ID Q16V22_AEDAE Unreviewed; 685 AA.
AC Q16V22;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=AAEL009721-PA {ECO:0000313|EMBL:EAT38370.1};
GN ORFNames=AAEL009721 {ECO:0000313|EMBL:EAT38370.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT38370.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT38370.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38370.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT38370.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38370.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EAT38370.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38370.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CH477606; EAT38370.1; -; Genomic_DNA.
DR RefSeq; XP_001654016.1; XM_001653966.1.
DR AlphaFoldDB; Q16V22; -.
DR STRING; 7159.Q16V22; -.
DR MEROPS; M41.006; -.
DR PaxDb; 7159-AAEL009721-PA; -.
DR VEuPathDB; VectorBase:AAEL013841; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_1_1; -.
DR OMA; FFFMRAQ; -.
DR PhylomeDB; Q16V22; -.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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 Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 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; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF8; PARAPLEGIN; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 133..147
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 78..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 75724 MW; 51ED0F118E83E79F CRC64;
MLRLALFKPS LTGRLLSGPL RTLSSNGSNL SNHPAAFKND NSRFQQQLNS NQLRQLNDEY
RAVLRLLSRS SGVPQHILSR SLHSSVRRFQ QNRDEGSSSG SGPDGKKPKN DDDKEKMMSL
VTKTLFWMKS VVCYHCGKPG HRKRNCKAYL AECGGNADPK RKKAKAKTVR ENDAKSFTFM
VRSGKHDASA WTQMGRAKFT LVDPVEGGRG VYFKDVAGLQ EAKQEVMEFV DYLKAPERYQ
RLGAKVPKGA LLLGPPGCGK TLLAKAVATE AAVPFLSMNG SEFIEMIGGL GAARVRDLFK
EARKRSPCII YIDEIDAIGR QRDGGGSFGG VSSGESEQTL NQLLVEMDGM ASKEGVLMLA
STNRADILDK ALLRPGRFDR HILIDLPNLT ERKEIFEKHL SGIALEASPD KYSARLATLT
PGFSGADIAN VCNEAALHAA RSSQKTVMTK NLEYAVERLV GGTEKRSHAL SPVERRVIAF
HESGHALVGW LLPNSDVLLK VTIVPRTSLA LGFAQYTPKE QKLYTKEQLF DKMCMALGGR
AAENITFNRI TTGAQNDLEK VTKMAYAQIK YFGMSSTIGP ISFSEESESD PYAGKPYSKQ
MANLFDVEAR RMITEAYEKT EQILRDNGDK LRTLAEALLE KETLNYDQVV ELIGPPLYDD
AKRKIEPVEF EDSLKKLANG GEEPK
//
