GenomeNet

Database: UniProt
Entry: A0A061DDE0_BABBI
LinkDB: A0A061DDE0_BABBI
Original site: A0A061DDE0_BABBI 
ID   A0A061DDE0_BABBI        Unreviewed;      1429 AA.
AC   A0A061DDE0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=DNA repair protein rhp16, putative {ECO:0000313|EMBL:CDR97304.1};
GN   ORFNames=BBBOND_0312070 {ECO:0000313|EMBL:CDR97304.1};
OS   Babesia bigemina.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR97304.1, 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LK391709; CDR97304.1; -; Genomic_DNA.
DR   RefSeq; XP_012769490.1; XM_012914036.1.
DR   STRING; 5866.A0A061DDE0; -.
DR   EnsemblProtists; CDR97304; CDR97304; BBBOND_0312070.
DR   GeneID; 24565845; -.
DR   KEGG; bbig:BBBOND_0312070; -.
DR   VEuPathDB; PiroplasmaDB:BBBOND_0312070; -.
DR   OMA; SCWVHLD; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000033188; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16448; RING-H2; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 3.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR001510; Znf_PARP.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45626:SF12; DNA REPAIR PROTEIN RAD16; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 2.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01197; FANCL_C; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50800; SAP; 1.
DR   PROSITE; PS50064; ZF_PARP_2; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033188};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          64..100
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   DOMAIN          663..697
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          826..967
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1159..1210
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1260..1419
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          126..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1222..1243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..829
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1429 AA;  158093 MW;  3A9F43D7FFD8A36C CRC64;
     MADSNALAAW HTPSNVLYVN CLLDIGRGEW MSPSTANHFK GKRTKDIVKY KCIIRKHNRT
     AVQCQKCQRS IGKNDVIVGI PIKSIRGPYG FISLWRHVDC AVPALVCIFE LQSSKASQAA
     TGKTLAKQDG EAGTHKDNAG ASKSGKDLPS SGVKTRRGRK PKVEATTKDE AAASSADAPK
     SDGAKAKGKT AKGKAAKAAK DESGDKEDSK GTDETGKGKE EPDPLMAQLV EHAYGFDSLG
     ALQKVVVAKI RLAMEYPDEL DEEFEIRDAV ETVAITPELE SLPQPPELLV PLLPFQRDGV
     TWMYHQEKGP VKGGILADEM GMGKTIQTIA LLIAAKRDAL LAQQKAQAIE SGADAAGKST
     SRKGSASSSK EAPQVDSQVT YKPESKPESK GKKGKKSDKK DAKNVSMLNR RGCTLIVSPL
     AALLQWYNEI KTKVADGYLS VLLYHGPHRK SLTHVLHEYD VVLTTYAIVE AEFRKVQNKS
     KIACEFCGRM YLHKTLVLHQ KYFCGPTAIR TEKQRLSERK ADSGSIVLKI HARLFPDIKK
     AVDEINAKKG EADNEAYEDD DNDSSGSPKR QKVEVEMEVE EEDPEDEDYF GAKLLKIEIT
     DAFTTLGIPE KDVESALGSL SSGVKVFVEQ LKVLAEKSNV REMKQLELLE RFASSDELDM
     GLLKSTRVVE LKSLLGHFGL SAFGSKTELI NKVIVFINKM RRLSEQYSEA SIATKSAENK
     LPIGVTGGSP DGDMQNVRVK LEFDESSIKK LVSKKKILDN EEAIPDYDAT PSSMATIEAD
     NAESDGSYED DEEATVVRRR LRSGTTHKDK EASTSGGKSG RDMKRKRESI SNTAIKVKLE
     DGTGDGLATQ LPEKATEIKV KMEPDSANTN VYKPLKSHVK KETVDQKRLK PLPSASDETI
     CEGSVLHEMV WDRIVIDEAH RIKTKSNSTS QAIIRLRSSG SRWCLTGTPL QNRVGDVFSL
     ISFLKMYPFA HNFCGKYGCS CECTEFSCSD FKYCDFCGHS RILHYSYFNK RILKPILSCG
     YSNEGQVAMS ALHNDVLGKI MLRRTKAERA KDVNLPPMHV TIRRDVLSDF ERDFYEALYK
     QSAIKFDTYA RSGTLLHNYA HIFDLLTRLR QAVDHPYLIL YGPSSLAMKA SNAPDPKTKA
     ELEATVSESL PAAGSERSCG LCFDKLTDSD EFCTSNCKHS FHQPCLNDYL QSRPDDVTGD
     DNNVVTCPTC YAALTIKIRH TPQVEEDSPA RTGSDAAPHG TSKHSILQHI KLSEFKSSTK
     IEALFAEISE ILTTTTDKCL VFSQYCSMLE LISFRLKTAQ VQCAVLAGST SLEARRNMLL
     EFNNNPNLRV MLISLKAGGE GLNLQIANRI FLMDPWWNPA SELQAIQRAH RIGQTKPVYA
     VRFICKDTIE ERIIELQEKK MIVFDATISS SAESMAKLSS EDLSFLFKR
//
DBGET integrated database retrieval system