ID A0A026W098_OOCBI Unreviewed; 747 AA.
AC A0A026W098;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=ATP-dependent zinc metalloprotease YME1-like protein {ECO:0000313|EMBL:EZA49447.1};
GN ORFNames=DMN91_009351 {ECO:0000313|EMBL:RLU18993.1}, X777_11945
GN {ECO:0000313|EMBL:EZA49447.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA49447.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA49447.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
RN [2] {ECO:0000313|EMBL:RLU18993.1, ECO:0000313|Proteomes:UP000279307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU18993.1};
RX PubMed=30249741; DOI=10.1101/gr.237123.118;
RA McKenzie S.K., Kronauer D.J.C.;
RT "The genomic architecture and molecular evolution of ant odorant
RT receptors.";
RL Genome Res. 28:1757-1765(2018).
RN [3] {ECO:0000313|EMBL:RLU18993.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU18993.1};
RA Mckenzie S.K., Kronauer D.J.C.;
RL Submitted (JUL-2018) 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; KK107519; EZA49447.1; -; Genomic_DNA.
DR EMBL; QOIP01000009; RLU18993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026W098; -.
DR STRING; 2015173.A0A026W098; -.
DR MEROPS; M41.A11; -.
DR EnsemblMetazoa; XM_020033378.2; XP_019888937.1; LOC105284713.
DR OMA; VNRITAY; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR Proteomes; UP000279307; Chromosome 9.
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: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 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; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF37; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:EZA49447.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EZA49447.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 249..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..463
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 747 AA; 83692 MW; D45085EBA2ACCDE9 CRC64;
MVSLQSHNQV LYHLTQLTLA VTPRTTSVQI IRPDKSLQKN ADDICRDSLE EAARNCTELP
EISLNALSML RLKEDKVCMM LDDIAVSILG KPLNETNKWR VSYLSGLSFT ENKQGFSCSP
LMEPIILPAI HLASKQQRKL LHTWHVKALR NHSHVPIRTF KSQRSIKMEL EQNRPFMSRL
KKWLGLSSNV QVNMQDLKKT DYDRLKQIFN STETDEQKRM KLAFAEGYES GLLRQSRGQY
FVLKIMQRLI TLFIIISLIL GISLYVSYPG GGVFKLSMGH RIEINPEDIN VTFSDVKGVD
EAKQELLNVV EFLKNPDKFS ALGGKLPKGV LLVGPPGTGK TLLARAVAGE AGVPFFHVAG
PEFDEILVGQ GARRVRDLFR AAKEKAPCVV FIDEIDSVGA KRTNSVLHPY ANQTINQLLS
EMDGFRQNEG VIVLGATNRR KDLDKALMRP GRFDVEIYVN KPDYLGRKEI LDLYLSRILT
HDIDTVYLAR CTTGFTGADI ENMVNQAALR AAIDEADYVT MKHLEYARDK VLMGPEGKLK
SRDEEVNRIT AYHEAGHALV AFYTKDATPL HKVTIVPRGP SLGHTSFMHE KDVYYTTRAQ
LLATLDSMMG GRAAEELVYG TDKITTGASS DLMEATKIAE TMVKNFGMSD KVGFRSISDG
KEFFGNGITY AASTTEAIDY EVKRLLQESY ERAKTILKTH AKEHKQLAEA LLQYETLDAE
DVAAIANDTG LSKRDFTGDS KRLTKES
//
