ID F0VGU4_NEOCL Unreviewed; 959 AA.
AC F0VGU4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Putative cell division protein {ECO:0000313|EMBL:CBZ52938.1};
GN ORFNames=NCLIV_027270 {ECO:0000313|EMBL:CBZ52938.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ52938.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|Proteomes:UP000007494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA Wastling J.M.;
RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT Neospora caninum: Coccidia differing in host range and transmission
RT strategy.";
RL PLoS Pathog. 8:e1002567-e1002567(2012).
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; FR823389; CBZ52938.1; -; Genomic_DNA.
DR RefSeq; XP_003882970.1; XM_003882921.1.
DR AlphaFoldDB; F0VGU4; -.
DR GeneID; 13442968; -.
DR VEuPathDB; ToxoDB:NCLIV_027270; -.
DR eggNOG; KOG0731; Eukaryota.
DR eggNOG; KOG0734; Eukaryota.
DR InParanoid; F0VGU4; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000007494; Chromosome VIIb.
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; -; 2.
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:CBZ52938.1};
KW Cell division {ECO:0000313|EMBL:CBZ52938.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007494};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..959
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003262872"
FT DOMAIN 111..252
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 32..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 582..613
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 42..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 105008 MW; 3D9E2C89AC66D9CE CRC64;
MFVSFLTFRL LHSLHDGADS VDLDSTDYEG VDDEGIRPSD GGYGNQMNNT TNSSLGSNAA
SSETALVPPQ PTFPPLTFND LAGLTEAKTE LQEVVQFLRD PSKFERLGAR LPKGVLLVGP
PGTGKTALAR AVATEAGVPY FYASGSEFVE IYVGQGARRV RGLFSYARNH SPCIIFLDEL
DAVGGRRQAA GGPGAGNREH DQTLNQLLVE MDGFNQAHRI VVLAATNRVD TLDPALLRPG
RFDRIVHVSL PDVAARELIL QKYLQRVPVE PESQEGAVSG FASLVGGGDE RARAQNRAPA
SSASHSSSTS ETRGEDEKER GSEGVPGRRE ADGKAGLGPE AYRQRPDPER GTEKPVFLDK
TGAGDKDGKE DSEEPEKKRV LTQVHRDLAK QIAKITPGFS GAELENLVNE AALLAARADK
DAVTLQELHE ARDKVTMGPA RKTRIMSPYQ RQLTAYHEAG HAILAFYLQP YADPIHKATI
VSRGSALGFV EQVPLEDRYG HGVAQLEARL CVCMGGRVAE RLVFGRDALS NGASSDIETA
TRMAYVMVTE WGMSEKLGPL NYQVHGRSRR AFISSETANL VEEEVKQLVM TAERKAEKLL
RKHRRQLREV ALQLLEKETL SGEEISDILD PSGSYRSKVE RLRTRMQQGE QPSLWQRLVV
QLKRGFQWLF LPRDQTEFAA IGEADKELKA HEGTEKKQGE STSELEGKRD DGGNDDSGNG
GTESREVPPS GEVDLHRNGD GNDEHGDKDH AFSSVKELST KQSEISGAAE NGHEDGSSDN
STYLRCPRGS VAEGQHCSSF SMQGNEQDSA FSGRENSHEE PESENVSRYA EVDILPSQPM
MSRGAPSDAA ASDEALPSEG DLGQEWTHTT PRSVQRHEAF VLENRNKGSS MLERKDSSID
RREHRVGEIL SSAASQCSDS GAENCVNREA REHSRRTKRV QQWQLTPWGL GLSTVTREE
//
