PEPF_ASPNG
ID PEPF_ASPNG Reviewed; 531 AA.
AC P52718;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Serine-type carboxypeptidase F;
DE Short=Proteinase F;
DE EC=3.4.16.-;
DE AltName: Full=CPD-II;
DE Flags: Precursor;
GN Name=pepF;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=7828908; DOI=10.1016/0378-1119(94)90634-3;
RA van den Hombergh J.P.T.W., Jarai G., Buxton F.P., Visser J.;
RT "Cloning, characterization and expression of pepF, a gene encoding a serine
RT carboxypeptidase from Aspergillus niger.";
RL Gene 151:73-79(1994).
RN [2]
RP SEQUENCE REVISION.
RA Schaap P.J., Visser J.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 53-71, AND CHARACTERIZATION.
RX PubMed=1637154; DOI=10.1128/aem.58.7.2144-2152.1992;
RA Dal Degan F., Ribadeau-Dumas B., Breddam K.;
RT "Purification and characterization of two serine carboxypeptidases from
RT Aspergillus niger and their use in C-terminal sequencing of proteins and
RT peptide synthesis.";
RL Appl. Environ. Microbiol. 58:2144-2152(1992).
CC -!- FUNCTION: Removes any amino acid from the C-terminus of a long peptide.
CC Digests preferentially peptides containing a positively charged residue
CC in P1' position, as well as arginine, lysine or phenylalanine in P1
CC position of ester substrate. Catalyzes also peptide synthesis.
CC -!- ACTIVITY REGULATION: Inhibited by DFP, and Hg(Cl)2.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4. Unstable above pH 8.;
CC -!- SUBUNIT: Monomer.
CC -!- INDUCTION: In the following growth conditions: acidic pH, absence of
CC nitrogen or carbon source.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; X79541; CAA56075.1; -; Genomic_DNA.
DR EMBL; L33408; AAB57723.1; -; Genomic_DNA.
DR PIR; S57907; S57907.
DR AlphaFoldDB; P52718; -.
DR SMR; P52718; -.
DR STRING; 5061.CADANGAP00005956; -.
DR ESTHER; aspng-pepf; Carboxypeptidase_S10.
DR MEROPS; S10.006; -.
DR VEuPathDB; FungiDB:An07g08030; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1120907; -.
DR VEuPathDB; FungiDB:ATCC64974_48920; -.
DR VEuPathDB; FungiDB:M747DRAFT_292917; -.
DR eggNOG; KOG1282; Eukaryota.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Protease; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..52
FT /evidence="ECO:0000269|PubMed:1637154"
FT /id="PRO_0000004297"
FT CHAIN 53..531
FT /note="Serine-type carboxypeptidase F"
FT /id="PRO_0000004298"
FT ACT_SITE 211
FT /evidence="ECO:0000250"
FT ACT_SITE 430
FT /evidence="ECO:0000250"
FT ACT_SITE 507
FT /evidence="ECO:0000250"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 53
FT /note="I -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="D -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="N -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="Y -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 59536 MW; 6CDF0EA9E897B550 CRC64;
MLFRSLLSTA VLAVSLCTDN ASAAKHGRFG QKARDAMNIA KRSANAVKHS LKIPVEDYQF
LNNKTKPYRV ESLPDVHFDL GEMYSGLVPI EKGNVSRSLF FVFQPTIGEP VDEITIWLNG
GPGCSSLEAF LQENGRFVWQ PGTYQPVENP YSWVNLTNVL WVDQPVGTGF SLGVPTATSE
EEIAEDFVKF FKNWQQIFGI KNFKIYVTGE SYAGRYVPYI SAAFLDQNDT EHFNLKGALA
YDPCIGQFDY VQEEAPVVPF VQKNNALFNF NASFLAELES IHEQCGYKDF IDQYLVFPAS
GVQPPKAMNW SDPTCDVYDI VNNAVLDPNP CFNPYEINEM CPILWDVLGF PTEVDYLPAG
ASIYFDRADV KRAMHAPNIT WSECSVESVF VGGDGGPEQE GDYSANPIEH VLPQVIEGTN
RVLIGNGDYD MVILTNGTLL SIQNMTWNGK LGFDTAPSTP INIDIPDLMY NEVFIENGYD
PQGGQGVMGI QHYERGLMWA ETFQSGHMQP QFQPRVSYRH LEWLLGRRDT L
