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Database: UniProt
Entry: A0A3Q2VJF2_HAPBU
LinkDB: A0A3Q2VJF2_HAPBU
Original site: A0A3Q2VJF2_HAPBU 
ID   A0A3Q2VJF2_HAPBU        Unreviewed;       799 AA.
AC   A0A3Q2VJF2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=AFG3 like matrix AAA peptidase subunit 2 {ECO:0000313|Ensembl:ENSHBUP00000008168.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000008168.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000008168.1}
RP   IDENTIFICATION.
RG   Ensembl;
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_005946480.1; XM_005946418.2.
DR   AlphaFoldDB; A0A3Q2VJF2; -.
DR   STRING; 8153.ENSHBUP00000008168; -.
DR   Ensembl; ENSHBUT00000002412.1; ENSHBUP00000008168.1; ENSHBUG00000009683.1.
DR   GeneID; 102311965; -.
DR   CTD; 10939; -.
DR   GeneTree; ENSGT00940000159566; -.
DR   OMA; ARQKGNF; -.
DR   OrthoDB; 9585at2759; -.
DR   Proteomes; UP000264840; 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; 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:SF9; AFG3-LIKE PROTEIN 2; 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   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:UP000264840};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        137..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          334..473
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          59..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   799 AA;  88387 MW;  1FF7B06CA536B959 CRC64;
     MAHRYLRLSA GCRGLFRLLP PSGAPARLVT SSTTAQVQSG RSLLSDLLGA YRRLSSKPPK
     GFEKYFPDSQ KTQKHSEAEA AAKESKPANS QRASGRSTGG GGGAGGGGGG KRGGRKDESH
     WYSRLQKGEV PWDDREFRMY FLSGVAFWTT VTYYFFLRDG GREVTWKDFV NNYLSKGVVD
     RLEVVNKRYV KVVFSAGKTP ADGQYVWFNI GSVDTFERNL ETAQYELGIE GENRLPVVYS
     TESDGTFLLS MLPTVLIIGF LLFMLRRGPA GAGRPGRGMG GLFSVSETTA KILKDEIDVK
     FKDVAGCEEA KLEIMEFVNF LKNPKQYQDL GAKIPKGAIL TGPPGTGKTL LAKATAGEAN
     VPFITVNGSE FLEMFVGVGP ARVRDLFVMA RKNAPCILFI DEIDAVGRKR GRGNFGGQSE
     QENTLNQLLV EMDGFNTATN VVVLAGTNRP DILDPALMRP GRFDRQIYIG PPDIKGRASI
     FKVHLRPLKL EPDMDKDSLA RKMAALTPGF SGADIANVCN EAALIAARHL SDAISQKHFE
     QAIERVIGGL EKKTQVLQPE EKKTVAYHEA GHAVAGWFLE HADPLLKVSI IPRGKGLGYA
     QYLPKEQYLY TKEQLLDRMC MTLGGRVSEE IFFGRITTGA QDDLRKVTQS AYAQIVQFGM
     NPKVGQVSFD LPRQGEMVLE KPYSEATARL IDTEVRTLIS EAYQRTQQLL NDKKAEVEKV
     AQRLLEKEVL DKNDMVELLG KRPFAEKSTY EEFVEGTGGE DEDTALPEGL KDWNQERRPE
     REETPDEQVA RQISGGMPF
//
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