ID A7TDR8_VANPO Unreviewed; 797 AA.
AC A7TDR8;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=Heat shock protein 78, mitochondrial {ECO:0008006|Google:ProtNLM};
GN ORFNames=Kpol_1018p70 {ECO:0000313|EMBL:EDO19538.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO19538.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; DS480378; EDO19538.1; -; Genomic_DNA.
DR RefSeq; XP_001647396.1; XM_001647346.1.
DR AlphaFoldDB; A7TDR8; -.
DR STRING; 436907.A7TDR8; -.
DR GeneID; 5547895; -.
DR KEGG; vpo:Kpol_1018p70; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; A7TDR8; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 35211at2759; -.
DR PhylomeDB; A7TDR8; -.
DR Proteomes; UP000000267; 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:UP000000267}.
FT DOMAIN 120..263
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 520..665
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 693..782
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 332..412
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 797 AA; 89877 MW; B55F5BF2B33A0120 CRC64;
MLRQAAKRSV PFKGHFNSLS RQSYTRVGQI GSSIATRNSF SILNHINGKI NNANSIRSFH
SSNNLLIQMR MNPNQQKDNE PALEQFGTNL TKLAKEGKLD PVIGRDEEIS RAIQILSRRT
KNNPVLIGRA GVGKTSLIDG LAQRIVSGEV PDSLKDKQLI ALDLGSLIAG AKYRGEFEER
LKNVLKEIDD SNGEVIVFID EVHMLLGLGK TDGSMDASNI LKPKLAKGLR CISATTIDEF
KIIEKDPALT RRFQPIILNE PSVTDTISIL RGLKERYEVH HGVRITDAAL VSAAVLSNRY
LTERFLPDKA IDLVDEACAV LRLQHESKPD EIQKLDRAIM KIQIELESLK KETDPISVER
RDKLDEELNL KNEELNRLTK VWDAERAEIE SIKNAKADLE QARIELEKSQ REGDYTKASE
LRYSKIPELE RKVSLSENKN KEDSESQVLL HDSVTSDDIS KVVSKMTGIP SDTVMKGDKD
RLLYMEKTLQ ERVVGQDEAI SAVSDAVRLQ RAGLTSEKRP IASFMFLGPT GTGKTELTKA
LAEFLFDNES NITRFDMSEF QEKHTVSRLI GAPPGYVLSE SGGQLTEAVR RKPYSIVLFD
EFEKAHPDVC KILLQVLDEG KLTDSLGHHV DFRNTIIVMT SNIGQDILLS DKETSDDGKI
NKNTRDRVIN AMKKSYPPEF INRIDEMIVF NRLSKSVLRS IVDIRIKEIQ ERLIEKRITL
KLTDEAKIWL TENGYDAMYG ARPLNRLIHK QILNPMATYM LKGQILNGED VNVIVEKNKL
IVKPNHEEGE TKPEKQT
//