ID A7ARW4_BABBO Unreviewed; 438 AA.
AC A7ARW4;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=26S protease regulatory subunit 4, putative {ECO:0000313|EMBL:EDO07283.1};
GN ORFNames=BBOV_IV009290 {ECO:0000313|EMBL:EDO07283.1};
OS Babesia bovis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5865 {ECO:0000313|EMBL:EDO07283.1, ECO:0000313|Proteomes:UP000002173};
RN [1] {ECO:0000313|EMBL:EDO07283.1, ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2Bo {ECO:0000313|EMBL:EDO07283.1};
RX PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA Nene V.M.;
RT "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT hemoprotozoa.";
RL PLoS Pathog. 3:1401-1413(2007).
RN [2] {ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33294524; DOI=10.1016/j.dib.2020.106533;
RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT "Transcriptome dataset of Babesia bovis life stages within vertebrate and
RT invertebrate hosts.";
RL Data Brief 33:106533-106533(2020).
RN [3] {ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33069745;
RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT "Comparative analysis of gene expression between Babesia bovis blood stages
RT and kinetes allowed by improved genome annotation.";
RL Int. J. Parasitol. 51:123-136(2021).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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:EDO07283.1}.
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DR EMBL; AAXT01000002; EDO07283.1; -; Genomic_DNA.
DR RefSeq; XP_001610851.1; XM_001610801.1.
DR AlphaFoldDB; A7ARW4; -.
DR STRING; 5865.A7ARW4; -.
DR EnsemblProtists; EDO07283; EDO07283; BBOV_IV009290.
DR GeneID; 5479085; -.
DR KEGG; bbo:BBOV_IV009290; -.
DR VEuPathDB; PiroplasmaDB:BBOV_IV009290; -.
DR eggNOG; KOG0726; Eukaryota.
DR InParanoid; A7ARW4; -.
DR Proteomes; UP000002173; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19502; RecA-like_PAN_like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 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:0000313|EMBL:EDO07283.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:EDO07283.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000002173}.
FT DOMAIN 216..355
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 438 AA; 49087 MW; AAB78FEB9F0CB1B0 CRC64;
MGNAQGDLNN NQESKKNEDS TPREKPPPPV FGKHKKKQQR QFAPVRIPTV TPSAKCRLRL
LKLERIKDYL LLEEEYVANK IRLNPTKNKN QDDLLRLEDL RGSPMSVGTM EEMIDDNHAI
VTSSMGPEYY VNILSFVDKT LLEPGCSVLL HNKTNSVVGI LLDAIDPLVS LMKVERAPLE
SYSDIGGLED QIQEIKEAVE LPLTHPELYE EVGIRPPKGV ILYGPPGTGK TLLAKAVANE
TCATFLRVVG SELIQKYLGE GPKLVREMFR VAEENAPSII FIDEIDAIGT KRYDATSGGE
KEIQRTMLEL LNQLDGFDPQ ADVKVIMATN RIESLDPALI RPGRIDRKIQ LPNPDTKTKR
KIFEIHTSKM TMSSDVDLEE FVNTKDDLCG ADIKAICTEA GLLALRERRM QITQADLRKA
REKALQLKKG NIPESMYC
//
