ID A0A0N5AUQ6_9BILA Unreviewed; 697 AA.
AC A0A0N5AUQ6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=AAA domain-containing protein {ECO:0000313|WBParaSite:SMUV_0000859701-mRNA-1};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000859701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000859701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
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 AlphaFoldDB; A0A0N5AUQ6; -.
DR STRING; 451379.A0A0N5AUQ6; -.
DR WBParaSite; SMUV_0000859701-mRNA-1; SMUV_0000859701-mRNA-1; SMUV_0000859701.
DR Proteomes; UP000046393; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 233..373
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 651..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 77435 MW; CD86CC80F18E551A CRC64;
KDEVHRLLNQ QISIETFGRY VQGLCTLFAT NFPKGLQKLL EELSKGQQPQ KLQPFFVALG
IALALYLVYG SVMGKEISWK EFYSDYLERG LVERLEVVNK RYVRVILKSS EAHKTVHFNI
GSVESFERSL AAAQNHLGIP AEHQIPVLYK NEINCTFCYA FLGKTTKKKG GTSGGFPFFG
SSMGQSTARL INKNDIKVAF KDVAGCEEAK IEIMEFVNFL KNPQQYKSLG AKIPKGALLT
GPPGTGKTLL AKATAGEANV PFLSVSGSEF LEMYVGVGPA RVRDMFAEAR KNSPCILFID
EIDAVGRKRG RNLGGSHSEQ ENTLNQLLVE MDGFSTDEAS VIVIAATNRV DILDPALLRP
GRFDRQIYIP VPDIKGRASI FRVHLAPLKT SLNKTELARK MSALTPGFSG ADIANVCNEA
ALVAARDGGE EIVMKNFEQA IERVVAGMEK KSQVLQPDEK KTVAYHEAGH AITGWFLEHA
DPLLKVSIIP RGKGLGYAQY LPKEQYLYTK EQLLDRICMM LGGRVSEEIF FGRITTGAQD
DLQKVTQMAY SQIVKYGMSA KVGPLSFQAP APGEMAFDKP YSEATAQLID QEVRDLVNKA
LNRTRELLLS KQQQIEKVAL RLLDREVLSR DDMEELVGKR PFAEKSTYEQ FVEGTGGLDE
DTSLPKGLES WNKPREDNSS AKDKEENHNR TNEDKDK
//
