ID A0A0J7KXH3_LASNI Unreviewed; 810 AA.
AC A0A0J7KXH3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Afg3-like protein 2-like protein {ECO:0000313|EMBL:KMQ95021.1};
GN ORFNames=RF55_4783 {ECO:0000313|EMBL:KMQ95021.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ95021.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ95021.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ95021.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-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:KMQ95021.1}.
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DR EMBL; LBMM01002288; KMQ95021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7KXH3; -.
DR STRING; 67767.A0A0J7KXH3; -.
DR PaxDb; 67767-A0A0J7KXH3; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000036403; 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: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 Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403}.
FT DOMAIN 332..471
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 74..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 90577 MW; 4BB6BC0A3ABE5E59 CRC64;
MLSSASKLER LILRSTQKGY FDTLQLRRHL TLLKNGTTLS MIEQLQQKWR LFCKEPPKGF
EKFFKPGGAK NAENVAKKAE EASSKKASTQ KPSSSSSSSS SSSKDSGFQW AFKMFSDSSQ
RGGKSFEGGD KDRTFMILGA LGVTGLLAYI LSQDFNQKEI TWREFTYNYL SKGLVDKLEV
VNKKWVRVRL LPGHTVDGSD TLWFNIGSTD TFERNLENAQ IELNMGPENY IPVVYKNEIE
SANILSYLPQ IFMWGLLFYL IRRSAEAMTG KGGKRGGLFG TVMESTAKLI NSKDIGVRFK
DVAGCEEAKI EIMEFVNFLK NPQQYIDLGA KIPKGAMLTG PPGTGKTLLA KATAGEANVP
FITVSGSEFL EMFVGVGPSR VRDMFSMARK HAPCILFIDE IDAVGRKRGG RNFAGHSEQE
NTLNQLLVEM DGFNTTTNVV VLAATNRVDI LDKALLRPGR FDRQIFVPAP DIKGRASIFK
VHLAPLKTLL DKDQLARKMA SLTPGFTGAD IANVCNEAAL IAARDLYDNI KLKNFEQAIE
RVVAGMEKKT NVLQPEEKKT VAYHEAGHAV AGWFLEYADP LLKVSIIPRG KGLGYAQYLP
REQYLYTKEQ LFDRMCMTLG GRVSEEIFFG RITTGAQDDL QKITEIAYAQ ITQYGMNEKV
GNVSFQMPKP GDMALDKPYS EYTAQLIDNE VRELIDRAHK RTRALLDEHK ENVIKVAERL
LKQEILSRDD MIELLGARPF REKSTYEEFV EGTGSFEEDT TLPEGLKEWN KSKEESSEDG
DKKDKAAESG ESQTQSSKIA SSDKQPQQRL
//
