ID A0A135L959_PENPA Unreviewed; 248 AA.
AC A0A135L959;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 03-MAY-2023, entry version 17.
DE SubName: Full=Cyclase/dehydrase {ECO:0000313|EMBL:KXG45483.1};
GN ORFNames=PGRI_040320 {ECO:0000313|EMBL:KXG45483.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG45483.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG45483.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG45483.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
CC -!- FUNCTION: Required for the function of coenzyme Q in the respiratory
CC chain. May serve as a chaperone or may be involved in the transport of
CC Q6 from its site of synthesis to the catalytic sites of the respiratory
CC complexes. {ECO:0000256|ARBA:ARBA00024947}.
CC -!- SUBUNIT: Interacts with coenzyme Q. {ECO:0000256|ARBA:ARBA00011814}.
CC -!- SIMILARITY: Belongs to the COQ10 family.
CC {ECO:0000256|ARBA:ARBA00006885}.
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:KXG45483.1}.
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DR EMBL; LHQR01000071; KXG45483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135L959; -.
DR STRING; 5078.A0A135L959; -.
DR OMA; QLHAAMM; -.
DR OrthoDB; 2722348at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0048039; F:ubiquinone binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:InterPro.
DR CDD; cd07813; COQ10p_like; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR044996; COQ10-like.
DR InterPro; IPR005031; COQ10_START.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR12901:SF10; COENZYME Q-BINDING PROTEIN COQ10, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12901; SPERM PROTEIN HOMOLOG; 1.
DR Pfam; PF03364; Polyketide_cyc; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT DOMAIN 82..237
FT /note="Coenzyme Q-binding protein COQ10 START"
FT /evidence="ECO:0000259|Pfam:PF03364"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 248 AA; 27421 MW; 586DE83EE1307723 CRC64;
MRPFRTLRLP SRPTLPSQRH VCPPSSQLKT TRTINTTRPS LRQPLPINNT KTTTRSFGLP
NLSSFLPNNS SPHRVLTATR NLPYNPALLY KVISSVESYS QFLPFLTAST VTARDPETGY
PTQAFLTVGY GPLSETFTSR VICDVEKLTV EANSGAKYGE KDGQGKSSGL SGLFPGANEG
LFEYLTTRWE LVPLSGTQGP LTKVNLEVRF EFRSQMHATI MSSVEGQMAG VMIEAFEKRM
REVEGKGQ
//
