ID   PALB_NEUCR              Reviewed;         932 AA.
AC   Q7RZP7; U9W3D3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 3.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Calpain-like protease palB/cpr-8;
DE            EC=3.4.22.-;
DE   AltName: Full=Cysteine protease 8;
GN   Name=cpr-8; Synonyms=rim13; ORFNames=NCU00317;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Required for the proteolytic cleavage of the transcription
CC       factor pacc-1 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; CM002238; ESA43337.1; -; Genomic_DNA.
DR   RefSeq; XP_011393811.1; XM_011395509.1.
DR   AlphaFoldDB; Q7RZP7; -.
DR   SMR; Q7RZP7; -.
DR   STRING; 5141.EFNCRP00000000354; -.
DR   MEROPS; C02.008; -.
DR   EnsemblFungi; ESA43337; ESA43337; NCU00317.
DR   GeneID; 3873926; -.
DR   KEGG; ncr:NCU00317; -.
DR   VEuPathDB; FungiDB:NCU00317; -.
DR   HOGENOM; CLU_006770_1_0_1; -.
DR   InParanoid; Q7RZP7; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; 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   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..932
FT                   /note="Calpain-like protease palB/cpr-8"
FT                   /id="PRO_0000207744"
FT   DOMAIN          96..419
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   REGION          890..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        346
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        366
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   932 AA;  101464 MW;  70F6A8297F129747 CRC64;
     MEARALEHER RLAESHGQEA LKHAIAAAEI YMRAAEKAAN PKDRNRLQRK CSDLIALGER
     LKANAKSAAT SARSPVPEST RTLTIAEKTL LLKSSKLHGN IFPPWEKTPA SDEFAASKAA
     DGCFTDHSPF TLSPEQQDIF AGWKRPHEIF MDVPERGVDV FMTATESIDL GQDLATDCSV
     VASLCAAVRQ FGPRTGSLLS SLMYPYDDDV KRPAVSQNGK YIFRMYFNGC WRKVLIDDRL
     PTSSSERTLY VVDRRNPYLI WPALIEKAYL KIRGGYDFPG SNSGTDLHAL TGWIPEQIFL
     QTDDIELNET WSRIKTAYEQ GNALVTLGTG KFSREEERTL GLVREHDYAV LDLRNDGNNR
     LFLVKNPWRD SLVWTGVGST ATSSTDRSGS PEESMSNTFW MTFEDVLQHF DSLYVNWSPS
     LFRFRQDHHF TWTIPPKAEE LVFTQNPQYS ILSHTGSPVW ILLNRHWQDS ELDILRERKQ
     EHDFHQPLKS LGYMSLSLFA SHPPGTRIPL SEGSHHALHQ GPFVDSPNTL LRYSPTPGVA
     QTLVIAQSDL PLPSYSFTLS FFSNSPLTIS PASDPLPYNE TITGAWTRRT AGGSTVYPSY
     VTNPQYALTL TRPSPLSLVL STERADNLPV HIAVLYSNGG QRVTAVVGRD LICSSAEYQR
     GCTFASTLPS SNTSNVTSSV ASNNHGHTSS SLIDPGTYTI VLSTYEPGQT GRYSLRVSAA
     CPFTIEPILS DAAGRLRTPA PSPATFRQGE GRVRARVDVA RLTRASVLAR SVKTGSTTQK
     TAMVRVALEL GTIEGRKRVL ASTASGGGGE LAASLSNLSL SERLGGIGGI GGGHIHGGQG
     TTEGDGYSAK GEFADASLGL RTREVDLDPD VIRVYGGLWL VVEQIGGGGQ GHVTEGSDDD
     GGGGGGGGGG VHVEISSDGV VSIGEWEVAD ED