ID A0A319FJY0_ASPSB Unreviewed; 1550 AA.
AC A0A319FJY0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=BRO domain-containing protein 1 {ECO:0000256|ARBA:ARBA00041284};
GN ORFNames=BO78DRAFT_405985 {ECO:0000313|EMBL:PYI08243.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI08243.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI08243.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI08243.1,
RC ECO:0000313|Proteomes:UP000248423};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endosome {ECO:0000256|ARBA:ARBA00004177}.
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DR EMBL; KZ826336; PYI08243.1; -; Genomic_DNA.
DR STRING; 1448318.A0A319FJY0; -.
DR Proteomes; UP000248423; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR CDD; cd09242; BRO1_ScBro1_like; 1.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR CDD; cd09237; V_ScBro1_like; 1.
DR Gene3D; 1.20.120.560; alix/aip1 in complex with the ypdl late domain; 1.
DR Gene3D; 1.20.140.50; alix/aip1 like domains; 1.
DR Gene3D; 1.25.40.280; alix/aip1 like domains; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR025304; ALIX_V_dom.
DR InterPro; IPR045251; BRO1-like.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR038499; BRO1_sf.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR23030; PCD6 INTERACTING PROTEIN-RELATED; 1.
DR PANTHER; PTHR23030:SF45; VACUOLAR-SORTING PROTEIN BRO1; 1.
DR Pfam; PF13949; ALIX_LYPXL_bnd; 1.
DR Pfam; PF03097; BRO1; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM01041; BRO1; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS51180; BRO1; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00546}.
FT DOMAIN 83..147
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 237..318
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT DOMAIN 556..957
FT /note="BRO1"
FT /evidence="ECO:0000259|PROSITE:PS51180"
FT ZN_FING 237..318
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1373
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1497
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1550 AA; 167939 MW; 6F25D148C7BDA823 CRC64;
MSATSAAMPK AAALPARLLR TSRQCSKQSP AASVCSATPV RSYHVSTAPS TSQRLRDGVR
SKPNSFLSSR VFHTTAPLGA ISDPYKVLGV DKGASAADIK KAYYGMAKKY HPDTNKEPGA
KEKFSEAQSA YEVLSDPKKR ENFDRFGSAA FDQNGGFDPS GGNPFAGAGG FHGFGGGFGG
GFPGGFSADI NFEDLFGAFT GGARRSGRGR RSPFQEILVG EDIEVQTNIS FMEAAKGTSK
DIVITPLKEC GTCDGDGLKK GAKRSQCRQC NGSGTRVHMM QGGFQVAATC DACGGAGMSV
PRGSECGSCN GNGVVRDRKT VQVDIPGGVE DGMRLRVTGE GDAPPTGTAA APGSRTQRGD
LYVSIRVSPD HRFSRSGSDI LYTASIPLTT ALLGGEVTVP TLDGEVKVKV GTGTGTGDRI
TLSGMGMKKL SGRSKAFTPT GDLKVEFKVA MPKYLTGNQR TILEVLADEM GDKSARRVMD
IPRDGSSPSD SSATSDPSKN EGFLKSAWHK LMHHTKQSGS EGSTSDSSKK DTGDAKKPDG
EKNSPLLPRN KMVESPMISC PLKQTNEIDW IRPLKDYIRQ SYGEDPERYS SECATLNRLR
QDMRGAGKDS ATGRDLLYRY YGQLELLDLR FPVDENHIKI SFTWYDAFTQ KPTSQYSLAF
EKASIIFNIS AVLSCHAANQ NRAEDTGLKT AYHSFQASAG MFTYINENFL HAPSTDLNRE
TVKALINITL AQGQEVFLEK QIADSKKAGL LAKLASQSAY LYSQAAEGMQ EFAKGVFDKV
WTIVVQAKAG HMASVASYYQ ALADSETGSH GVAIARLQLA EKNSTAALGW AKSFPSSVSP
NANLSSESGT NLLDMIKYHL ANVQAKLTVF KKDNDFIYHQ PIPSEAGLSA VSKLPAAKAI
PVSELYQGQD IQRIIGPDIF QKLVPMSVTE TASLYDEEKA KLIRAETEKV ETANGEMAAS
LDYLKLPGSL NILKGGMDQE MTVDDEFRRW CQELGGHQPF IKAFDGLQDR KAEILAQLDQ
CSKQLDLEES VCEKMRSKYG VDWSQQPSAR LNTTLRGDIR TYRDTINEAS ASDSQLLSTL
RQYEADFDEM RSAGETDEAE VLFQRAMIKA GSKHSKGKNG VSSPYSASGE GSLIDDVFDE
GGTSVAEQIA RVESILKKLN LVKRERAQVL KDLKEKVHTD DISNVLILNK KTIAGQESQL
FEAELEKFRP HQNRLLQANH KQASLMKELT KIYGDLLQDK RVRAEQSKYE TITRQRNTVM
SRYKKIYDAF NGLLSGTAQA QTFYKEMGET VDSLKKNVET FINNRRSEGA QLLGQIERDK
ASNANEQEDR EREKLRQLME RLSTEPKTSP APPSAPAAPS KAKSPPPAIQ TPAYPNPAIS
SPKMSPRFPP NVSGQSHGIP VSHSPAPYGQ YIGHGTGVSY VPGQPFQQGA AAPLSEGYNP
MAYPVPPSVS PPPNQQFYSS TPTPFSYAGP TPPAAPSSFM PQGYVPPPPP PRPQQTTYPS
STGPYPSGPG GYAQGRPYGT SQHHKAPSQS QSQSATSSSN DPWAGLNAWK
//
