ID L0B1Q0_THEEQ Unreviewed; 696 AA.
AC L0B1Q0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=ATPase, AAA family domain-containing protein {ECO:0000313|EMBL:AFZ81398.1};
DE EC=3.6.4.3 {ECO:0000313|EMBL:AFZ81398.1};
GN ORFNames=BEWA_008080 {ECO:0000313|EMBL:AFZ81398.1};
OS Theileria equi strain WA.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=1537102 {ECO:0000313|EMBL:AFZ81398.1, ECO:0000313|Proteomes:UP000031512};
RN [1] {ECO:0000313|EMBL:AFZ81398.1, ECO:0000313|Proteomes:UP000031512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA {ECO:0000313|EMBL:AFZ81398.1,
RC ECO:0000313|Proteomes:UP000031512};
RX PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT "Comparative genomic analysis and phylogenetic position of Theileria
RT equi.";
RL BMC Genomics 13:603-603(2012).
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 EMBL; CP001670; AFZ81398.1; -; Genomic_DNA.
DR RefSeq; XP_004831064.1; XM_004831007.1.
DR AlphaFoldDB; L0B1Q0; -.
DR STRING; 1537102.L0B1Q0; -.
DR MEROPS; M41.A21; -.
DR EnsemblProtists; AFZ81398; AFZ81398; BEWA_008080.
DR GeneID; 15805475; -.
DR KEGG; beq:BEWA_008080; -.
DR VEuPathDB; PiroplasmaDB:BEWA_008080; -.
DR eggNOG; KOG0734; Eukaryota.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000031512; Chromosome 3.
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: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: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 ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AFZ81398.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000031512}.
FT DOMAIN 254..390
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 696 AA; 77619 MW; 4FC414A9AE2F908F CRC64;
MAQNPTIFSG VLKSNVPVYG TISTIRSLDR RFTHSSTRIY RLRRTIEDGI QNKRLSELNL
REANAYDPRL VIRAVESCYS NTIPKDEGIL KEYLKALVFT NSLDSRSLKS LVDTNSDTLS
GEIFNDNRGN FPENKEMYLK TDDKNPIHVV VNSPNGNTNG FLKFSRRLLS IGTIALCFGT
FYLMLNQNLQ RGIKYSFKIV SPEDLDTTFD DVKVRNSYIS TLIIQGCDEV REELDEIIEY
LRNPKKFEKL GAKLPKGILL AGSPGTGKTL LARAVAGEAG VPFIHSSGSE FEEMFVGVGA
RRIRELFKTA RSISPCIVFI DELDAVGSKR SSTDHSSVRM TLNQLLVELD GFAKYDGVVV
LCATNFPESL DPALIRPGRL DKTIHIPLPD YTGRYEILKL YSKKILLSPE VDLKTIAKRT
VGMTGADIFN ILNMAALKCS IQGLASVTTS AIEEAFDRVV VGLKGKPLVN DRERTATAYH
EGGHTLVSLH TQGTTKVHKA TILPRGRTLG VTWKIPEEKY DTRMVELKSE LDVLMGGMAA
EEAIYGKENI TTGCQSDLER ATEIARTMVM KFGVGLKNVS GPMYIDTKRY PELSEELRKK
IDSAVQTLLD EAYERASSVI RNNIGQLHNL SKALVRYETL TLEEINKAVD GNIEEIAVQR
KLIQESKNTS SRLKDTINVA GDFLPEPQHS FKSHKM
//
