ID A0A060XNE4_ONCMY Unreviewed; 830 AA.
AC A0A060XNE4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=GSONMT00054598001 {ECO:0000313|EMBL:CDQ81138.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ81138.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ81138.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ81138.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-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}.
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DR EMBL; FR905712; CDQ81138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060XNE4; -.
DR STRING; 8022.A0A060XNE4; -.
DR MEROPS; M41.007; -.
DR PaxDb; 8022-A0A060XNE4; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
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; 3.40.1690.20; -; 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; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR43655:SF7; AFG3-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 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 Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380}.
FT DOMAIN 338..477
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 72..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 92699 MW; A18CE4D72D8F3E4B CRC64;
MMGLLSVSVV PLRNGVQAWG RGCATIHAAF RYSNFSSLSK CSALKRINPM GLNQCTFTLA
RLLSSKPPRG FEKFFPKSED TPGVNKSSEE TGDEKTKETE SQGGGEEGQN ESGERERRRG
GRKDESDWWT RFQNDFPWDE KTTRNVAIGF AGMASAFLYF YFRETGKEVS WKDFINNYLA
RGLVDRLEVV NKQYVRVIPV HGVNTSEVSY LWFNIGSVET FERNLELAQQ EMGLDSTHRV
PVIYGSESDG TFLMSILPTL LLVGFLLFTM RQGPMAGGRG GGRGNPFSMG ESKAKVMKDN
IDVRFKDVAG CEEAKLEILE FVNFLKNPRQ YQDLGAKIPK GAVLSGPPGT GKTLLAKATA
GEANVPFITV NGSEFQEMFV GVGPARVRDM FAMARKNAPC ILFIDEIDAV GRKRGRGNFG
GQSEQENTLN QLLVEMDGFN TSTNVVVLAG TNRPDILDPA LMRPGRFDRQ IYIGPPDIKG
RASIFQVHLR PLKLDSSIDS EALARKLAAL TPGFTGADIA NVCNEAALIA ARYLNESIIV
KHFEQAIERV IGGLEKKTQV LQPLEKTTVA YHEAGHAVVG WFLEHADPLL KVSIIPRGKG
LGYAQYLPKE QYLFTREQLF DRMCMMLGGR VAEQVFFGKI TTGAQDDLRK VTQSAYAQVV
QFGMSEVVGQ VSFELPRHGE MLMEKPYSEP TAQLIDQEVR SLIDAAFQRT HQLITEKRDV
VEKVGRRLLE KEVLDRADML ELLGPRPYKE KSTYEEFVEG TGPMKEDTSL PEGLKNWNKD
RGTEEPPQEQ QRKQALYLVC LFGLLSINNG KFRLLFIIPY QTTYSCTMFG
//
