ID A0A061D8V1_BABBI Unreviewed; 403 AA.
AC A0A061D8V1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE SubName: Full=LytB protein, putative {ECO:0000313|EMBL:CDR96397.1};
GN ORFNames=BBBOND_0303010 {ECO:0000313|EMBL:CDR96397.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR96397.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; LK391709; CDR96397.1; -; Genomic_DNA.
DR RefSeq; XP_012768583.1; XM_012913129.1.
DR AlphaFoldDB; A0A061D8V1; -.
DR STRING; 5866.A0A061D8V1; -.
DR EnsemblProtists; CDR96397; CDR96397; BBBOND_0303010.
DR GeneID; 24564938; -.
DR KEGG; bbig:BBBOND_0303010; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0303010; -.
DR OMA; DSICRQV; -.
DR OrthoDB; 226678at2759; -.
DR Proteomes; UP000033188; Chromosome 3.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:InterPro.
DR CDD; cd13944; lytB_ispH; 1.
DR Gene3D; 3.40.50.11270; -; 1.
DR Gene3D; 3.40.1010.20; 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, catalytic domain; 2.
DR HAMAP; MF_00191; IspH; 1.
DR InterPro; IPR003451; LytB/IspH.
DR NCBIfam; TIGR00216; ispH_lytB; 1.
DR PANTHER; PTHR30426; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR30426:SF0; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1.
DR Pfam; PF02401; LYTB; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000033188};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..403
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001595574"
SQ SEQUENCE 403 AA; 44334 MW; 268F7D13F6C19699 CRC64;
MYGVIFLALS VLSVECLSVH RPGFVLRKAG NAFVVRDHRF GGRWSNHAAL NQQSTSLEAN
VCEESGSQTR DAPAVANSSK TLYLVNPRGF CEGVRRAIRT VEEAVRLFGP PVYVKHEIVH
NEFVCNRLRA KGVIFIEDLE TVPEGSTLIF SAHGVSPAVK ELARKRNFVE IDASCPLVNK
VHVYVKKKAE EGYKIVLIGH KNHVETIGTA GEAPGVTTVV ETVDDVDQLD YPEGTPLFYA
TQTTLSLDDC KVIKDRLLER FPWIETIPSG SICYATTNRQ TAVQKVCAVC DLMLVVGSTL
SSNAKRLLET ATVRNIRGYL IPNADAVTEE MIGNATRVAV SSSASTPEEL TNGVVEKLAS
PPFNFSVEFF DGGEERVPKW RLPRNLETFI KEHDSKTEAA EAQ
//
