ID G0RZ38_CHATD Unreviewed; 865 AA.
AC G0RZ38;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=CTHT_0001590 {ECO:0000313|EMBL:EGS23466.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS23466.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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}.
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DR EMBL; GL988032; EGS23466.1; -; Genomic_DNA.
DR RefSeq; XP_006690708.1; XM_006690645.1.
DR AlphaFoldDB; G0RZ38; -.
DR STRING; 759272.G0RZ38; -.
DR MEROPS; M41.004; -.
DR GeneID; 18254197; -.
DR KEGG; cthr:CTHT_0001590; -.
DR eggNOG; KOG0734; Eukaryota.
DR HOGENOM; CLU_000688_9_0_1; -.
DR OMA; MSHFEWA; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000008066; 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:UP000008066};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 311..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 390..526
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 791..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 93158 MW; C65299BEF7FE1CD9 CRC64;
MAFHASGLPS IASATSDLWP SLANTLAIPF RGPKCSSPAP SKHLNSANAP PAAAAPVVAA
AGLVEAAVRS HLPDFLRDAP VPTPRFLDRG LANASPVNIF SEISHMSSRS LAMANPLFRR
SYAALMSRPL STLPGCRYMS TYQPSRMQQF SWIQPLSVSR NVQRRSLHHG GIPRDLLAAR
EAAANRNPNS ASAQASFYQL LLKANLPAIV VERYQTGRFA TNEATDEAYR QALAMLNASA
GSGTGATVDS NAYGSGLSPS TLQAVGQAVA AHRTGGNTAF SAQAPNGTKS GPLHVIVDET
TGSALLRWIK FFLWFGLCAY ISMVVITMVV EGLSSIKRPG AKLTDIEAKA EHQKARFSDV
HGCDEAKEEL QELVEFLKNP EKFSALGGKL PKGVLLVGPP GTGKTLLARA VAGEAGVPFF
FMSGSEFDEI YVGVGAKRVR ELFQAAKAKA PSIVFIDELD AIGGRRNSRD ATYVRQTLNQ
LLTELDGFAQ NSGVIILAAT NFPESLDKAL TRPGRFDRQV VVPLPDVRGR IAILKHHASK
IKMGKDVNLE HIAQRTPGLS GAELENIVNQ AAIYASKNKA NAVTQAHFEW AKDKVIMGAE
RKSMVITAKE KEMTAYHEAG HALVAYYSKD TSGQLYKVTV LPRGRSLGHT AFLPEMDKYA
WSVKDYLGLI DRAMGGKVAE EIVYGHDLVT SGVSADLDQA TRTAWNMVAR LGMSQRLGPV
EYLRNYNSLS SETRAMVEAE VKRVLDESYA RARALLLEHR KELDLLAKAL VEYETLDRSE
VEKVIRGEKL EGRIPVPPGP MSVPKPDESE SVKPGLGGII PIPGKGAGNG SGNPPPAPPP
PAPAREGTEE SKRIMEEGED GRIDE
//
