ID A0A1V6PVC2_9EURO Unreviewed; 725 AA.
AC A0A1V6PVC2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DUF726 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENANT_c030G08951 {ECO:0000313|EMBL:OQD80958.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD80958.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
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).
CC -!- SIMILARITY: Belongs to the TMCO4 family.
CC {ECO:0000256|ARBA:ARBA00009824}.
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:OQD80958.1}.
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DR EMBL; MDYN01000030; OQD80958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PVC2; -.
DR OrthoDB; 8526at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR007941; DUF726.
DR PANTHER; PTHR17920:SF22; DUF726 DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_2G12860); 1.
DR PANTHER; PTHR17920; TRANSMEMBRANE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 4 TMCO4; 1.
DR Pfam; PF05277; DUF726; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 280..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 79137 MW; BF206B7C5A5E0BE4 CRC64;
MFKTLKEKQT ALFDSKRSNN NASESDRGQD LSSILDRSQR ADLTILVAEV AESMRISVLE
IFENQTPNSK SDSKDEPRTP SIPRKPLPTE ETDEDTPPLP PRPSNESAGK GGSPRTGASK
PLKPQAKITA LSIFEDWRDS VLLRIGEVVN KDDDDEGHQV SEEMQKAAKS DEIPFEGDRD
SLEKLQEIYH PVETPLVKLP KATRLLIVHS LLLLMLSLKH YSAYSRVLML NVASSLNIDI
NVLNEDEVKV ARGLLDTALA LSDQEPKKEP KKDDMRKWKV GIASVAGAAL IGLTGGLAAP
LVAAGLGTVM GGLGLGATAA AGYLGVLAGS SVVVGGLFGA YGGRMTGRMM DKYAREVDDF
AFLPIRGQRS RDEKDSEAAR QDHRLRVTIG VTGWVKEEAN FTVPWKVIGS NSEVFGLRWE
MEPLMNLGNA ISALVTSAAW SVAGREVLAR TVFHTLMSAV MLPLGLLNVA GVVDNPFSVA
KSRADKAGEV LADVLINKAQ GERPVTLIGY SLGSRLIFSC LQTLAKRNAY GIVESVIMMG
SPTPSNAEHW RLMRSVVSGR VVNVFSENDN VLAFLYRTSS LQLGVAGLQK VEGVPGVENL
DVSEMVSGHL RYQYLLGRIL TLTGLQDLDA NEIEREETAL AIEEEQQEKE LQQNQREAGV
KDPKSSAAQE TLNSQAGFGE DARLQKQVEM QTQENMTNHR IQMLDMNDDD YSTPLKDDPL
KHSAL
//