ID A0A3R7FSP0_9EURO Unreviewed; 802 AA.
AC A0A3R7FSP0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=CFD26_105086 {ECO:0000313|EMBL:RLL97138.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL97138.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|EMBL:RLL97138.1, ECO:0000313|Proteomes:UP000215289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL97138.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RLL97138.1}.
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DR EMBL; NIDN02000087; RLL97138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7FSP0; -.
DR STRING; 1245748.A0A3R7FSP0; -.
DR Proteomes; UP000215289; 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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000215289};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 288..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 366..502
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 782..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 87710 MW; 4697475C7C817520 CRC64;
MAFQVPVSRP NLAAVTSDLW PSMSKLLNAP WTSIERTAAS GFPTTQRLPR RTLGGTESSV
TARFPLPECL DTVPLEALNS NVMQRSVQHG LSRTFLRDSL WSSVTVSPRP HASHFARSYS
TLSATVSRTR QAPRPYGLSK LQHQRFLFGG PSHSLLAQKE KTANNNPSSA NAQNAFYQAL
LRANMPAIVV ERYRSGHFAS NSLSEAIYLK ALQRVGGADP AAAAPIQGQN QNLNPDQLQA
IGQAVAARTH GNQIGLATKQ SGTGAKDDPL HVVVEESLGS TVFRWARFLL GFGFFCYISL
VIITILVETT GVLKNIKGPQ SNEAQPQQQT VRFSDVHGCD EAKEELQELV EFLLNPERFS
SLGGKLPKGV LLVGPPGTGK TLLARAVAGE AGVPFFYMSG SEFDEVYVGV GAKRVRELFA
QARNKAPAII FIDELDAIGA KRNERDAAYV KQTLNQLLTE LDGFSQTSGV IIIAATNFPQ
LLDKALTRPG RFDRKVVVDL PDVRGRMDIL KHHLKNIQIS TDVDVAVLAR GTPGFSGADL
ENLVNQAAIY ASRNKKAKVG PKDLDWAKDK IMMGAEARSR IIQDKDKLLT AYHEAGHALV
AYFSPSSTPL YKITIVPRGM ALGVTHFLPE MDTVSRNYTE YLSDIDVSMG GKAAEELVFG
PDKVTSGISA DIQQATETAF TLITRFGYSK KLGNVDLSTN YDSLSSETKQ EIESEVRRLV
EEARLRATKI LTERRHELEL LTKALIEYET LTKEEMEKVL RGEKLDKMAS VPSAPLKLPE
ALQTAKLNHP STQAEEPPVA AK
//
