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Database: UniProt
Entry: A0A369SM26_9METZ
LinkDB: A0A369SM26_9METZ
Original site: A0A369SM26_9METZ 
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}.
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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
//
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