ID A0A1V6T412_9EURO Unreviewed; 797 AA.
AC A0A1V6T412;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=PENFLA_c016G05415 {ECO:0000313|EMBL:OQE20660.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE20660.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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:OQE20660.1}.
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DR EMBL; MLQL01000016; OQE20660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6T412; -.
DR STRING; 254877.A0A1V6T412; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000191342; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR CDD; cd22265; UDM1_RNF168; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR InterPro; IPR048438; Yme1-like_N.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF37; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR Pfam; PF21232; Yme1-like_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000191342}.
FT DOMAIN 363..499
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 775..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 721..748
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 797 AA; 86685 MW; C53DE70DE94CAC1B CRC64;
MAFQVPIPMP NVAAVTSDLW SSMYNVLAVP WKQTGRTTAN VSESLQRSTS RQGKETITQR
ATLPEYLERV SIEALRADIV SRPSQQTWSS LLNRNNVLRA TSSFTPIRHA IPATRSYSTL
TPFRLNSLRT TPKVSGLSKS QQQRFLSGGS WHHVLAQKEK IANKSPNNAD AQNALYSALL
RAKMPGIVIE RHRSGYFAGD LTTEALVQQA QSSVGGADAG AGAFAGPNHN LSPEQLQAVG
QAVAARATGS QIGMGKQNGT GAKDAPLYVV VDESLGSTVF RWVKFLLIFG FFTYISLVTV
TILVETTGVL KNVRGAQDKE AQPEQQTARF SDVHGCDEAK DELQELVEFL LNPDRFSSLG
GKLPKGVLLV GPPGTGKTLL ARAVAGEAGV PFFYMSGSEF DEVYVGVGAK RVRDLFAQAR
GKAPAIIFID ELDAIGGKRN ERDAAYVKQT LNQLLTELDG FSQTTGVIII AATNYPQLLD
KALTRPGRFD RRVVVDLPDV RGRMDILTHH MKEIQFGPDV DVGVIARGTP GFSGADLENL
VNQAAVHASR DRKAFVGPLD FDWAKDKIMM GAEARSRIIQ DKDKLLTAYH EAGHALVAHF
SPSSTPLYKI TIVPRGMALG ITHFLPEMDT VSRNYTEYLA DIAVSMGGKA AEELVFGHDN
VTSGISADIQ SATETAFTLI TRFGYSKKLG NVDLSTNYDS LSSETKQEIE AEVRRLVEEA
RDRATNILTE KRNELELLTK ALIEYETLTK EEMEQVLKGE KLNKLVSTPS APLKLPSALQ
SANLNPSAAG RAPTANE
//
