PSGSTEWMED FNLDLIAKTV EDFRRQRPSM VQNLSQYALC YESVLEWLIS EMN
//
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