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Database: UniProt
Entry: A0A1X1BMI8_9APIC
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ID   A0A1X1BMI8_9APIC        Unreviewed;       644 AA.
AC   A0A1X1BMI8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   08-NOV-2023, entry version 26.
DE   RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
GN   Name=ruvbl2 {ECO:0000313|EMBL:ORM41313.1};
GN   ORFNames=BXIN_0817 {ECO:0000313|EMBL:ORM41313.1};
OS   Babesia sp. Xinjiang.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=462227 {ECO:0000313|EMBL:ORM41313.1, ECO:0000313|Proteomes:UP000193856};
RN   [1] {ECO:0000313|EMBL:ORM41313.1, ECO:0000313|Proteomes:UP000193856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinjiang {ECO:0000313|EMBL:ORM41313.1,
RC   ECO:0000313|Proteomes:UP000193856};
RX   PubMed=27784333; DOI=10.1186/s13071-016-1846-1;
RA   Guan G., Korhonen P.K., Young N.D., Koehler A.V., Wang T., Li Y., Liu Z.,
RA   Luo J., Yin H., Gasser R.B.;
RT   "Genomic resources for a unique, low-virulence Babesia taxon from China.";
RL   Parasit. Vectors 9:564-564(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|RuleBase:RU363048};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|ARBA:ARBA00007519,
CC       ECO:0000256|RuleBase:RU363048}.
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:ORM41313.1}.
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DR   EMBL; MBFZ01000031; ORM41313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1BMI8; -.
DR   VEuPathDB; PiroplasmaDB:BXIN_0817; -.
DR   OrthoDB; 5479950at2759; -.
DR   Proteomes; UP000193856; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:0008094; F:ATP-dependent activity, acting on DNA; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.50.360; RuvB-like helicase, domain II; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR002809; EMC3/TMCO1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR027238; RuvB-like.
DR   InterPro; IPR041048; RuvB-like_C.
DR   InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR   InterPro; IPR010339; TIP49_P-loop.
DR   PANTHER; PTHR11093:SF2; RUVB-LIKE 2; 1.
DR   PANTHER; PTHR11093; RUVB-RELATED REPTIN AND PONTIN; 1.
DR   Pfam; PF01956; EMC3_TMCO1; 1.
DR   Pfam; PF06068; TIP49; 1.
DR   Pfam; PF17856; TIP49_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01415; DUF106; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363048};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363048};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363048};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363048};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU363048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193856};
KW   Transcription {ECO:0000256|RuleBase:RU363048};
KW   Transcription regulation {ECO:0000256|RuleBase:RU363048};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          224..525
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          622..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   644 AA;  72348 MW;  6B8914E5DD2DC9C5 CRC64;
     MEDLLLVVSF AILSGALKEL TSYIFMYRRP DFQEKFKELT KRYEEYHRTF VIFEPRTSHR
     NCFTVVTQRL LDITKELREL QTVYNCVNGL AFMLLMLLVM SYFEGCVVAK LPFTPIWPIS
     IFTKGDAIGT DLTSCSATCI YTVLSMLVKD AIQVLLGIFD KMTHIIETSD VTKIERVGIH
     SHIRGLGLDE HLNVKYQADG LVGQVQARRA AGLVVKMMNS GVIGGRGILL AGQPGSGKTA
     IAIAISKALG EDTPFTHLSA SEVYSMEMSK TECLLQAFRR SVGVRVSEES EVIEGEVTEI
     EIDRFTNRQV DPTSFSSAPT TVGKMTIKTT DMETLYDVGH KLIEAMRREN ITAGDVIRID
     KASGTVRKLG RTYARARDYD ATGPNVKYVP CPSGELQKRQ TVTHTVTLHD IDVINSRSQG
     FLALFAGDTG EIDSQIRTQI DAKIREWQAD NRAEILPGVL FIDEAHMLDI ECFSFLCRHL
     ESEMCPFLIL ATNRGITNVR GTNYKSPHGI PLDLLDRLLI IPTYPFQPED TEKIILERCT
     EEDVELDDES LHLLCKIASE TSLRYALQLI NAGDLIRRRR GGKSVTSADV RRAFGLFVDT
     RRSTKYLVEF QHDFMFSELQ VDDDEMQAEP EAPAESQMKV DSEA
//
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