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Database: UniProt
Entry: K9FQD7_PEND2
LinkDB: K9FQD7_PEND2
Original site: K9FQD7_PEND2 
ID   K9FQD7_PEND2            Unreviewed;      1247 AA.
AC   K9FQD7;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Lipase/esterase family protein {ECO:0000313|EMBL:EKV04948.1};
GN   ORFNames=PDIG_86120 {ECO:0000313|EMBL:EKV04948.1};
OS   Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV04948.1, ECO:0000313|Proteomes:UP000009882};
RN   [1] {ECO:0000313|Proteomes:UP000009882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT   postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(2012).
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:EKV04948.1}.
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DR   EMBL; AKCT01000316; EKV04948.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9FQD7; -.
DR   STRING; 1170229.K9FQD7; -.
DR   eggNOG; KOG1515; Eukaryota.
DR   HOGENOM; CLU_004893_0_1_1; -.
DR   InParanoid; K9FQD7; -.
DR   OMA; PHWVRTE; -.
DR   OrthoDB; 1943592at2759; -.
DR   Proteomes; UP000009882; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR   GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR   CDD; cd09630; CDH_like_cytochrome; 1.
DR   CDD; cd08760; Cyt_b561_FRRS1_like; 1.
DR   Gene3D; 1.20.120.1770; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR015920; Cellobiose_DH_cyt.
DR   InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR   InterPro; IPR005018; DOMON_domain.
DR   InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   PANTHER; PTHR48081:SF35; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   Pfam; PF16010; CDH-cyt; 1.
DR   SMART; SM00665; B561; 1.
DR   SMART; SM00664; DoH; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF49344; CBD9-like; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1247
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003928700"
FT   TRANSMEM        221..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        285..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..150
FT                   /note="DOMON"
FT                   /evidence="ECO:0000259|SMART:SM00664"
FT   DOMAIN          219..341
FT                   /note="Cytochrome b561"
FT                   /evidence="ECO:0000259|SMART:SM00665"
FT   REGION          846..884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1001..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1155..1174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..863
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1009..1031
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1032..1074
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1212..1232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1233..1247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        565
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
SQ   SEQUENCE   1247 AA;  137077 MW;  62F97AC8A889E146 CRC64;
     MIRHNFAWLW AIPALAQVQV HSIHPQGHNE ITYSFNVPDN TAKSGSGPIY FQMNSTRQVQ
     WFALGQGMQM AGANMFIVYT SGNTVTVSPR SGVGEIEPLY NKDAQIKILH GSGVYDGVIT
     ASVRCDTCLK WNGGIENVTS SSSPWIWAVK YGEALNSVSV SEGITQHDDH GVTTIDLKKA
     TGGNSVNPFA QMARASISPS EEDPGFAAFR STVKRKKTAH AVLMVLAFVV MFPFFALGLH
     IFPSKWTVNV HGTFQLLTLA VVMAGFGLGI SLARQIELID SYHTILGMII VPCLVLFQPA
     MGMLQHTFFR KTGRKGPFAY MHRWFGRLMM ILGIINVGLG FKLAQAPRGA VIATSVVAGI
     IAMVYIVIYL HRKLLHNKPT VHVTYDEGIQ IIRQFLFYAS KHPVEDLQAF TRQWVPSPHW
     VRTETITIPD EFLSSAADAV TKQLGPKGVT RVGGEKWWQW RGPSGELKGE WIEMRNHYNQ
     TEGADRHCNR VMLYVHGGAY FFGSVDTHRY MMQRHARKLK GRVFAPEYRL SPQFPFPCGL
     HDCMAAYLWL LKSHEPKEII LAGDSAGGGL ALSMLVIMRD QGIPLPAGAI LISPWVDLTH
     SFPSIIEDNP GDYIPAYGFR HKPSPAWPPP NADDILEMKN LSRQPTVTAE NVKKAIPQPN
     STAEETAIRG YAIHENTPPA AERAYPGQQQ APNPASLHAE PDNIHVVLDG KTVELKDQIQ
     LYTTNQLMSH PLVSPVLQPS LGGLPPLQIL TGGGEMLRDE QFYIAHKAAN PTAYPPSDVY
     LDEYDPTREI LNKYEPTYVQ LQVWDNLCHV APTLSFTRPA KYMFRAISQF GSWALARAQN
     GEVETVDDSA LSAASSNSSE DEDVPGPETA LNSPPGTPGA SCVGKAGDPL PAFHQYMIRQ
     RIDKRGHVFP LDPPSFYPVL KIPPAQIGAI NPLLIRMWLD AKKEWDIRFA KEKLRVQSQR
     LKELAHGFQD FDGECPPPSS LAARRAAPGV LPKRHAKKNH GMMMWSGWGS RHDERRMEME
     TRAEESGRRS TRVSTDAGQA GAWPSTPATN PQIEKTSDQY LTNNKSQSNG YTAVSPDKKE
     EFSNGDSSTE RTSTDLETVS RTLSQKSAGP ILILPEVNNN KFTDENASTR ALVHAAGSLP
     MKSDLSLAQS KYRPASATGS ATSRSEMLSD TTSTVGGDKD SVAYMNMASD TASTQAVIGA
     RGIIAPVTAG ENGCRSTETP SVFSAAGQDS MSHRSEISER EGFKTAD
//
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