ID A0A369SM26_9METZ Unreviewed; 771 AA.
AC A0A369SM26;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE SubName: Full=Paraplegin {ECO:0000313|EMBL:RDD47073.1};
GN ORFNames=TrispH2_000217 {ECO:0000313|EMBL:RDD47073.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD47073.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD47073.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD47073.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD47073.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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:RDD47073.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NOWV01000004; RDD47073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369SM26; -.
DR STRING; 287889.A0A369SM26; -.
DR Proteomes; UP000253843; 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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
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 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000253843}.
FT DOMAIN 365..487
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 131..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 87355 MW; FE5C61684370E818 CRC64;
MTNMYLVSST IRCCYRIHNN LRIGYRTLSY FTGNNYVHSN GHHGASSGRH RIHNGLSHLN
ICQISVTTHP IRNFLTIFQR PWLLANLHKA LQLNPQTLPL ANKWASQILF NLTTKYDRIL
WNKDEKFFET NQDHDQKNRH TNTDGDGKNE NNNNNNNGQF EQQNMPAWQN LILWMIIMYY
LLGNEDLVPQ ISWSTFYKEI LVTGEVRHLE INKSHDRVDV YLHDGAFISG KKISRPGPHF
CFSIPSAEMF EEKLVEAQKE IGITHNEYIP VTYQADSIFD QIAWPMMLTV VMLGFIYLAF
SRRRPNIKTG KFTKFGLAKP TIVEHPVGNI NFSKVAGMQE AKQEISEFVQ YLKSPQKFKE
LGARIPKGAL LTGPPGTGKT LLAKAVANES QVPFLSMAGS DFVEVFAGVG AARVRDLFKQ
ARGRSPKTMG GHGEQENTLN QLLVEMDGMQ SLDGVIVLAS TNRVDILDEA LLRPGRFDRT
ITIDLPTMSE RIDIFKLYLS NYVLKKKPDH YAQRLAELTP GKSGADIANI CNEAALHAAR
SSESSVDKKN FDYAIERVIV GMAKKSASIS PHERKVIAFH EAGHALTSWL LEHTDPLLKV
SIAPRTKSAL GYTQSLPSDR KLYSREQIFD IMCTTLGGRA AEMLKFKTIT TGAEDDLKKV
TDLAYKQIVE CGMNDTIGHL SFRIKKPGEW GKKPYSDKLA HIIDTEVSQL IRRAYIRTEE
ILTDNMDKLE KLANKLLKDE VLHQEDIVKV IGPPSYPYKI RDRSLSEDQF S
//