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Database: UniProt
Entry: A0A250WRU3_9CHLO
LinkDB: A0A250WRU3_9CHLO
Original site: A0A250WRU3_9CHLO 
ID   A0A250WRU3_9CHLO        Unreviewed;      1040 AA.
AC   A0A250WRU3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=CEUSTIGMA_g845.t1 {ECO:0000313|EMBL:GAX73392.1};
OS   Chlamydomonas eustigma.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX73392.1, ECO:0000313|Proteomes:UP000232323};
RN   [1] {ECO:0000313|EMBL:GAX73392.1, ECO:0000313|Proteomes:UP000232323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX73392.1,
RC   ECO:0000313|Proteomes:UP000232323};
RA   Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA   Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT   "Acidophilic green algal genome provides insights into adaptation to an
RT   acidic environment.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAX73392.1}.
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DR   EMBL; BEGY01000003; GAX73392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A250WRU3; -.
DR   STRING; 1157962.A0A250WRU3; -.
DR   OrthoDB; 306812at2759; -.
DR   Proteomes; UP000232323; Unassembled WGS sequence.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19501; RecA-like_FtsH; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.760; Peptidase M41; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   PANTHER; PTHR23076:SF56; INACTIVE ATP-DEPENDENT ZINC METALLOPROTEASE FTSHI 2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 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   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232323}.
FT   DOMAIN          597..736
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          60..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1040 AA;  115297 MW;  7313BD93A96640CD CRC64;
     MTIRGNLNFG RESNACRHRL LWRKGAVSRV NKSFRAKGSE REENLVLTQA SADNQVTGLL
     KSSDGRQQGH LGTEQLQPSA NTEDTSSREE HATALGLRSA FAGGKLQGET SPLVEKPTMI
     HMDPLPEKNL GALRGGRYPF VYDPVYGLPI VQEVTKYGEV LRDMREGRVK EILWFASPKN
     DNSKALDFEG RCIIRYKNES VKQAMLRPND LRLAQAMNIH AVKSVTLPLE PRYVEGLLHH
     DNPGLMNPVS RWVRENVMYL EGLEGHPQRG PRIGPTPAEE ALLPEMRDEL ERMLEEEAQQ
     VKDFSASLSR MPTEDFELYV QAEGGDSRAG EDHGSMNRRQ KVKQTSWMDS IQITQDQQAL
     ILRYAPILGP IIGSAFIIGL YMAARLVRGD LTDRMAMMNQ EDEKKKRTAL KEARIAFLEE
     EVPALVSKGT SLEDVRKKCQ TVNSKLGKLE ISDTELEGTY DACIRLLQAG EDISGVAGST
     SAADRILAEE AAKEKEAAAK EINGDGSGDA AMAAAVADMS KLNTARIRKA IDPKILEVKR
     RVRQARRSLK RESKVQLSDE IIFFDDVAGN EQAKLELQEV VDFFRQPERF KNSGAKAPKG
     VLLMGPPGNG KTLMARAVAG ESGVAFISSS ASEFIEMYMG LGAARVRDLF TTARSLAPCI
     IFIDELDAVG RARSGAGGGN DERDTTVNQL LTELDGFEAE SSGVVVMAAT NRKDVLDAAL
     TRAGRFDRSI EVRRPDFNGR LEGIKVHLRD KPLSDDIDYP LLAIMTSGLS GAQLAGVCNA
     ACFIASREGR MDVTMVDMKA AIEQSKYGKA VDLQRFISPA RRKRFAVMEA SISLVATLLP
     AIEPVDFVTI LPSLKSPIGR TVLKPNIGRY TTGMWTKRYL QEQLLVSLAG RAGEELVFGR
     DEMSSLHQSR NMLARQIATK MLNAGMSDHP DFNNLRTLGT TWYDPSFEPG RFQTYTIITD
     KNQSRSEWID MDMEMELKIR SSYEEVKALI DRNRTCLDLL IELLLRRERV TGEDIREVVE
     GAAHPEDLAK RAMEAGAAML
//
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