ID A0A3Q1FVD7_9TELE Unreviewed; 734 AA.
AC A0A3Q1FVD7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=SPG7 matrix AAA peptidase subunit, paraplegin {ECO:0000313|Ensembl:ENSAPOP00000021288.1};
GN Name=SPG7 {ECO:0000313|Ensembl:ENSAPOP00000021288.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000021288.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000021288.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3Q1FVD7; -.
DR Ensembl; ENSAPOT00000016709.1; ENSAPOP00000021288.1; ENSAPOG00000001741.1.
DR GeneTree; ENSGT00940000156329; -.
DR Proteomes; UP000257200; 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: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:UP000257200};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 281..421
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 693..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 152..179
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 701..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 82060 MW; 2C5C26E0AEB4D655 CRC64;
MFNDCDYYCY SNVLLHCYCN STNFVPTFPY QSFLHRPLGP GMLGLSKELI RSNLLRNPVG
LVNLLEEKKR REQDDQMYRE RLRTLFLIAL IMSLLNSLTS SGGNISWNDF VHEMLAKGEV
SRVQVVPESD IVEIYLHPGA VIFGRPRLAL MYRMQVANID KFEEKLRAAE EELNIDTKDR
IPVSYKRTGF FGNAVYALGM AAIGVAILWY IFRLAGMGGR EGGFSAFNQL KMAKFTIVDG
KSGKGVSFKD VAGMHEAKME VKEFVDYLKN PERYLQLGAK VPKGSLLLGP PGCGKTLLAK
AVATEAQVPF LAMAGSEFVE VIGGLGAARV RSLFKEARAR APCIVYIDEI DAVGKKRSTN
MSGFSNTEEE QTLNQLLVEM DGMGTTDHVI VLASTNRADI LDNALMRPGR LDRHIFIDLP
TLQERKEIFE QHLKILKLTQ PANFYSLRLA ELTPGFSGAD IANICNEAAL HAAREGYKSI
DTFNFEYAVE RVIAGSAKKS KILSKEEQRV VAFHESGHAL VGWLLEHTEA VMKVSIAPRT
NAALGFAQIL PRDQYLFTKE QLFERMCMAL GGRAAEAITF NKVTTGAQDD LRKVTRVAYS
MVKQYGMCDS VGQVSFPDTE ERGAVGRRPF SQGLQQQMDH EAKMLIARAY RHTEKLLLDN
RDKLTLLANA LLEREVVNYD DIEALLGPPP YGPKKMIMPQ SWVEAERDKQ DSGEDEPQPP
SNKHGEEDMN PQLA
//