GenomeNet

Database: UniProt
Entry: E7F6D6_DANRE
LinkDB: E7F6D6_DANRE
Original site: E7F6D6_DANRE 
ID   E7F6D6_DANRE            Unreviewed;       751 AA.
AC   E7F6D6; A0A8M2BAK7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=AFG3-like protein 1 {ECO:0000313|RefSeq:XP_005163264.1};
DE   SubName: Full=Si:ch1073-174d20.2 {ECO:0000313|Ensembl:ENSDARP00000127080};
GN   Name=afg3l1 {ECO:0000313|ZFIN:ZDB-GENE-121214-51};
GN   Synonyms=si:ch1073-174d20.2 {ECO:0000313|RefSeq:XP_005163264.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000127080};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000127080, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000127080};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000127080}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000127080};
RG   Ensembl;
RL   Submitted (MAY-2013) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_005163264.1}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_005163264.1};
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   EMBL; FP245543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FP312612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005163264.1; XM_005163207.4.
DR   STRING; 7955.ENSDARP00000127080; -.
DR   PaxDb; 7955-ENSDARP00000127080; -.
DR   PeptideAtlas; E7F6D6; -.
DR   Ensembl; ENSDART00000152240; ENSDARP00000127080; ENSDARG00000079651.
DR   Ensembl; ENSDART00000152240.2; ENSDARP00000127080.1; ENSDARG00000079651.5.
DR   GeneID; 570430; -.
DR   KEGG; dre:570430; -.
DR   AGR; ZFIN:ZDB-GENE-121214-51; -.
DR   CTD; 114896; -.
DR   ZFIN; ZDB-GENE-121214-51; afg3l1.
DR   eggNOG; KOG0731; Eukaryota.
DR   HOGENOM; CLU_000688_16_2_1; -.
DR   OMA; YDKQGGG; -.
DR   OrthoDB; 9585at2759; -.
DR   PhylomeDB; E7F6D6; -.
DR   TreeFam; TF105004; -.
DR   Proteomes; UP000000437; Chromosome 25.
DR   Bgee; ENSDARG00000079651; Expressed in heart and 19 other cell types or tissues.
DR   GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
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; IPR003960; ATPase_AAA_CS.
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:SF7; AFG3-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 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.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|PeptideAtlas:E7F6D6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        100..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        206..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          292..431
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          56..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..751
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  83001 MW;  23277C7A1C58FE5B CRC64;
     MAALLSASLR GAARTALRFH TARIRSCAAH PPFSGLYGVS PLRSVGKRFT FPQSCYSTDA
     PKDAPPPGGG GGGRRGGRKS WPARLAQGDF PWDDRDFRHL LLAASGVAAL LLYLLFRDPG
     KEITWKDFVH RYLDRGLVER LEVVNKQFVR VILERDADAN EGSYVWFNIG SVDTFERNLE
     AAHYELGLEP SHRAAVVYTS ESDGSFLMSF IPTLLLIGFL LFTLRRGPMG GGMGGRRGGL
     FGMSESTAKM MKDSIEVKFK DVAGCEEAKV EIMEFVNFLK NPQQYQDLGA KIPKGAVLSG
     PPGTGKTLLA KATAGEANVP FITVNGSEFL EMFVGVGPAR VRDMFALARK NAPCILFIDE
     IDAVGKKRGG GNFGGNSEQE NTLNQLLVEM DGFNSSTNVV VLAGTNRPDV LDPALMRPGR
     FDRQIYLGPP DIKGRASIFK VHLRPLKLDP SVDRDAIARK MAAATPGFTG ADIANVCNEA
     ALIAARYLNE SVSVKHFEQA IDRVIGGLEK KTQVLQPTEK KTVAYHEAGH AVVGWFLQHA
     DPLLKVSIIP RGKGLGYAQY LPKEQYLYTR EQLFDRMCMM LGGRVAEQVF FNKITTGAHD
     DLKKVTQSAY AQIVQFGMSE RVGQVSFDLP RQGETVLEKP YSEATAELID EEVRDLVDRA
     YRRTLELVTE KREQVDMVGK RLLEKEVLDK ADMLELLGAR PFEEKSTYEE FVEGTGSFEE
     DTSLPEGLKD WNQERRGEPE EPTDSQEQRA A
//
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