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Database: UniProt
Entry: A0A3Q1FVD7_9TELE
LinkDB: A0A3Q1FVD7_9TELE
Original site: A0A3Q1FVD7_9TELE 
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
//
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