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Database: UniProt
Entry: A0A085MWJ6_9BILA
LinkDB: A0A085MWJ6_9BILA
Original site: A0A085MWJ6_9BILA 
ID   A0A085MWJ6_9BILA        Unreviewed;      1462 AA.
AC   A0A085MWJ6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN   ORFNames=M514_04173 {ECO:0000313|EMBL:KFD61592.1};
OS   Trichuris suis (pig whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD61592.1};
RN   [1] {ECO:0000313|EMBL:KFD61592.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD61592.1};
RX   PubMed=24929829; DOI=10.1038/ng.3012;
RA   Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA   Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA   Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT   "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL   Nat. Genet. 46:701-706(2014).
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; KL367618; KFD61592.1; -; Genomic_DNA.
DR   MEROPS; M41.A10; -.
DR   Proteomes; UP000030758; 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:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04094; eSelB_III; 1.
DR   CDD; cd19501; RecA-like_FtsH; 1.
DR   CDD; cd00165; S4; 1.
DR   CDD; cd03696; SelB_II; 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; 2.
DR   Gene3D; 1.20.58.760; Peptidase M41; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
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; IPR049394; eEFSec_C.
DR   InterPro; IPR049393; eEFSec_III.
DR   InterPro; IPR004161; EFTu-like_2.
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   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
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; PF21131; eEFSec_4th; 1.
DR   Pfam; PF21208; euk_SelB_III; 1.
DR   Pfam; PF06480; FtsH_ext; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   Pfam; PF01479; S4; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00674; AAA; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS50889; S4; 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   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        788..808
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        897..914
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..210
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          581..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1427..1462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..754
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1462 AA;  162751 MW;  AD9B5F69C95DA66C CRC64;
     MTVRDATAAG TPRVLNFNVG ILGHVDSGKT ALAKAISKVA GTAAFDKHPE SRRRGITIDL
     GFSCFTVPVT EQMTIRDEQL MNYDVIQVTL VDCPGHSSLF RTVIGCSQIV DMVFLIVDIQ
     KGIQPQTADC IVLANITCPS KMLIALNKVD TLPAEDRSNV IAMTERRIRR ALARTTFRNV
     PMVPISVVPP DANSIDRFMD AFALSIYVPD RTVAANDPFM FYFDHCFSLR GKGTVVTGTV
     ISGKLTQGQT VEIPMAQQTR KVKTIESFHR PVSSIGPGDR AGLCLSQSST YNLDRGLLCE
     PGALKMSYGA IVTLKRVPYY KFSIASRLQF QICIGYETIP AKCCFFACEP GKCIQDDKVL
     SFKKEGEYAW VHEVHKSNEE AENACHLFAL LRFTRGIYCA LGCNYLGTKL EIEPSSSVCR
     IAFYGRTLHL FEDPKFRGTK INWLNVYKPR VRRGVVERIK DEKYATVRDM FRKGCNIEPY
     LGCNVTLSTG EVGRLESSFG QGGKVTVFLP GGAKKSTINT VSKQSKNLDD DLVQLSRMAT
     TRSLVRWLRL ARTTARPTTM TNRFAPIQPI PRADDVTQRA MHTSGALRRK QKVPKKPTYE
     DDDVEVEDNV DDLIDEVDGS AIRCVNVKRP RLDAILKIGC NVSRNSADEV VSEGRVFVNG
     RRALKKSLEF FNSFAFVSFL PPQTEAMLST LLPRMLRRLA GRALPTTGNR YIVCCYFSSD
     RPKGFGRFYP GAEGERKDEP KKEEKAEQPP EKADSEPNPS DWQGFFKRPP FAQVRTGGPG
     GGEQDNRWLL SAVSIGASMA AIVVLYYYMG YREITWKEFV NSYLSKGAVD KLEVVNKKWV
     RVYLNPLTAA EPKIPWFNIG SVDSFERLLE NIQKDLNIDA RNYIAVVYKN EVDSNSIISN
     LPSILLFLFF LWGMRRFSSF AGMARGGRGA SGGIFGFGAS TARVIKQGDI KVRFKDVAGC
     EEAKLEIMEF VNFLKNPQQY MKLGAKIPKG AILTGPPGTG KTMLAKATAG EANVPFITVS
     GSEFLEMFVG VGPARVRDMF AMARKKAPCI LFIDEIDAVG RIRGQRFSSG GSEQENTLNQ
     LLVEMDGFQT GQANVIVMAA TNRVDMLDKA LLRPGRFDRQ IYVPAPDIKG RASIFRVHLS
     PLAAEPDKTE LSRKLAALTP GFTGADIANV CNEAALIAAR DLNEKIKMKH FEQAVERVVA
     GMEKKSQVLQ LEEKTTVAYH EAGHAVTGWF LEHADPLLKV SIIPRGKGLG YAQYLPKEQY
     LYTKEQLFHR MCMTLGGRAS EEIFFGRIST GAQDDLQKIT QMAYAQVIKF GMSEKVGPLS
     FQTPEAGDVV IDKPYSEQTA QLIDQEVRTI VSNALQFTRK MVEEHREGVE KVVLLLNDFQ
     VVYGVFFCWQ VAKRLLEREV LAREDLIELL GQRPFPEKHT YEQFVEGTGG LDDDVSVPEG
     LKHWNEPKQE QPAAASEKAN AL
//
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