ID A0A2G9H3X6_9LAMI Unreviewed; 621 AA.
AC A0A2G9H3X6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=CDL12_15169 {ECO:0000313|EMBL:PIN12222.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN12222.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
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:PIN12222.1}.
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DR EMBL; NKXS01002749; PIN12222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9H3X6; -.
DR STRING; 429701.A0A2G9H3X6; -.
DR OrthoDB; 446149at2759; -.
DR Proteomes; UP000231279; 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: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 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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF19; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 12, CHLOROPLASTIC; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..280
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 621 AA; 70666 MW; 643CFE646C48477C CRC64;
MKEGFPLEYI VDIPLDPFLF EAISCSGVEV DLLQKRQIHY FLKTVFALLP GLIILYFIRE
SVSLLLITTN TLLYKKYNQI VDKARAENFI LPVGRDVGQI KSMYKDVILG GDIWDLVDEL
MMYMRNPMRY YEKEVKFVRG VLLYGPPGTG KTHFARTLAK KSGVPFVFAS GAEFIDSEKR
GAAKMNQLFS MARKNAPAFV FVDEIDAIAG RYSRRDPQRG ATFDALIAQL DAEKERTGID
RFSLKQAVIF ICATNRPHVL DKRLVRPGRI DRRAYIGLPD AKQRVQIFGV HSAGKELAED
VDFEKVVFRT VGFSGADIRN LVNEAGIMSV RKGHSKIYQQ DIVDVLDKQL LEGMGVLLTE
EELLKCERRI SLETKRLLAV HEAGHIVLAH LFPRFDWHAF SQLLPGGKET AMSVFYPREK
IIQGAATIGY LKMQMVVAHG GRCAERIVFG DDITDGGRHD LKKITKLARE IVISPSNERL
GLTPLTKRIK LADRRPADRP QDEVIKYRWD DRRVIPASMS LEVSELFMRE LTRCIDETEE
LAMKGLRDNR HILDVIAERL LQNSRVTGSE VEEIIKGLSP IMFEDFAEVF EISEEEDGPL
PHLDRLPYQP LDIFPAPMHR C
//
