ID A0A3P9MXR7_POERE Unreviewed; 946 AA.
AC A0A3P9MXR7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=AFG3 like matrix AAA peptidase subunit 2 {ECO:0000313|Ensembl:ENSPREP00000002025.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000002025.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000002025.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000002025.1};
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; A0A3P9MXR7; -.
DR STRING; 8081.ENSPREP00000002025; -.
DR Ensembl; ENSPRET00000002070.1; ENSPREP00000002025.1; ENSPREG00000001470.1.
DR GeneTree; ENSGT00940000159566; -.
DR OMA; ARQKGNF; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000001470; Expressed in caudal fin and 1 other cell type or tissue.
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:UP000242638};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 213..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 410..549
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 105406 MW; 4DEFC01954066113 CRC64;
MENVADLPDE YGGSSSSQGG RGFSSFSAVP FRACRRRGHL YQTLTEEEGV EETCRRRWMI
TERLFWTRSV FRTPPSLSAM AHRYLRLPAG CGSLVRLLLR PCGAPARTVS PAGSGRVRSG
PDPLSELLGA SRILSSKPPK GFEKYFPESQ NRARTSEPEA KGKEDTESKP AQKPSGKPGG
SGSGGGKRGG RKEENHWYSR LQKGDVPWDD KEFRLYLLTG VAFWTAITYY FFLRDGGREV
TWKDFVNNYL SKGAVERLEV VNKRYVRVAF SPGKTPLDGQ YVWFNIGSVD TFERNLETAQ
SELGIESENR LPVVYSTESD GSFLLSMLPT ALIIGFLLFM LRRGPAGGGR PGRGMGGLFS
VSETTAKILK DEIDVKFKDV AGCEEAKLEI MEFVNFLKNP KQYQDLGAKI PKGAILTGPP
GTGKTLLAKA TAGEANVPFI TVNGSEFLEM FVGVGPARVR DLFVMARKNA PCILFIDEID
AVGRKRGRGN FGGQSEQENT LNQLLVEMDG FNTATNVVVL AGTNRPDILD PALLRPGRFD
RQIYIGPPDI KGRASIFKVH LRPLKLSTDL DKDALAKKMA ALTPGFSGAD IANVCNEAAL
IAARHLSDTI NQKHFEQAIE RVIGGLEKKT QVLQPEEKKT VAYHEAGHAV AGWFLEHADP
LLKVSIIPRG RGLGYAQYLP REQYLYTKEQ LQDRMCMTLG GRVAEEIFFG RVTTGAQDDL
RKVTQSAYAQ IVQFGMNPKV GQVSFDLPRQ GEMVLEKPYS EATARLIDSE VRTLIGEAYR
RTQLLLTDKK AEVDKVAQRL LQREVLSKED MEELLGRRPF AERSTYEELV EGTGGEDEDT
ALPDGLRDWN QDRNQDRNQE SPEEQNLSRY SPAVRKMFHQ NIWHRSDGET IGPEFYWVQH
PVPQRDFQLG PSRTTVLQPL DASLLQQTRT RQPGSEVRFR SGTGNF
//
