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
//