ID   PALA_DEBHA              Reviewed;         766 AA.
AC   Q6BLT2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=pH-response regulator protein palA/RIM20;
GN   Name=RIM20; OrderedLocusNames=DEHA2F10912g;
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. May act as a scaffold
CC       protein that recruits the calpain-like protease RIM13 via VPS32 to its
CC       substrate RIM101 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RIM101 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; CR382138; CAG89184.2; -; Genomic_DNA.
DR   RefSeq; XP_460839.2; XM_460839.1.
DR   AlphaFoldDB; Q6BLT2; -.
DR   SMR; Q6BLT2; -.
DR   STRING; 4959.XP_460839.2; -.
DR   EnsemblFungi; CAG89184; CAG89184; DEHA2F10912g.
DR   GeneID; 2903574; -.
DR   KEGG; dha:DEHA2F10912g; -.
DR   VEuPathDB; FungiDB:DEHA2F10912g; -.
DR   eggNOG; KOG2220; Eukaryota.
DR   HOGENOM; CLU_007181_0_0_1; -.
DR   InParanoid; Q6BLT2; -.
DR   OMA; SEWIHHM; -.
DR   OrthoDB; 550620at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
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..766
FT                   /note="pH-response regulator protein palA/RIM20"
FT                   /id="PRO_0000218878"
FT   DOMAIN          4..395
FT                   /note="BRO1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT   REGION          740..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          544..581
FT                   /evidence="ECO:0000255"
FT   COILED          633..692
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        740..758
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  88649 MW;  674788FDF3D4D094 CRC64;
     MNTNLLYIPY RETDIIDLGN ELRNIIKMEY FQPSSNFDRD LQAVRNLRNN ISNLKNEQVN
     NNDETVCVQY YHQLSNVIKK FPDECVEFSW YGTLGYGRSG PTRSRSLRIE QLNILYQLGS
     YFSQAALMES RYSDEGLKKS CSYLQAAAGC FNSMILQIQK ENEKETGMIR IPRDLQPETL
     QFLKSLMIAQ AQETIWQKSL ASGMKDSVIA RLSIQTSEYY STAAKYGNSS EFIKLEWINH
     VTVKQFHFKA AAHYRVSILN HEGFKYGEQV ASLQVALSSC DSAFRKKKYV NDFVIEDLQG
     LTETIKSTLR VAEKDNDLVY LKPVPKENDL APIPGASLVK PILPPAIESF DDSSVLFKEL
     LPYLIVQVGQ AYRERQDSFI RDSFIDPIQS LNKIMYKFIT ERNLPASIDT IQKPENLPES
     IIQHSQEIIS YGGTKLIEDS LNEIAKLTLE SRHILEGCQE RLKIEADEDD IMRERQGSQR
     WARPKSSEAS SEFINKINKM EQYLDQAKEG DQFIISQYHE IEPYLQLYCG GYKELIQFIP
     NSTYVKLDTK INEIIIKLRE LINEVSRIEN QRKQFLTRIE IKARNNNILP SIIDSFKKKQ
     RKLYEENAAI DERSFEDVYA KHITMFNSDL RFLEDSKHAQ IALEGNIDDL NQEFESEYQH
     TNNESQYKRQ EVLQTLENVY TKYLELISNL NEGSKFYSDF IIKSNSVLKE CDEYVYHRRV
     EGRELEMFLN NQAVPVESVG SQQSAPDFPP QPMGGTWNPN NGIKFG