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Database: UniProt
Entry: A0A0N5D6K8_THECL
LinkDB: A0A0N5D6K8_THECL
Original site: A0A0N5D6K8_THECL 
ID   A0A0N5D6K8_THECL        Unreviewed;       815 AA.
AC   A0A0N5D6K8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=AAA domain-containing protein {ECO:0000313|WBParaSite:TCLT_0000867301-mRNA-1};
GN   ORFNames=TCLT_LOCUS8662 {ECO:0000313|EMBL:VDN06239.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000867301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000867301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN06239.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; UYYF01004665; VDN06239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N5D6K8; -.
DR   STRING; 103827.A0A0N5D6K8; -.
DR   WBParaSite; TCLT_0000867301-mRNA-1; TCLT_0000867301-mRNA-1; TCLT_0000867301.
DR   OMA; VKLGFAQ; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; 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: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   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:SF8; PARAPLEGIN; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        100..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          318..511
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          72..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   815 AA;  91210 MW;  141E1442C8E99413 CRC64;
     MIRTEFLNDY KRPSWGTKKT KTSYSDNFTV PFSFIHSLPK RYPSKAVSLL HQSFSRQSES
     YGFRRFFGTS SAVCSAPDKS DSRSEQESSK EPDDGKFKKF AVGVFIGSLV ATVIMSVITN
     IWQTRNKNQL TVQDFLTRIV PLGQIEQIIV TGNVARVIMK PGPIQNLPFN DLGYNLFKPG
     IGWQKVYVLT TMDAKKLEAD IRAVETAIGK APEEWIPVSI INASVEGFLY GYFVADSACT
     NAFRGLEISS FSEGVHLGSL QDVLGMKMKL NIINPKGTNS LKIKFKDVAG LHEAKIEIKE
     FVDYLKRPEK YTKLGARLPK GALLTGPPGC GKTFLAKALA AESSVPFISI NGTEFVEMIG
     GIHFIVYNLD DVFSFLRLGA SRIRNLFKTA KKIAPCIIYV DEIDAIGRKR SQSDFAGGGS
     REEEQTLNQL LVEMDGIDSG RGIVLLGSTN RGDILDKQKS VSGCKFFQLY MEAVDAAESV
     KCLNLLGSKK FIQALLRPGR FDRHIIIDLP TALERQEMFE LYLKKIKLDK EPQYYSKRLA
     QMTPRFSGAD IANVVNEAAI RAASLKKNLV TVDELDASLQ RILAGAEKRS RSMVEEEREI
     VAYHESGHAL IGWLLEHTDA LLRVSIIPRT SAKLGFAQYS PRERKLLTKE ECLTEMILYY
     DSNMFDRMCM LLGGRAAENI VFGRVTTGAE DDLKKVVTKS AYAQVQQYGM SEAIGPLSFP
     VTDDDKSEEG IYRKPFSMKL QHLIDQEASK LVSKAYFAAE DILKTNREKL KKLADSLLQK
     EVLRYEDMVR LIGPPKFPKQ VIELTDSVLE NLKDS
//
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