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Database: UniProt
Entry: A0A0A2KVM0_PENIT
LinkDB: A0A0A2KVM0_PENIT
Original site: A0A0A2KVM0_PENIT 
ID   A0A0A2KVM0_PENIT        Unreviewed;       459 AA.
AC   A0A0A2KVM0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=DUF676 domain-containing protein {ECO:0000259|Pfam:PF05057};
GN   ORFNames=PITC_028370 {ECO:0000313|EMBL:KGO71834.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO71834.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO71834.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO71834.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- SIMILARITY: Belongs to the putative lipase ROG1 family.
CC       {ECO:0000256|ARBA:ARBA00007920}.
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:KGO71834.1}.
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DR   EMBL; JQGA01000917; KGO71834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2KVM0; -.
DR   STRING; 40296.A0A0A2KVM0; -.
DR   HOGENOM; CLU_027968_1_1_1; -.
DR   OMA; FCTPHVG; -.
DR   OrthoDB; 48091at2759; -.
DR   PhylomeDB; A0A0A2KVM0; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; IPR007751; DUF676_lipase-like.
DR   InterPro; IPR044294; Lipase-like.
DR   PANTHER; PTHR12482:SF65; ESTERASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G12320)-RELATED; 1.
DR   PANTHER; PTHR12482; UNCHARACTERIZED; 1.
DR   Pfam; PF05057; DUF676; 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:UP000030104};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        274..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..212
FT                   /note="DUF676"
FT                   /evidence="ECO:0000259|Pfam:PF05057"
SQ   SEQUENCE   459 AA;  51176 MW;  BF0BC78D6111508C CRC64;
     MESTSETMLD ISKADHLCVL VHGLWGNPSH LDFIASALRD RYSDDGLYIL CPETNSGNYT
     YDGIEVGGER MVHEIEETLE SLAEKGQKIT KISVIGYSLG GLVARYAIGL LNARGWLDKL
     EPMNFTTFAT PHVGVRAPLK GYKDWIFNVL GPRTISASGR QMWLMDSFRD TGRPLLAVLA
     DPESIFIAGL KKFRQRSVYA NIVNDRLVLF YTSGLSKVNP FQDLENTNIN YVKGYEDVII
     DPDLHVLPPV ERGPETAAGG FWKKVKSVTR SIPLSLLLIA FVPLASVLFL INAGIQSIRS
     SKRIRMHEVG ENGERFGRYR VPVLIQDVQH AMEQAFENAN AIQEPAYLSN SDTEVSEAVP
     EKFASSSVSE SAQNGVGAES ASARRLWTTE ASTHYPKLAL THEQFEIIDS LNAVGIRKYP
     VHIQNHHHSH AAIIVRVEKD GFREGKIVMK HWLDNEFAL
//
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