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Database: UniProt
Entry: A0A226DFQ1_FOLCA
LinkDB: A0A226DFQ1_FOLCA
Original site: A0A226DFQ1_FOLCA 
ID   A0A226DFQ1_FOLCA        Unreviewed;       807 AA.
AC   A0A226DFQ1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=AFG3-like protein 2 {ECO:0000313|EMBL:OXA43808.1};
GN   ORFNames=Fcan01_21407 {ECO:0000313|EMBL:OXA43808.1};
OS   Folsomia candida (Springtail).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX   NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA43808.1, ECO:0000313|Proteomes:UP000198287};
RN   [1] {ECO:0000313|EMBL:OXA43808.1, ECO:0000313|Proteomes:UP000198287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VU population {ECO:0000313|EMBL:OXA43808.1,
RC   ECO:0000313|Proteomes:UP000198287};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXA43808.1};
RA   Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT   "The genome of Folsomia candida.";
RL   Submitted (DEC-2015) 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:OXA43808.1}.
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DR   EMBL; LNIX01000021; OXA43808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226DFQ1; -.
DR   STRING; 158441.A0A226DFQ1; -.
DR   OMA; ARQKGNF; -.
DR   OrthoDB; 9585at2759; -.
DR   Proteomes; UP000198287; 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:0008270; F:zinc ion binding; 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; 3.40.1690.20; -; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        150..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        256..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          349..488
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          55..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..792
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   807 AA;  88671 MW;  0FFAC6E4DB39F8EE CRC64;
     MMAHRFVLTP CRQLDRVLRR SLITGDASHI YRRFPEIHRI LSQVRVYFGD KPPPKGFEKF
     FRPSKSGDKA PPSKSGDGKE AGTKKSGENA PPPPPSRAAS SSGPTNTPPP SSARPPGDPW
     SSFLGGGGPR GGSTGGGKQG GLGSEGGDKM IFLSVVATIG LLGTFAYYEM SYKEITWKDF
     VNNFMARNIV EKLEVVNKKW VRVRLNPGQN VDGSSILWFN IGSVDSFERN LENAQMEMGI
     EGSNFIPVIY KTEIEAASLT GVLPTILIIG FLLYMMRRSA EMMGGAGRGG RRGGIFGSVM
     ESTAKLINSS DIGVRFKDVA GCEEAKVEIM EFVNFLKNPN QYYELGAKIP KGAILTGPPG
     TGKTLLAKAT AGEANVPFIT VSGSEFLEMF VGVGPSRVRD MFAMARKHAP CILFIDEIDA
     VGRKRGGRSF GGHSEQENTL NQLLVEMDGF NTTTNVVVMA ATNRIDILDS ALLRPGRFDR
     QIFVPAPDIK GRASIFKVHL KPLKSELDKN DLSRKMAALT PGFTGADISN VCNEAALIAA
     RDMNTTISLK HFEQAIERVV AGMEKKTNVL QPDEKKTVAY HEAGHAVAGW FLKHADPLLK
     VSIIPRGKGL GYAQYLPKEQ YLYTKEQLFD RMCMTLGGRV SEQIFFGRIT TGAQDDLKKV
     TQSAYAQIVH YGMNDKVGNV SFDMPQPGEM VMDKPYSEET AQLIDTEVRV LISTAYEYTH
     KLLTEHKQDV LKVAERLLKQ EILSRDDMIE LLGKRPFPEK STYEEFVEGT GSFEENTELP
     EGLKEWNKAR PEEKGTPPPQ AATPAST
//
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