ID Q387H5_TRYB2 Unreviewed; 984 AA.
AC Q387H5;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=DNA repair protein, putative {ECO:0000313|EMBL:EAN79056.1};
GN ORFNames=Tb11.03.0400 {ECO:0000313|EMBL:EAN79056.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000313|EMBL:EAN79056.1, ECO:0000313|Proteomes:UP000008524};
RN [1] {ECO:0000313|EMBL:EAN79056.1, ECO:0000313|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN79056.1,
RC ECO:0000313|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
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DR EMBL; CH464491; EAN79056.1; -; Genomic_DNA.
DR RefSeq; XP_828168.1; XM_823075.1.
DR AlphaFoldDB; Q387H5; -.
DR STRING; 185431.Q387H5; -.
DR PaxDb; 5691-EAN79056; -.
DR GeneID; 3665848; -.
DR KEGG; tbr:Tb11.03.0400; -.
DR VEuPathDB; TriTrypDB:Tb927.11.750; -.
DR eggNOG; KOG1002; Eukaryota.
DR InParanoid; Q387H5; -.
DR OrthoDB; 11932at2759; -.
DR Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR GO; GO:0031981; C:nuclear lumen; IDA:GeneDB.
DR GO; GO:0000113; C:nucleotide-excision repair factor 4 complex; ISA:GeneDB.
DR GO; GO:0005634; C:nucleus; IDA:GeneDB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISA:GeneDB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; ISM:GeneDB.
DR GO; GO:0044145; P:modulation of formation of structure involved in a symbiotic process; IMP:GeneDB.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0009372; P:quorum sensing; IMP:GeneDB.
DR CDD; cd18008; DEXDc_SHPRH-like; 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; 2.
DR Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
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; 3.
DR Pfam; PF00645; zf-PARP; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM01336; zf-PARP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50064; ZF_PARP_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 29..77
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 157..522
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 678..709
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 692..735
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 820..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 287..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 110754 MW; 2FF1CAA9398A926C CRC64;
MTSKHSAVLT ITEKGDWRTA KNGEKVWRYM VQTAPTMRAR CRKCSQPILK GDLKWGTPIR
HSHGAYGWIT AWHHVGCTRI AERKGFSDIV HGIDLLPPEK RAQVVAEVTS DSMPEHLLPL
NPDDLVKKPL LPETEAPAEL LRPLLRYQKE GLGWMVSQEL SQVKGGILAD EMGMGKTIQM
ISLFLARRLV GPTLVVCPVS SMLQWESEVK DHVVSGSLSV VVVSRTKNVR RDDIQNADVV
LTTYPMLEQS WRELVNKKRV PCPYCQQLYL PRQLVVHNRY FCGPHAKKTS KQAKREKRQG
GTGSSPTRKV QAKETIMKGL RTLRVDVDDN AEEGEDSVFE EGPRGVVGPM GLYRELMVEA
GRKVRSRWDP AYVGSDSSGD TNNSTTESST SSERDDSEEV LSKEEVADDK LSSFRCLHCG
FQLLRYPFCP KIGQCHVLSD YMKQIIETDD GSDGVDLSQS VFHSVTWSRI VLDEAHRIKG
SNTSTSRAAF ALVGEHRWCL TGTPLQNRVG DVYSLVRFLR LAPYARYYCG TEGCSCSSFS
HPFSGNDLRH CIFCGHGPVQ HYAYFNRHIL NPIIRYGYVG DGRRGMMMLS NEILQKCMLR
RTKAERASDL HLPPMTVETF QVKLTDEERS FYESLYKKST AAFDTFVEKG TVLHNYAHIF
QLLSRLRQAL DHPLIVINSM NVGGSSCSKG MCGICTESCG ENSVQVDPCK HTFHRICLSQ
FVESQPLKEY NCPVCYVAIN IDLRSLHSGW DEDGAQPVLP PELVHSDNES DENNVEEESK
GRKLDDSAEG KSARARSVKK RGILSRIDSS KPLRGTKLDA ITEYICSIPE EEKVIVFSQF
GDTLDLIQLW LQKVKVKTVK LVGSLMLSQR QAVLRAFLHD KSVRAILISL KAGGEGLNLQ
IANHVVLVDP WWNPAVEMQA AQRAHRIGQT RPVRVVRFVT ERSVEERMLE LQEKKMLVIE
GTIDGKVSSL QSLSEDDLQF LFTR
//
