ID Q4N6P8_THEPA Unreviewed; 806 AA.
AC Q4N6P8;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Cell division protein FtsH, putative {ECO:0000313|EMBL:EAN34360.1};
GN OrderedLocusNames=TP01_1122 {ECO:0000313|EMBL:EAN34360.1};
OS Theileria parva (East coast fever infection agent).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5875 {ECO:0000313|EMBL:EAN34360.1, ECO:0000313|Proteomes:UP000001949};
RN [1] {ECO:0000313|EMBL:EAN34360.1, ECO:0000313|Proteomes:UP000001949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Muguga {ECO:0000313|EMBL:EAN34360.1,
RC ECO:0000313|Proteomes:UP000001949};
RX PubMed=15994558; DOI=10.1126/science.1110439;
RA Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT lymphocytes.";
RL Science 309:134-137(2005).
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:EAN34360.1}.
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DR EMBL; AAGK01000001; EAN34360.1; -; Genomic_DNA.
DR RefSeq; XP_766643.1; XM_761550.1.
DR AlphaFoldDB; Q4N6P8; -.
DR STRING; 5875.Q4N6P8; -.
DR EnsemblProtists; EAN34360; EAN34360; TP01_1122.
DR GeneID; 3502999; -.
DR KEGG; tpv:TP01_1122; -.
DR VEuPathDB; PiroplasmaDB:TpMuguga_01g01122; -.
DR eggNOG; KOG0734; Eukaryota.
DR InParanoid; Q4N6P8; -.
DR OMA; QNREHDQ; -.
DR Proteomes; UP000001949; Unassembled WGS sequence.
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:0051301; P:cell division; IEA:UniProtKB-KW.
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:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 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 Cell cycle {ECO:0000313|EMBL:EAN34360.1};
KW Cell division {ECO:0000313|EMBL:EAN34360.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001949};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 159..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 263..403
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 18..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..784
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..806
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 89845 MW; 826719EC2BB5B954 CRC64;
MYNNSDHRVP VVANSRFTGH NFPEERSNID INSDNSAQTR PVYQYDDIND DPYGFSTGSG
ERDLLLSHSE VNNLFYYPNS TGINYNKPSQ QHRTGFGLHV PYECINTSKN ADSRGSSTIT
NEISSGFSSF IEFFKKLSKE ASSKSLDFLT TILSIAKSVF LYVIGIALGL FLTMFFFAMI
SHFLYNGNNI NDFKNEPKKR SPPTPPPPKT QTKQQDPPPK PEVTFEPVHF KDILGIDEAK
EDVQEIVKFI KQPFLYKKVG AKVPKGILLV GPPGTGKTML AKAVATETGI PFIYTSGPEF
VEIYVGQGAQ RIRALFHKAR KIAPCIIFID EIDAVGSKRA SGSFSGQNRE HDQTLNQLLV
EMDGFNVSTG ITILAATNRL SALDRALLRP GRFDRVVHIP LPSIKGREEI LQHYLKDVTY
NKETIDVKEL SKITPGYSGA DLKNLINEAA LITVKQDRLM VELSDLYEAR DKIIMGNKRK
LLMPDIERKM TAYHEAGHAL VAYYLYPNTD PIHKATIITR GTALGFVEQL PNDDYDKSSY
KLIEMKSRLA VCMAGRLAEK LVFGFDNVTS GASSDIIVAT DLAYKMITQY GMSNKLASLN
FHNLNNLNNK LSTDLNVKIE NEIIELIKEA EHIAESILRS KRSQLELLAS ELLKYETLTG
EQIKTLLKTN KSLNLPINGL PDHSTDVQKD AKPNPKTDSS SETSGDSESN AKTETNTDDT
PTNNENASNS YDTDVDNGTD NDNDTPNPDN NNSDMDAEDL KDDEDDDGDP NGDADDDLDD
DTEHHDVDDT SKDDEEPEDN DREEDQ
//
