ID A0A1V6YNW1_PENNA Unreviewed; 427 AA.
AC A0A1V6YNW1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=MOSC domain-containing protein {ECO:0000259|PROSITE:PS51340};
GN ORFNames=PENNAL_c0015G08926 {ECO:0000313|EMBL:OQE89017.1},
GN PNAL_LOCUS1844 {ECO:0000313|EMBL:CAG7999631.1};
OS Penicillium nalgiovense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE89017.1, ECO:0000313|Proteomes:UP000191691};
RN [1] {ECO:0000313|EMBL:OQE89017.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|EMBL:OQE89017.1};
RA Nielsen J.C., Nielsen J.;
RT "Uncovering the secondary metabolism of Penicillium species provides
RT insights into the evolution of 6-MSA pathways.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000191691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
RN [3] {ECO:0000313|EMBL:CAG7999631.1}
RP NUCLEOTIDE SEQUENCE.
RA Branca A.L. A.;
RL Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases.
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:OQE89017.1}.
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DR EMBL; CAJVNV010000054; CAG7999631.1; -; Genomic_DNA.
DR EMBL; MOOB01000015; OQE89017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6YNW1; -.
DR STRING; 60175.A0A1V6YNW1; -.
DR OMA; KSFRCID; -.
DR OrthoDB; 5490564at2759; -.
DR Proteomes; UP000191691; Unassembled WGS sequence.
DR Proteomes; UP001153461; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR005303; MOCOS_middle.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000191691};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..407
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT REGION 57..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 47725 MW; B143681BEA96B6E1 CRC64;
MSNVDIPHGG ILPNFIVIFF LSVLFLVLKT LTTLKTSNNP KGCRRLGLPP GQSNLDDEFD
SKYSQGVPSD QDDHGRPSWR VKALFSYPLK SCGAVELQVS NVVPTGLEFD RQFVFAEYNN
DEWNIRTLRN PGFNRLALIH PEIWVPDPSA SDYDADLPEI KSQGVMLISY PRMLPAGWKS
LPIKVGMALK FLKSQQTFQV PLLPPADSKF PLVPVKIWKD KVLAHDYGRL LPASLHAYLG
SGPSKNTLTL LRASAPHSRQ IFRNAPRKED LGFQPNTAFA DAYPIHLLSI SSHRDVAARC
VYAIPRLSIC RFRANIIVQG PSAFEEDHWK RLAIGGTEIH ASCRTVRCRL PNVDPLSGDR
HKAEPDRTLK SYRRIDDGDR TNACLGMQLV PAKEEFVLRV GDSVEVLETG DHQYIKMLAP
GEKVEGV
//
