ID   PALA_EMENI              Reviewed;         847 AA.
AC   P79020; C8V8Z2; Q5B529;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=pH-response regulator protein palA/RIM20;
GN   Name=palA; ORFNames=AN4351;
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].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=9045850; DOI=10.1128/jb.179.5.1832-1835.1997;
RA   Negrete-Urtasun S., Denison S.H., Arst H.N. Jr.;
RT   "Characterisation of the pH signal transduction pathway gene palA of
RT   Aspergillus nidulans and identification of possible homologues.";
RL   J. Bacteriol. 179:1832-1835(1997).
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   INTERACTION WITH PACC AND VPS32.
RX   PubMed=12588984; DOI=10.1128/mcb.23.5.1647-1655.2003;
RA   Vincent O., Rainbow L., Tilburn J., Arst H.N. Jr., Penalva M.A.;
RT   "YPXL/I is a protein interaction motif recognized by Aspergillus PalA and
RT   its human homologue, AIP1/Alix.";
RL   Mol. Cell. Biol. 23:1647-1655(2003).
CC   -!- FUNCTION: Required for the proteolytic cleavage of the transcription
CC       factor pacC in response to alkaline ambient pH. May act as a scaffold
CC       protein that recruits the calpain-like protease palB via vps32 to its
CC       substrate pacC (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:3016485}.
CC   -!- SUBUNIT: Interacts with pacC by binding to its two YPX[LI] motifs.
CC       {ECO:0000269|PubMed:12588984}.
CC   -!- SIMILARITY: Belongs to the palA/RIM20 family. {ECO:0000305}.
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DR   EMBL; Z83333; CAB05920.3; -; Genomic_DNA.
DR   EMBL; AACD01000075; EAA60512.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF77701.1; -; Genomic_DNA.
DR   RefSeq; XP_661955.1; XM_656863.1.
DR   AlphaFoldDB; P79020; -.
DR   SMR; P79020; -.
DR   ELM; P79020; -.
DR   STRING; 162425.CADANIAP00006107; -.
DR   PRIDE; P79020; -.
DR   EnsemblFungi; CBF77701; CBF77701; ANIA_04351.
DR   EnsemblFungi; EAA60512; EAA60512; AN4351.2.
DR   GeneID; 2872147; -.
DR   KEGG; ani:AN4351.2; -.
DR   VEuPathDB; FungiDB:AN4351; -.
DR   eggNOG; KOG2220; Eukaryota.
DR   HOGENOM; CLU_007181_0_0_1; -.
DR   InParanoid; P79020; -.
DR   OMA; SEWIHHM; -.
DR   OrthoDB; 550620at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0000815; C:ESCRT III complex; IMP:AspGD.
DR   GO; GO:0071467; P:cellular response to pH; IMP:AspGD.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; IEA:InterPro.
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:1900376; P:regulation of secondary metabolite biosynthetic process; IMP:AspGD.
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   1: Evidence at protein level;
KW   Coiled coil; Reference proteome.
FT   CHAIN           1..847
FT                   /note="pH-response regulator protein palA/RIM20"
FT                   /id="PRO_0000218879"
FT   DOMAIN          4..397
FT                   /note="BRO1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT   REGION          763..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          256..312
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        768..799
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..847
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  94769 MW;  D5707F68A5AF826A CRC64;
     MASNILQIPF RRSHTVSLST ALTQYISTKY DQRPDMFADD LLIIDRLRNE AINVQEPHVS
     GISRLVTYAA QLKWLGGKFP VDVGVEFPWY PAFGFNTSRP VSQDNIRFEL ANVIFNLAAL
     YSQLAFAVNR TTTDGLKQAC NYFCQAAGIL AHLRTDIVPD MRSAPPEDMD EMTLRSLEEL
     LLAQAQECFW QKAVMDGLKD ASIARLAGQV SDFYGDACDH AVKSNAISPE WIHHMTAKQH
     HFAAAAQYRQ SLDCLEKRKY GEEVARLRDA VACVNEALKE SRWINRTVLG DLQGLKNRVT
     EDLKRAEKDN DMIYLNPVPP KSELKLIDRA CMVAAKAPSQ VTDAISMLGE KGPLGQPLFS
     KLVPYAVHIA ASIYSDRRDR LVNERIIGEL ENMTDKLRDL LSSLNLPGSL QALEKPLGLP
     PSLVAHAEEM RQQDGLNRLR KSLLDIAKVK SNDRAVYTEG VELLAAEKAE DDASRRKFGT
     DRWTREASEA AAPKLYTTAR EIDGYFTSAQ SSDNLVEQKL HDSEAVFRVL TGTNRDLEAF
     VPSSRRATIP PEVEREVSRL RSCISEVNRL ESRRKRKAQA VKDKARADDI SSALVREAAR
     LEREFPMQAI QASQFEDLFE SRLRDYDVDL DMVAQEMHDQ DQIVAQVRDA NRAFTRAHTG
     DASTKEREKA LQELENGYLK YKEIISNIEV GRKFYNDLAK IVGRFRDDVK AFVHKRRMEA
     SQLEQDISSV AAMASLNISP IRQPPQQTVV SAPVSVSAAA SVPAPTHFNP VKPQPQPPSQ
     AIPPQSQPQP QPQPLRTPLT APQPTRSVPQ VTPGMWSPEM GIRFGPGGTT AQQSQQTWDP
     SKGMKFS