ID A0A3Q0T613_AMPCI Unreviewed; 691 AA.
AC A0A3Q0T613;
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=Si:ch1073-174d20.2 {ECO:0000313|Ensembl:ENSACIP00000027580.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000027580.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000027580.1}
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: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q0T613; -.
DR STRING; 61819.ENSACIP00000027580; -.
DR Ensembl; ENSACIT00000028309.1; ENSACIP00000027580.1; ENSACIG00000021343.1.
DR GeneTree; ENSGT00940000160625; -.
DR OMA; YDKQGGG; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 231..370
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 76730 MW; C4C57FCBFDCD1558 CRC64;
LERNCNNNKT RPAGGGGGKR GGKDWWSRMQ KGDFPWDEKD FRYVAITVAG VSSALLYFYF
RDSGKEISWK DFVHRYLGRG KVDRLEVVNK QYVRVVLVPG ADSYVWFNIG SVDTFERNLE
TAVMELGMES TRRPAVIYSS ESDGSFLMSM IPTLLLIGFL LFTLRRGPMG GGAGGGRNPF
SMSESTAKMM RDNIEVKFKD VAGCEEAKLE IMEFVNFLKN PQQYQDLGAK IPKGAMLSGP
PGTGKTLLAK ATAGEANVPF ITVNGSEFLE MFVGVGPARV RDMFAMARKN APCILFIDEI
DAVGRKRGGG NFGGQSEQEN TLNQLLVEMD GFNTATNVVV LAGTNRPDIL DPALLRPGRF
DRQIYIGPPD IKGRASIFKV HLQPIKLDPD LDKDALARKM AAATPGFTGA DIANVCNEAA
LIAARHLNPS INAKHFEQAI DRVIGGLEKK TQVLQPTEKK TVAYHEAGHA VVGWFLQHAD
PLLKVSIIPR GKGLGYAQYL PREQYLYTRE QLFDRMCMML GGRVAEQVFF SRITTGAQDD
LKKVTQSAYA QVVQFGMSEK VGQVSFDLPR QGEVVMEKPY SEATAELIDE EVRGLVNRAY
ERTLQLIEEK KDLVELVGKR LLEREVLNKA DMLELLGPRP FEEKSTYEEF VEGTGSFEED
TSLPEGLRDW NQERGGEAEE ASPNQDKQQA V
//