BRO1_ASPFU
ID BRO1_ASPFU Reviewed; 976 AA.
AC Q4X0Z5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Vacuolar protein-sorting protein bro1;
DE AltName: Full=BRO domain-containing protein 1;
GN Name=bro1; ORFNames=AFUA_2G11760;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Involved in concentration and sorting of cargo proteins of
CC the multivesicular body (MVB) for incorporation into intralumenal
CC vesicles. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BRO1 family. {ECO:0000305}.
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DR EMBL; AAHF01000001; EAL93470.1; -; Genomic_DNA.
DR RefSeq; XP_755508.1; XM_750415.1.
DR AlphaFoldDB; Q4X0Z5; -.
DR SMR; Q4X0Z5; -.
DR STRING; 746128.CADAFUBP00002689; -.
DR PRIDE; Q4X0Z5; -.
DR EnsemblFungi; EAL93470; EAL93470; AFUA_2G11760.
DR GeneID; 3513086; -.
DR KEGG; afm:AFUA_2G11760; -.
DR VEuPathDB; FungiDB:Afu2g11760; -.
DR eggNOG; KOG2220; Eukaryota.
DR HOGENOM; CLU_003661_0_0_1; -.
DR InParanoid; Q4X0Z5; -.
DR OMA; ANHKQSA; -.
DR OrthoDB; 550620at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
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; Cytoplasm; Endosome; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..976
FT /note="Vacuolar protein-sorting protein bro1"
FT /id="PRO_0000218860"
FT DOMAIN 5..387
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REGION 743..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 748..775
FT /evidence="ECO:0000255"
FT COMPBIAS 773..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..804
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..936
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 108306 MW; 9694D2749259F78D CRC64;
MVQSPMLSCP LKQTNEIDWI RPLKDYIRQS YGEDPERYNQ ECATLNRLRQ DMRGAGKDSA
TGRDLLYRYY GQLELLDLRF PVDENHIKIS FTWYDAFTHK PTSQYSLAYE KASIIFNISA
VLSCHAANQN RAEESGLKTA YHSFQASAGM FTYINENFLH APSTDLNRET VKTLINITLA
QAQEVFLEKQ VTDQKKAGFL AKLASQAAYL YSQAAEGIQE YAKGVFDKSW TIVVQAKAAH
MASVASYYQA LADSESNSHG VAIARLQLAD KNSTAAMGWA NLVDTIKYHQ ANVQVKLATF
VKDNDFIYHQ PVPNEAGLSA VAKLPAAKAI PVSELYQGQD IQRIIGPDIF QKLVPMSVTE
TASLYDEEKA KLIRAETEKV ETADSEMAAS LDYLKLPGSL NILKGGMDQE MTVDDEFRQW
CQELAGHQSF AKAFDTLQDR KGEILSQLDR CSKQLDLEES VCEKMRSKYG ADWSQQPSAR
LNSTLRSDIR TYRDTINEAS ASDSQLLATF RQYETDFDEM RSAGETNEAD VLFQRAMIKA
GSKHGKGRNG VGSPYASTQE GSLLDDVYDE GSLSVAEQIA RVESILKKLN LVKRERSQVL
KDLKEKVHND DISNVLILNK KSIAGQESQL FETELEKFRP HQNRLLQANH KQAALMKELT
KVYGDLLQDK RVRSEQSKYE AITRQRNTVM ARYKKIYDAF NGLLSGIAQA QTFYTEMVET
VESLKKNVET FINNRRSEGA QLLGQIEREK AGTATDQEDR EREKLRQLME RLSTEPKPTS
TPLPSTAPSK AKSPPPPVKA PGYPGPGIAS PQMSPHFAPG VAGQQHGIPL SHSPAPYGQY
VAPPSGVSYM QGQPFQQGAA APLSEGYNPM AYPAPTSISP PPSQQYYSST PAPYSGYSNP
APPNAPSQFM PQGYVPPPPP PRPQQPSYPP STGPYPSGPG GYAQSRPYGT SQHHKTPSQS
QSSSSTDPWA GLNAWK
