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Database: UniProt
Entry: A0A2Y9DNC1_TRIMA
LinkDB: A0A2Y9DNC1_TRIMA
Original site: A0A2Y9DNC1_TRIMA 
ID   A0A2Y9DNC1_TRIMA        Unreviewed;       794 AA.
AC   A0A2Y9DNC1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Paraplegin isoform X2 {ECO:0000313|RefSeq:XP_004377865.1};
GN   Name=LOC101348857 {ECO:0000313|RefSeq:XP_004377865.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004377865.1};
RN   [1] {ECO:0000313|RefSeq:XP_004377865.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_004377865.1; XM_004377808.3.
DR   AlphaFoldDB; A0A2Y9DNC1; -.
DR   GeneID; 101348857; -.
DR   KEGG; tmu:101348857; -.
DR   OrthoDB; 9585at2759; -.
DR   Proteomes; UP000248480; Unplaced.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
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; IPR011546; Pept_M41_FtsH_extracell.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   NCBIfam; TIGR01241; FtsH_fam; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000248480};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        145..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          341..481
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          106..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          212..239
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        107..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..794
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  88119 MW;  053EFDE500858DC1 CRC64;
     MAAVLLLLRA LRQGRRLGPG WLRSPGSGRS PGLFARVGRR RPYVTQGPPG GLAGAGGRAL
     QSLELQLLTP TFQGISGLLL KQHLIQNPVS LWKILGGTYY FNTSRMKQRN KDNDKSRAKT
     PEDDEEERKR KEREDQMYRE RLRTLFIIAV VMSLLNSLSS SGGNISWNDF VNEMLAKGEV
     QRVQVVPESD VVEVYLHPGA VVFGRPRLAL MYRMQVANID KFEEKLRAAE DELNIEVKDR
     IPVSYKRTGF FGNALYALGM TAVGLAILWY IFRLAGMTGR EGGFSAFNQL KMARFTVVDG
     KMGKGISFKD VAGMHEAKLE VKEFVDYLKS PERFLQLGAK VPKGALLLGP PGCGKTLLAK
     AVATEAQVPF LAMAGPEFVE VIGGLGAARV RSLFKEARHR APCIVYIDEI DAVGKKRSTT
     MSSFSNTEEE QTLNQLLVEM DGMGTTDHVI VLASTNRADI LDSALMRPGR LDRHVFIDLP
     TLQERREIFE QHLKSLKLTR ASSFYSQRLA ELTPGFSGAD IANICNEAAL HAAREGHTSV
     HTSNFEYAVE RVLAGTAKKS KILSKEEQRV VAFHESGHAL VGWLLEHTEA VMKVSIAPRT
     NAALGFAQML PRDQHLFTKE QLFERMCMAL GGRASEAISF NRVTSGAQDD LRKVTRIAYS
     MVRQFGMAPS IGPVSFPDAQ ESPTGIGRRP FSQGLQHLMD HEAKLLVAKA YRHTEQVLQD
     NLDKLQALAN ALLEKEVINY EDIEALIGPP PYGPKKMIMP QRWADAEREK QDSGDEEAAQ
     QPPLRGEEPD KEPS
//
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