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Database: UniProt
Entry: A0A3Q0T613_AMPCI
LinkDB: A0A3Q0T613_AMPCI
Original site: A0A3Q0T613_AMPCI 
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}.
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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
//
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