ID A0A091RNR9_NESNO Unreviewed; 739 AA.
AC A0A091RNR9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Paraplegin {ECO:0000313|EMBL:KFQ44068.1};
DE Flags: Fragment;
GN ORFNames=N333_08513 {ECO:0000313|EMBL:KFQ44068.1};
OS Nestor notabilis (Kea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ44068.1, ECO:0000313|Proteomes:UP000053840};
RN [1] {ECO:0000313|EMBL:KFQ44068.1, ECO:0000313|Proteomes:UP000053840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ44068.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KK928487; KFQ44068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RNR9; -.
DR MEROPS; M41.006; -.
DR Proteomes; UP000053840; 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: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 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:UP000053840};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 83..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 285..425
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 53..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ44068.1"
FT NON_TER 739
FT /evidence="ECO:0000313|EMBL:KFQ44068.1"
SQ SEQUENCE 739 AA; 82898 MW; 5A5FDC4FB26DE1AF CRC64;
PQSLLSPALS PPCQGLGGVL VKQHIIRDPV RLWNLLGSTY WFTTSSCRWS NQKNGGFKKK
SPQEDDEDEK RRKKENQMHI ERLRALLIIT FIVLLFRFML SENREGTNIS WNYFVNEMLA
KGEVQRIEVV PESDIVEVYL HPGGTPHGQV NVTLLYTMRV ANIDKFEEKL RAVEDELNID
ERERIPVSYK HPGFYGNDVI SLIVTLVAVS MLWSIFRLIR VAGRVGGFNA FNQLKMARFT
IVDGKSGKGI GFKDVSGMHE AKMEVKEFVD YLKNPERYLQ LGAKVPKGAL LLGPPGCGKT
LLAKAVATEA QVPFLAMAGS EFVEVIGGLG AARVRSLFRE AQARAPCIVY IDEIDAVGKK
RSTNISGFAN AEEEQTLNQL LVEMDGMGTT DHVIVLASTN RADVLDNALM RPGRLDRHIF
IDLPTLQERR EIFEQHLKGL KLIQDASFYS QHLAELTPGF SGADIANICN EAALHAAREG
HKSIDTFNFE YAVERVIAGT AKRSQILSPE ERKVVAFHES GHALVGWLLE HTEAVMKVSI
APRTNAALGF AQILPREQYL FTKEQLMERM CMALGGRVSE AITFNKVTTG AQDDLKKVTK
IAYSMVKQYG MVPSIGQVSF PDLDSAPGIG RRPFSQGLQQ MMDHEAKVLV AQAYRRTEKL
LLENRDKLQI LSNALLEKEV INYDDIEALI GPPPYGPKKM IAPQSWLQAE RDKQDTRDEE
MPQQPPNHEE EEEPRLRPV
//
