ID A0A163A6X6_DIDRA Unreviewed; 1554 AA.
AC A0A163A6X6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=BRO domain-containing protein 1 {ECO:0000256|ARBA:ARBA00041284};
GN ORFNames=ST47_g7846 {ECO:0000313|EMBL:KZM21020.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM21020.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM21020.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM21020.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endosome {ECO:0000256|ARBA:ARBA00004177}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM21020.1}.
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DR EMBL; JYNV01000258; KZM21020.1; -; Genomic_DNA.
DR STRING; 5454.A0A163A6X6; -.
DR Proteomes; UP000076837; 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 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:UP000076837};
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 67..131
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 231..311
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT DOMAIN 590..992
FT /note="BRO1"
FT /evidence="ECO:0000259|PROSITE:PS51180"
FT ZN_FING 231..311
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 22..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1510
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1554 AA; 169309 MW; 72E909067E1DCA3C CRC64;
MSFVGPMPLK AVAPARIVSA SRQCQRRNMS RARTQMKRPA LAAQTQTQNA PSIRLFHASP
TTHAMTDPYK TLGVDKSATA ADIKKAYYGL AKKYHPDTNK EPTAKEKFAA AQSAYEVLSD
KEKKAAYDSY GSSAFDQNGG FNPGAGAGAG PGGNPFGGGF GGFGGFGGAQ GGFGGQGGFQ
DINFEDLFGA FAGGRRPRGG GGRRNPFQEE IMVGDNIEVQ TNISFLDAAK GVKKEIHITP
MVECGTCKGK GMKAGAKKAE CKGCGGTGQR VTSMGGFHMS ATCSQCGGSG FAIPRGSSCG
TCGGDGAVKE RKTIQIDIPG GVEDGMRLRV NGEGDAALTG QAMSGGTVRG QKGDLYVLIR
VAADSKFKRN GSDILHTATI PFTTAVLGGE IKVPTLDGEV MVKVPTGSGT GDNITLSGMG
MKVLSSGRRG AGKGDLKVEF KVNMPKYLSV NQRTILEMLA DEMGDKSAKR IMNLSKFRED
AQAAAEKPST ASTPDEHKNE GFLKSAWHNL TGQHNHLKKD QPKKDEPTSE KKDDEKKGAG
SATCSASAGD SALHCIRHRL AIPLTKPNPT QPNPTAAPAA LGSTMATQIP MISVPLKQTN
EIDWIQPLKG YIRQTYGDDP ERYAEECATL NRLRQDMRGA GKDSAAGRDL LYRYYGQLEL
LDLRFPVDEN HIKISFTWFD AFTHKPTSQY SLAYEKASII FNISAVLSCH AAHQNRHEDV
GLKTAYHSFQ ASAGMFTYIN ENFLHAPSQD LGRETVKCLI SVMLAQAQEV FLEKQVVDGK
KVGLLAKLAS QAAFLYAQAT EGAQENVTNA VFEKVWLLVC QIKANYMASA AQYYQALADD
DANAHGVAIC RLQVAETSAR DANRAANSFP NSAPANSNLT SETHGILSEM TKKHLSNVQE
KLAEFMKDND FIYHQGIPNE ASLTPIPKLP AAKAIPVSEL YQGQDVQRII GPDIFQKIVP
LAVTESASLY DEEKAKLIRA ESERVEVAND EMAASLDYLK LPDSLNVLRG GMDQDMMVDS
DFRKWCEDLA GHQSFSSAFD QLNRDKSEIA GTLDASMKQL DMEESVCEKM RSKYGPEWTQ
QPSSRLTATL RSDIRNYRGA VDEASTSDAQ LYNTFRQCEA DFDEMRSAGE TDEADVLYQR
AMIKAGAQKG KSPRPAEGNL IDDDFDDGPT VSDQIAAVED LLRKLNLVKK ERAQILLDLK
GKVHSDDISN VLILNKKAIA NQESQLFKAE LEKFRPHQNR ILQANHKQAS LLKELTRTYS
DLLKDKRVRS EQSKYEAFSR QRNTVMTKYR RVNQNFNDLV AGLNRAQQFY SEMKETVSSL
QKNVETFVNN RRSEGGQLLA RIEQSKSQGA DHEQQRLKDL MERMSMEPSG SPVSAGSGRK
KSVPPPLSSI PGYPSTSPAG HVQYNPAASP PVTPRYPPTT QQSFMSPQQS YSGAASNTFQ
PPPPRRESYQ QYPQHQHQTS QSYNPAQHQY NPVSPPAHHQ FFSPPPPQHP QHQPWGQPPP
QQPPPQPQWG QNVPQGYGSY PAGPGGYAQR PAQGQAQGQG QGGSDPWAGL SGWK
//
