ID A0A2G5UCM7_9PELO Unreviewed; 744 AA.
AC A0A2G5UCM7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN Name=Cni-ppgn-1 {ECO:0000313|EMBL:PIC37279.1};
GN Synonyms=Cnig_chr_IV.g15963 {ECO:0000313|EMBL:PIC37279.1};
GN ORFNames=B9Z55_015963 {ECO:0000313|EMBL:PIC37279.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC37279.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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:PIC37279.1}.
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DR EMBL; PDUG01000004; PIC37279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5UCM7; -.
DR STRING; 1611254.A0A2G5UCM7; -.
DR Proteomes; UP000230233; Chromosome iv.
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 HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR005936; FtsH.
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 Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 109..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 315..459
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 35..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 82893 MW; B83EFC4CB9CD80EF CRC64;
MHLLLKSGWI LHRTQAFHTS VNRFSSVLPQ ILNARQFPQR RSRPKREEPA SSSEKNVYKN
PWIEISWSSK GHRETKEDAK QASEGNENGN GGGKDDDPRK KLMEKMKRWL AISLFAYGVL
FMLSPKTNGG VTADKISWSE FINELLPTGQ IYRIIVLPEQ DIAYLYVYDT GAKNSRGERL
ANMYRVGIPS VGRFETEVRA AEAALGLPPE HWTQIEYKRS ENMAQWMTII FLGGLLIGGF
LLFRKFKGSF NMTDMMSNMT KGKFTIIDPH SAEGKKQLKI KFKDVAGCSE AKVEVREFVD
YLKNPGRFTK LGAKLPRGAL LTGPPGCGKT LLAKALAAES TVPFISMNGS EFVEVIGGLG
ASRIRGLFKE ARTRAPCIIY IDEIDAIGRK RSEGKGAGGF GGGSGEEEQT LNQLLVEMDG
MGSGNGVVVL ASTNRADVLD KALLRPGRFD RHISIDLPTM LERKDMFELY MRKIKLDHAP
QEYSQRLAAM TPGFSGADIM NVCNESAIRA ASNKKHVVTI KDVEYALDRV LAGSEKRSRS
LVEEEREVVA YHEAGHALVG WMLEHTDALL KVTIIPRTSA ALGFAQYSPR DKKLFAKEEL
FDRMCMMLGG RCAENLKFGR ITSGAQDDLQ KVTKSAYAQV KLYGMSENVG PLSFPNTEGF
QIKPYSKKFA AVFDQEASLM VAKASETTTQ LIKDNMDKLE TIAQALLKRE VLNYEDVKQL
IGKPKFGDKH LIDMVENVLP KDDV
//
