ID A0A094BHX2_9PEZI Unreviewed; 828 AA.
AC A0A094BHX2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=V492_05278 {ECO:0000313|EMBL:KFY09957.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY09957.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY09957.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY09957.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY09957.1}.
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DR EMBL; JPJU01001813; KFY09957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094BHX2; -.
DR STRING; 1420902.A0A094BHX2; -.
DR MEROPS; M41.004; -.
DR HOGENOM; CLU_000688_9_0_1; -.
DR Proteomes; UP000029299; 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:UP000029299};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 299..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 378..514
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 31..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 88542 MW; E75E004EBA3FD893 CRC64;
MAFQASALPS VAAATTEMWP SMVNVMGAPW RSAGSRTQSK QTRPVQRSEA AQPQPATVSQ
PSKPVLPECL QHAHGLTSSL AQYQTAAQTP FNVRDTLSSM RSGTLAAANP LARRLPNAPF
ASRQMTTISA FRLQQPRAPF TRILKPQQRT VFGANTSRNL LAHMEEAANR NPNSATAQNA
FYQALLRANM GAIVVERYQN GHFASNAACE AAYQKALASL NGAGAGFGAN DGGFGGGMAN
NGLNNSQLQA IGQAVAASSR GGNVGISRGQ PNGSGVKESP LYVVVEETIG SVIFKWVKLM
LYFALITYVC FALITVLVES LGVLKKVGNG KTDNEAKAEH QKVRFSDVHG CDEAKEELQE
LVDFLKNPEK FSTLGGKLPK GVLLVGPPGT GKTLLARAVA GEAGVPFFFM SGSEFDEIYV
GVGAKRVREL FSGAKSKSPA IIFIDELDAI GGKRSARDAS YAKQTLNQLL TELDGFEQNS
GVIILAATNF PETLDKALTR PGRFDRNVVV GLPDVRGRMA ILKHHMTNVV QGKDVNIEQL
AAGTPGFSGA ELENVINQAA VHASKAKALA VSMKDFEWAK DKVMMGAEKR SMVISDKEKE
MTAYHEAGHA LVGMFTKGAS PLHKITIMPR GQSLGMTMHL PEIDKYSKSM SEYRAHIDVC
LGGKMAEEII YGAEEVTSGV AGDLESATQV AYAMVTQFGM SSAAGNVDLS TNYNHLSSET
KQLIESEVRR TIEEGRQRAR ALLVHKRKEL DLLARALVSY ETLDKEEAFK VIRGEELVGK
VVMPSGLMKR PEGEVPRDLP LPPIPGSAAA GAQEGAGEPP KGGVMASG
//
