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CARP2_RHINI
ID   CARP2_RHINI             Reviewed;         391 AA.
AC   P43231;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Rhizopuspepsin-2;
DE            EC=3.4.23.21;
DE   AltName: Full=Aspartate protease;
DE   Flags: Precursor;
OS   Rhizopus niveus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 4810 / AS 3.4817;
RA   Horiuchi H., Nakamura H., Okazaki T., Yano K., Takagi M.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity similar to that
CC         of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots
CC         milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but
CC         does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of
CC         insulin.; EC=3.4.23.21;
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; X56964; CAA40284.1; -; Genomic_DNA.
DR   AlphaFoldDB; P43231; -.
DR   SMR; P43231; -.
DR   MEROPS; A01.012; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Disulfide bond; Hydrolase; Protease; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..68
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025885"
FT   CHAIN           69..391
FT                   /note="Rhizopuspepsin-2"
FT                   /id="PRO_0000025886"
FT   DOMAIN          84..388
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        285
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        115..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        319..352
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  41234 MW;  3F34230659DEA960 CRC64;
     MKLTLISSCV ALAFMALATE AAPSGKKLSI PLTKNTNYKP SAKNAIQKAL AKYHRFRTTS
     SSNSTSTEGT GSVPVTDYYN DIEYYGKVTV GTPGVTLKLD FDTGSSDLWF ASTLCTNCGS
     SQTKYNPNQS STYAKDGRTW SISYGDGSSA SGILGTDTVT LGGLKITKQT IELAKREATS
     FQSGPSYGLL GLGFDTITTV RGVKTPVDNL ISQGLISKPI FGVYLGKESN GGGGEYIFGG
     YDSSKYSGSL TTIPVDNSNG WYGITIKGTT IGSSKVSSSF SAILDTGTTL LILPNNVASA
     VARSYGASDN GDGTYTIDCD TSSFKPLVFS IGSSTFEVPA DSLVFEQDGS TCYAGFGYGD
     YDFAIFGDVF LKNNYVVFNQ EVPEVQIAPI A
 
 
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