ID A0A176VWA3_MARPO Unreviewed; 725 AA.
AC A0A176VWA3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=AXG93_2752s1710 {ECO:0000313|EMBL:OAE24156.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE24156.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE24156.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE24156.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) 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:OAE24156.1}.
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DR EMBL; LVLJ01002675; OAE24156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VWA3; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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: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 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 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 277..413
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 725 AA; 77610 MW; D3E66D9983939B37 CRC64;
MAWRQLVEQG GSAVKQVAAS SVWAGVRNDF RTSLFNLGSH VHNLTDGGLT FQKTQKRFMS
GYMSGFSRRL EQLERESSKY GTDDKHAAVL RELNKVDPEG VIRWFETQSA AHRSPAALAE
YVKALVKVDR LDQSALFKTL QRGASALGND IRGDSMPIMA GASSPLANVG MVTKDGVLGT
PNAPIHMITA EGGLKVQAWR TLRTLALGFL LLSGVGALIE DRGIGKGLGL NEEVQPSIES
NTKFSDVKGV DEAKAELEEI VHYLRDPKRF TRLGGKLPKG VLLVGPPGTG KTMLARAIAG
EAGVPFFYCS GSEFEEMFVG VGARRVRDLF SAAKKRSPCI IFMDEIDAIG GSRNPKDQQY
MKMTLNQLLV ELDGFKQNEG IIVIAATNFP ESLDKALVRP GRFDRHVVVP NPDVEGRRQI
LEAHMSKVPK AEDVDLSIIA RGTPGFSGAD LANLVNVSAL KAAMDGQKSV SMTDLEFAKD
KIMMGSERKS AVISDESRKL TAYHEGGHAL VALYTDGALP VHKATIVPRG MALGMVSQLP
EKDETSFSRK QMLARLDVCM GGRVAEELIF GEGEVTSGAS SDIVSATRLA REMVTKYGMS
KAVGVVAHNY EDDGKSMSTE TRLLVEQEVR DLLQKAYENA KTILTTHQKE LHALANSLLE
NETLTGNQIK ALLVSVSSPS KPASAPTSIP ALPSPSSAAA SAAAAAAAAA AAVAKPNSVA
QPAGT
//
