GenomeNet

Database: UniProt
Entry: R1G834_BOTPV
LinkDB: R1G834_BOTPV
Original site: R1G834_BOTPV 
ID   R1G834_BOTPV            Unreviewed;       725 AA.
AC   R1G834;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Putative heat shock protein chaperonin protein {ECO:0000313|EMBL:EOD44311.1};
GN   ORFNames=UCRNP2_8975 {ECO:0000313|EMBL:EOD44311.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD44311.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; KB916737; EOD44311.1; -; Genomic_DNA.
DR   RefSeq; XP_007588215.1; XM_007588153.1.
DR   AlphaFoldDB; R1G834; -.
DR   STRING; 1287680.R1G834; -.
DR   KEGG; npa:UCRNP2_8975; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_005070_4_0_1; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF176; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW   Stress response {ECO:0000313|EMBL:EOD44311.1}.
FT   DOMAIN          50..193
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          450..590
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          629..718
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          263..350
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   725 AA;  80489 MW;  35C2040C70FE04E8 CRC64;
     MNMGGGEEEK PALEQYGVDL TAKAKDGKLD PVIGRDAEIH RTIQILSRRT KNNPVLIGSA
     GTGKTAILEG LAQRIVRGDV PESIKNKRVI SLDLGSLIAG AKFRGDFEER LKKVLEEVEK
     AEGGVILFID ELHTLLGLGK AEGSIDASNL LKPALSRGEL QCCGATTLNE YRQIEKDVAL
     ARRFQPIVVG EPTVPDTISI LRGIKERYEV HHGVRITDGA IVAAATYSNR YITDRFLPDK
     AIDLVDEAAS ALRLQQESKP DAIQELDRQI MTIQIELESL RKEEDIASKE RREKLEQQLK
     AKNEELTKLN EKWESERREI EEIKNIKESL EKARLELEQS QREGNFAKAS ELRYATIPAL
     EQKLPKDGAE GAGKSPGSLL HDSVTADDIA NVVSRTTGIP VTKLMSGEIE KLIHMEDILR
     QSVKGQDEAL TAVANAVRMQ RAGLSGENRP LASFMFLGPT GVGKTELCKK MAGFLFSTET
     AVLRFDMSEF QEKHTVSRLI GSPAGYVGYE DAGQLTEAVR RKPYAVLLFD EFEKAHRDIS
     ALLLQVLDEG FLTDSQGHKI DFRNTIIVLT SNLGAEVIVG DDMIHRHQVD TETGEISPAV
     KKSVMDIVAS NYPPEFLNRI DEFIIFKRLS KEALRDIVDI RLKELQQRLD DRRITLKVPD
     EVKQWLTERG YDPKFGARPL NRLIAKEIGN KLADKIIRGE LRNGTAAVVG INEGQTGLQV
     SAETS
//
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