ID   PALB_EMENI              Reviewed;         847 AA.
AC   Q00204; C8VUJ8; Q5BGS4;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Calpain-like protease palB;
DE            EC=3.4.22.-;
DE   AltName: Full=Cysteine protease palB;
GN   Name=palB; ORFNames=AN0256;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=7499363; DOI=10.1074/jbc.270.48.28519;
RA   Denison S.H., Orejas M., Arst H.N. Jr.;
RT   "Signalling of ambient pH in Aspergillus nidulans involves a cysteine
RT   protease.";
RL   J. Biol. Chem. 270:28519-28522(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [4]
RP   FUNCTION.
RX   PubMed=3016485; DOI=10.1007/bf00333978;
RA   Caddick M.X., Brownlee A.G., Arst H.N. Jr.;
RT   "Regulation of gene expression by pH of the growth medium in Aspergillus
RT   nidulans.";
RL   Mol. Gen. Genet. 203:346-353(1986).
RN   [5]
RP   FUNCTION.
RX   PubMed=15686555; DOI=10.1111/j.1365-2958.2004.04472.x;
RA   Bignell E., Negrete-Urtasun S., Calcagno A.M., Haynes K., Arst H.N. Jr.,
RA   Rogers T.;
RT   "The Aspergillus pH-responsive transcription factor PacC regulates
RT   virulence.";
RL   Mol. Microbiol. 55:1072-1084(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, yielding the 53 kDa 'open'
CC       conformation intermediate protein, which is committed to further
CC       processing. Required for virulence in invasive pulmonary aspergillosis
CC       (IPA). {ECO:0000269|PubMed:15686555, ECO:0000269|PubMed:3016485,
CC       ECO:0000269|PubMed:7499363}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z54244; CAA91013.2; -; Genomic_DNA.
DR   EMBL; AACD01000005; EAA66129.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF89869.1; -; Genomic_DNA.
DR   RefSeq; XP_657860.1; XM_652768.1.
DR   AlphaFoldDB; Q00204; -.
DR   STRING; 162425.CADANIAP00002468; -.
DR   MEROPS; C02.008; -.
DR   EnsemblFungi; CBF89869; CBF89869; ANIA_00256.
DR   EnsemblFungi; EAA66129; EAA66129; AN0256.2.
DR   GeneID; 2876035; -.
DR   KEGG; ani:AN0256.2; -.
DR   VEuPathDB; FungiDB:AN0256; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   HOGENOM; CLU_006770_1_0_1; -.
DR   InParanoid; Q00204; -.
DR   OMA; CSTFAPD; -.
DR   OrthoDB; 343870at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0000815; C:ESCRT III complex; IMP:AspGD.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISA:AspGD.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0071467; P:cellular response to pH; IMP:AspGD.
DR   GO; GO:0042318; P:penicillin biosynthetic process; IMP:AspGD.
DR   GO; GO:1900198; P:positive regulation of penicillin biosynthetic process; IMP:AspGD.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IMP:AspGD.
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..847
FT                   /note="Calpain-like protease palB"
FT                   /id="PRO_0000207742"
FT   DOMAIN          1..84
FT                   /note="MIT"
FT   DOMAIN          116..436
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        366
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        386
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   847 AA;  94129 MW;  36A889BADEB32A39 CRC64;
     MSRTSSAPSQ KSLISRALKA ERDVITASSQ SQALDAAIDA AEHYMKALAL TSSSKDRNVL
     DAKCKEWLTR AEKIKGSEDW RSVAQSRRSR LRTPASTRKL TTREDIILLQ GAKLNGFIFP
     PWKAEPSLTE FETGTNGDVL FTDKPDLHLS NLQRDIFAGW KRPHELLSGQ VDDAGMPLNP
     VMTVSGNTDL VQDVLTDCSV VASLCATTSR SERGLDDTLL PIVYPCIHNS MKSDISPSGK
     YIFRFYFNGC FRKVVIDDRL PSSKTSRSLY MIDRNHRNFM WPALVEKAYL KLRGGYEFPG
     SNSGTDLWVL TGWIPEQVFL HSDEVTADQI WSDLFKSFHS GDVLLTIGTG KLTEREQKEL
     GLVSEHDYAI LDMKELKGRR QFLIKNPWAG TDAVYPALFA DPGPFPNSPF LSPGTFWMDC
     EMVLQNFENL YLNWNPGIFA YQEDIHFTWD LSTGKGMAGC FVKNPQFSVY TERGGVVWLL
     LGRHLRTIES RASEEDERFG FISIYVFKGG KRVALSDGAL HRGPYVDSPN TLMKLDVPPR
     STYTAVVSEE SLPRVSQNFT ISAFSDSPVR ISHAPNKYIC VTKVQGSWTP TTAGGNAESA
     RYSLNPQFSI VLSDPTDISI VLEPSDQELA THVKLFWSGG KRIARVRSRD IVADSGDYRR
     GGSLVEKQDL DPGEYTIVVS TFAPDQYGSF TLWVSTNITC EVTQLPSEAA GRRAVLSDIG
     VLLPGQDRML APLTTPRLTR VKLIARSRES RIGNRPVGPS PLLMTVELGQ GPYKEILATS
     EDGDHSDSIS GVRVEDFDLQ PGLEERGGVW IVLERIGGPG GQVEDHFEVE ALGEERVEIG
     EWIVEDA