ID B6Q8H1_TALMQ Unreviewed; 633 AA.
AC B6Q8H1;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 13-SEP-2023, entry version 67.
DE SubName: Full=ATP-dependent Clp protease, putative {ECO:0000313|EMBL:EEA25775.1};
GN ORFNames=PMAA_068690 {ECO:0000313|EMBL:EEA25775.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA25775.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; DS995900; EEA25775.1; -; Genomic_DNA.
DR RefSeq; XP_002146322.1; XM_002146286.1.
DR AlphaFoldDB; B6Q8H1; -.
DR STRING; 441960.B6Q8H1; -.
DR VEuPathDB; FungiDB:PMAA_068690; -.
DR HOGENOM; CLU_014218_1_2_1; -.
DR OrthoDB; 452393at2759; -.
DR PhylomeDB; B6Q8H1; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EEA25775.1};
KW Protease {ECO:0000313|EMBL:EEA25775.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT DOMAIN 192..384
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 473..567
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 303..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 68777 MW; D64F3819168F9E20 CRC64;
MKRPPVRFPR LAANIGGPQR SYIHNYSPRQ PRIPSSYRYN RNFTSLNSRL SSSHFNRSDF
TSQPFTGSYE AGLPTPGPLG STPAFGAPRL TPRMLKQYLD QFVVGQDRAK KILSVAVYNH
YQRIMELQRQ EEAAAEMMAQ RERRAAMEAH HLDDEFTGHQ RTMNLEQPMQ DTIESRLGGS
SSFPDTSSTQ LEKSNILLLG PSGVGKTLMA KTLARVLDVP FSMSDCTPFT QAGYIGEDAD
VCVHRLLAAA NYDVEKAERG IICLDEVDKI ATARVSHGKD VSGEGVQQAL LKIVEGTTVQ
VQVKPEKNTS RPAGGAPGSF PPGATPGSAF NSPSTASGPP PQKGEIYNVR TDNILFIFSG
AFVGLNKIIM DRISKSSMGF GQPVRASSIS SGNSSSSHDA SNQAPIPIIP GSEEEALYKK
HLPFFTSATP PTSSEEPVYF NPLDLSTPSD LQKFGFIPEL VGRIPVTTAL SSLSHSLLLR
ILTEPRNSLV TQYETLFDLS GIKLSFTTPA LHKIASNALS MGTGARALRT ELETILSDAM
FEAPGSSVKF VLVTEKVADR QEKPIYFGRG QGSRFHSMIA AEESDWENKM QKDKKQRSTT
NGGNGNGNGN GNKSGSKVLS FAEYRNRAST AGA
//