PALB_ASPOR
ID PALB_ASPOR Reviewed; 854 AA.
AC Q9Y6Z8; Q2URN3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Calpain-like protease palB/RIM13;
DE EC=3.4.22.-;
DE AltName: Full=Cysteine protease palB;
GN Name=palB; Synonyms=palBory; ORFNames=AO090005000756;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16232641; DOI=10.1016/s1389-1723(99)80223-0;
RA Futai E., Sorimachi H., Jeong S.-Y., Kitamoto K., Ishiura S., Suzuki K.;
RT "Aspergillus oryzae palBory encodes a calpain-like protease: homology to
RT Emericella nidulans PalB and conservation of functional regions.";
RL J. Biosci. Bioeng. 88:438-440(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10779397; DOI=10.1006/fgbi.1999.1179;
RA Yaver D.S., Lamsa M., Munds R., Brown S.H., Otani S., Franssen L.,
RA Johnstone J.A., Brody H.;
RT "Using DNA-tagged mutagenesis to improve heterologous protein production in
RT Aspergillus oryzae.";
RL Fungal Genet. Biol. 29:28-37(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Required for the proteolytic cleavage of the transcription
CC factor pacC in response to alkaline ambient pH. Probably is the
CC signaling protease that mediates the first proteolytic cleavage within
CC the signaling protease box of pacC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB020321; BAA77364.1; -; Genomic_DNA.
DR EMBL; AF133087; AAD28472.1; -; Genomic_DNA.
DR EMBL; AP007151; BAE55782.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y6Z8; -.
DR SMR; Q9Y6Z8; -.
DR STRING; 510516.Q9Y6Z8; -.
DR MEROPS; C02.008; -.
DR EnsemblFungi; BAE55782; BAE55782; AO090005000756.
DR VEuPathDB; FungiDB:AO090005000756; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF49758; SSF49758; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..854
FT /note="Calpain-like protease palB/RIM13"
FT /id="PRO_0000207737"
FT DOMAIN 2..83
FT /note="MIT"
FT DOMAIN 118..437
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT ACT_SITE 199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT ACT_SITE 364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT ACT_SITE 384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT CONFLICT 3..17
FT /note="RPNASAQKSFITQAL -> SILHAALVKILPGLP (in Ref. 3;
FT BAE55782)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 854 AA; 95470 MW; 48055DAD2E814567 CRC64;
MSRPNASAQK SFITQALKAE RDVSSATSQR QALEAAIDAA EHYMKALNLA SVQKDKHALD
AKCKEWLTRA EKIKESKDWQ AAARFHDKTV PEPRLPVSTR KLTTREEIIL LEGAKLNGFI
FPPWSTSPGS DEFKREDGES PFTDKPDLHL SYPQRKVFDG WKRPSELLAK DTEDVYTKVV
PVMSVPGKTD LVQDMLTDCS VVASLCATTS MLERGQCTHF LPMIYPSRGS SQPSPSGKYI
FRFYFNGCFR KVIIDDRLPS SKTSRSLHVI DRKNPNFLWP ALVEKAYLKL RGGYDFPGSN
SGTDLWVLTG WIPEQVFLHN DDVTGDQLWK RLYRSFHQGD VLLTIGTGEL TEREQRELGL
VSEHDYAILD MKESKGRRQL LVKNPWAGAD TAPGDNGSLS ASQDLPHNPP SFEPGTFWMD
CEKLLQHFEN LYLNWNPEIF KYREDVHFTW DLNNGRGVAG CFVNNPQFAV STENGGIVWL
LLGKHFRTTG QPERPLDEYQ ANEESAFISI YVFNADGKRV SLSDGALHRG PYVDSPNTLM
RLEMPPRTTY TVVVSEQSLP SLNQNFTLSA FSTCPVRMAK AQDKYMCVRK IQGSWTPSTA
GGNAESSRYP LNPQFRLEIE NDTDVSLLLE CPNTELATHV KLFWSNGNRV SRVRSRDIIA
DSGDYRRGGS LVEKKALEPG SYTIVCSTFA PDQLGRFTLW VSSLVPCKTS PLPPEAAGRR
TVISDIGVLP PGRDRMLASL QVPRLTRIKL ITRSRQSIIG SHPVGPSPVL MTVELGQGPY
KQILATSEDG THSDAVSGVR VEDFDLQPGL EESGGIWIVI ERIGGPGGQV EDHFEVEALA
EERVEIGEWI LEDA
