ID   PALA_NEUCR              Reviewed;         854 AA.
AC   Q7S532;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=pH-response regulator protein palA/prr-1;
GN   Name=prr-1; Synonyms=rim20; ORFNames=NCU05876;
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. May act as a scaffold
CC       protein that recruits the calpain-like protease palB/cpr-8 via
CC       snf7/vps-3 to its substrate pacc-1 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with pacc-1 by binding to its two YPX[LI] motifs.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the palA/RIM20 family. {ECO:0000305}.
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DR   EMBL; CM002242; EAA30631.2; -; Genomic_DNA.
DR   RefSeq; XP_959867.2; XM_954774.2.
DR   AlphaFoldDB; Q7S532; -.
DR   SMR; Q7S532; -.
DR   STRING; 5141.EFNCRP00000005796; -.
DR   EnsemblFungi; EAA30631; EAA30631; NCU05876.
DR   GeneID; 3875999; -.
DR   KEGG; ncr:NCU05876; -.
DR   VEuPathDB; FungiDB:NCU05876; -.
DR   HOGENOM; CLU_007181_0_0_1; -.
DR   InParanoid; Q7S532; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; IEA:InterPro.
DR   Gene3D; 1.25.40.280; -; 1.
DR   InterPro; IPR025304; ALIX_V_dom.
DR   InterPro; IPR045251; BRO1-like.
DR   InterPro; IPR004328; BRO1_dom.
DR   InterPro; IPR038499; BRO1_sf.
DR   PANTHER; PTHR23030; PTHR23030; 1.
DR   Pfam; PF13949; ALIX_LYPXL_bnd; 1.
DR   Pfam; PF03097; BRO1; 1.
DR   SMART; SM01041; BRO1; 1.
DR   PROSITE; PS51180; BRO1; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Reference proteome.
FT   CHAIN           1..854
FT                   /note="pH-response regulator protein palA/prr-1"
FT                   /id="PRO_0000218882"
FT   DOMAIN          5..402
FT                   /note="BRO1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT   REGION          739..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..854
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          632..699
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        747..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..782
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..844
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   854 AA;  96904 MW;  1C35E39B61AE42DC CRC64;
     MTTTHVLSLP FRKSTQLSLS RAIQQYISAK YDQHPDMFRH DLDTIDALRR DAINVREAHP
     SGIRKLQMYA AQLVWIGGKF PIDVGADFTW YPALGYHTEH PLVQNNLKYE LMNVLYNLAA
     LYSQLAVASN RNSTEGLKTA ASWFSHSAGV LTHIKTQVLP ELRMPSPPDD MDETTLESLI
     QLFLAEAQEC YWQKAVMDGY KDASIAKLAA RVSDLYNEAG EAAMRSEAIS SAWIHHMSAK
     HHHFAAAAQF RAASDCLERK KYGEEIARLR DAVACVNEGL KETRGGYLSK AVVEDLQGLK
     RRLEEDLKRA EIDNDRVYLH IVPPKTELKR LDRANMAVAR VPPQVAKPYE FLGDPSAEFG
     PALFTKLVPF AVHVAVSIYE ERRDRLVNNS IISELESMTS QLHEILSSLN LPGSLQALEK
     PLGLPGTLVQ HADEIRQADA LYRLQQGLTD IDKLCSSDLA IFEEGRSLLL AEEEEDSRLR
     LKYGTERWNR PQSRQDPSPN GGTKLWRQAQ DIEGYFGSST ASDQVVREKF NAVRDTLTIL
     AGSDRSIMDF IPNSRRTDIP ESLKPALGRL RSAYNDVQRL ESRRRKRVES LRARSRADDI
     KPDILVEAAR LERAYPTTAI ATAHFEDFFE KRLDRLYESE LEAVERDKQE QEKIVQEVKR
     ANKEFEAQKR QVDRAGGGNR EREEALQKLD AAYYKYKEIV SNVEVGRKFY NDLSQIVEQW
     RGLVRGWVSE RRRDARSLEE EINMPPLSSL NMHQSSFSYQ QQQHHQQPPP PPPQIPFPEP
     IQPHQPIVEQ AHIQSWADNV PQQQPKPVAP GAWAPNMGIK FGSPVAQGQQ HQQEQGQPGP
     VNATWDPSQG IRFG