ID F2PMT2_TRIEC Unreviewed; 785 AA.
AC F2PMT2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Heat shock protein 78 {ECO:0000313|EMBL:EGE03200.1};
GN ORFNames=TEQG_02238 {ECO:0000313|EMBL:EGE03200.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; DS995726; EGE03200.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PMT2; -.
DR VEuPathDB; FungiDB:TEQG_02238; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_0_1; -.
DR Proteomes; UP000009169; 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:SF18; 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|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Stress response {ECO:0000313|EMBL:EGE03200.1}.
FT DOMAIN 115..259
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 516..703
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 688..779
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 428..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 328..408
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 785 AA; 86652 MW; 9BA86604A3861744 CRC64;
MSCRLVMRGS RQLLPAPRAA AHINTTARRG LYGLLPRQLS KQYIPASGFV RHYANGRPHP
PGGTHRMNLG GEPEKPALEQ FGVDLTARAK DGKLDPVIGR DAEIHRTIQI LSRRTKNNPV
LIGAAGTGKT AVLEGLAQRI VRGDVPESVK NKRVVSLDLG QLIAGAKFRG DFEERLKRVL
KEVEDAQGGV ILFVDELHTL LGLGKAEGSI DASNLIKPAL ARGDLQCCGA TTLNEYRQIE
KDVALARRFQ PILVEEPTVP DTISILRGIK DKYEVHHGVR ITDGALVAAA TYSNRYITDR
FLPDKAIDLV DEAASALRLQ QESKPDAIQE LDRQIMTIQI ELESLRKEKD IASVERREKL
EELLKSKQED VGKLTEAWDK EKAELEAIKQ AKEDLERARG ELEQAQLEGN FAKAGELRYS
TIPNLEKKLP QEDDTGSTGT QGQSLLHDSV TADDIAGVVS RTTGIPVNKL MSGEVEKLIH
MEDTLRKSVR GQDEALEAVA NAVRMQRAGL SGENRPLASF MFLGPTGVGK TELCKKMAGF
LFSTETAVVR FDMSEFQEKH TVSRLIGSPA GYVGYDDAGQ LTEAVRRKPY AVLLFDEFEK
AHRDISALLL QVLDEGFLTD AQGHKIDFRN TLIVLTSNLG AEVLVSADAS EGEDISPEMK
SAVMGIVQSS YPPEFLNRID EFILFKRLSR SALRDIVDIR VKELQARLDD RRITLSVSDE
IKDWLCEKGY DPKYGARPLN RLISKEIGNH LADKIIRGQV VSGQTAIAIF NEDKTGLDIA
TEKSA
//
