ID   PALB_DEBHA              Reviewed;         764 AA.
AC   Q6BH66;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Calpain-like protease palB/RIM13;
DE            EC=3.4.22.-;
DE   AltName: Full=Cysteine protease RIM13;
GN   OrderedLocusNames=DEHA2G20988g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Required for the proteolytic cleavage of the transcription
CC       factor RIM101 in response to alkaline ambient pH. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR382139; CAG90965.2; -; Genomic_DNA.
DR   RefSeq; XP_462455.2; XM_462455.1.
DR   AlphaFoldDB; Q6BH66; -.
DR   STRING; 4959.XP_462455.2; -.
DR   MEROPS; C02.008; -.
DR   EnsemblFungi; CAG90965; CAG90965; DEHA2G20988g.
DR   GeneID; 2905404; -.
DR   KEGG; dha:DEHA2G20988g; -.
DR   VEuPathDB; FungiDB:DEHA2G20988g; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   HOGENOM; CLU_023416_0_0_1; -.
DR   InParanoid; Q6BH66; -.
DR   OMA; AGWIPEH; -.
DR   OrthoDB; 343870at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR022682; Calpain_domain_III.
DR   InterPro; IPR036213; Calpain_III_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; SM00230; CysPc; 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..764
FT                   /note="Calpain-like protease palB/RIM13"
FT                   /id="PRO_0000207741"
FT   DOMAIN          95..368
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        336
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   764 AA;  88947 MW;  EBBA2B29AAAA0E81 CRC64;
     MEEKELRQDL YECVSLLDVA HFNCCLGNEN NAKQQCLEIV KILNRLSKTK AFKEGYHSII
     KDISSYTLKF YDSIDKGNHF TYSEKIMWLS SKLYGEFYPP LTVYSHKLDS FHSYLLPIQK
     VIKEKTDILP LPESLNAHYE QVDIKNWTLD YNALSELYQD LLTNCSFVSS LLSIVELDRK
     DLLENLISPR QDSSIFKCQL YFNGSSRLVT IDNTLPFLND SNRNLTINSN ENLYWPALVE
     KAYLKVLGSG YKFEGSNMAI DTYMLTTWIP EIVPINNSKL YDCDDVWENY LSKSVLLGIG
     TGKLSVELSK KLNFISGHDY LVTSFDPITH TIVLKNPWIE NDNSYKRTLT ISDQDLHHFK
     YFYINWNPNA FFKYKFHMTF IYNVKDNTGT HMYQKPQFSL LNPTEDSQNV WLLLEKHLPL
     KNFSEQLINI LIYETQLGDK VIVSNQCIRA NKDSSTNSRL MLLKFTMKPK QAYTIVISST
     IANTFTLNMY NNISRDFTFT KAKFKYPTTI PTFKDKWTSD NSGGNWSLST YIDNPQYDIE
     VKTLPTNIMI GLFSEFKDKF VNFHIFQSDP SGKGHRIRLF DKSKLLVNEK YSMTYQFEDF
     KSLQPGFYKI VASAFDNNLN GAFELLAIHD SPPNNISITK IHPSLGLFLQ KKEFDWNSSN
     RFKLYFKATQ FSSRFTFHLK HYSHINKNTE SLSDYRPFIR GSIFDAENSQ PIQINEEWND
     SLYGLFIDCD IQKPKTYILL VERFESGSGR CKVDIGCNRK FNIL