ID B3S6M8_TRIAD Unreviewed; 773 AA.
AC B3S6M8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=TRIADDRAFT_30182 {ECO:0000313|EMBL:EDV21649.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV21649.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV21649.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV21649.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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; DS985252; EDV21649.1; -; Genomic_DNA.
DR RefSeq; XP_002115797.1; XM_002115761.1.
DR AlphaFoldDB; B3S6M8; -.
DR STRING; 10228.B3S6M8; -.
DR MEROPS; M41.007; -.
DR EnsemblMetazoa; TriadT30182; TriadP30182; TriadG30182.
DR GeneID; 6757147; -.
DR KEGG; tad:TRIADDRAFT_30182; -.
DR CTD; 6757147; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_16_2_1; -.
DR InParanoid; B3S6M8; -.
DR OMA; ARQKGNF; -.
DR OrthoDB; 9585at2759; -.
DR PhylomeDB; B3S6M8; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
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; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF2; SD01613P; 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:UP000009022}.
FT DOMAIN 329..469
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 16..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 85530 MW; B7D7087EBCDED032 CRC64;
MLFTVLNSCY FFQLTEPVQK DNSDKTNSIE QDKQHQQDQN LQADNKHDGK GPSVASDTPK
DDPSPAQKAQ VEKSKNEQDT KRTVSDTDTP EDDSTTPSSS SSSSSSSTSG GGDHNKKDDK
YWWEELSEAR MRQIGLGVAI AIGAGYYLYT TDHNATREIN WQQFRVNYLE KGLVEKLVVV
NKSYVKVFLK NHDDGMFESP QYHFTIGSVE NFERNLETVQ RDLNVDPIDQ VPVVYVKQYE
YLREILLLSP TLLLIGGMIY ASRRISTGSR GAGGIFGVGQ STAKFFNKET NIKVKFSEVA
GCEEAKIEIM EFVNFLKNPN QYQQLGAKIP RGAILSGPPG TGKTLLAKAT AGEAGVPFLS
ISGSEFLEMF VGVGPARVRD LYAQARKNAP CIIFIDEIDA VGRSRSKGGQ FGGHDERENT
LNQLLVEMDG FSSTTNVVVL AGTNRPDILD PALLRPGRFD RQIVISPPDI KGRLSIFKVH
LKPIKTDLDI NAVARKLAAL TPGFTGADIA NVCNEAALIA ARHLCSKVEL THFEQAIERV
IAGLEKKTQV LQPEEKNVVA HHEAGHAVAG WFLEHADPLL KVSIIPRGKG LGYAQYLPKE
QYLYTTEQAS NDHLMDRMCM TLGGRVAEQI FFNRITTGAQ DDLSKVTNNA YAQVIKFGMN
EAIGNLSFDM PGDGEPMFEK PYSEATAQLI DEEVRKLINL AYARTTELLK SHKDDVAKIA
NLLLEKEVLN RDDMIELLGP RPFPEKSTYE DFVANTGGDE EDTSLPEGLK DFS
//
