ID F9WSH3_TRYVY Unreviewed; 794 AA.
AC F9WSH3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Upf1 domain-containing protein {ECO:0000259|PROSITE:PS51997};
GN ORFNames=TvY486_0033510 {ECO:0000313|EMBL:CCD20512.1};
OS Trypanosoma vivax (strain Y486).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Duttonella.
OX NCBI_TaxID=1055687 {ECO:0000313|EMBL:CCD20512.1, ECO:0000313|Proteomes:UP000009027};
RN [1] {ECO:0000313|EMBL:CCD20512.1, ECO:0000313|Proteomes:UP000009027}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Y486 {ECO:0000313|EMBL:CCD20512.1,
RC ECO:0000313|Proteomes:UP000009027};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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|ARBA:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01341}.
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DR EMBL; CAEX01005754; CCD20512.1; -; Genomic_DNA.
DR AlphaFoldDB; F9WSH3; -.
DR VEuPathDB; TriTrypDB:TvY486_0033510; -.
DR OMA; VRSNDNQ; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000009027; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21400; ZBD_UPF1-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR018999; UPF1_CH/ZBD.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF364; REGULATOR OF NONSENSE TRANSCRIPTS 1; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF13604; AAA_30; 1.
DR Pfam; PF09416; UPF1_Zn_bind; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51997; UPF1_CH_RICH; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01341};
KW Reference proteome {ECO:0000313|Proteomes:UP000009027};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT DOMAIN 4..157
FT /note="Upf1"
FT /evidence="ECO:0000259|PROSITE:PS51997"
FT REGION 12..44
FT /note="C3H"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 26..54
FT /note="CC/SHH/C"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
SQ SEQUENCE 794 AA; 88255 MW; 57F947DB37547465 CRC64;
MGEGRRDEGP SCAYCAESNF ETLLRCDTCD KWFCNGARAK GRAHILYHAA INRSHPFSTH
PSCPITGMRL ECAACESTNV FALRFFPGTS GARNLLICRY CFDAGSLGDV PARRSADWLP
LVRGNRVIES VCRFPSEPCS DITENDINRL EAKWRGRPEE TVQGALQSIP VTFHNCKQYS
NVFREMVLHD RRCAAAGRRS EEIRHVSCHM VGEKGSAFFY ALRPFPWKDI GLSTGDVVSV
LRNDKPMTFQ GTIAKTEKLG QEQWCIIIVT PPARDASKHE NTASFIATAV PSENEHPVTK
KLEALMRFSF ASSRCEIARA VLGHPSGRRL SPSLQFDEDD EGFKGLNESQ QAAVKAALSN
AFTLIQGPPG TGKTSTSVQI IRQLLLRKKT RVLVCAPSNA AVDHLSESMY KNKIDFIRVQ
PRYREENDSG RPYTLGSRVR EIMEAMPLNR KKRDIVKRAL ESGRLSEEEK QLCQKLEDRA
VKKILAETRV VACTCIGAGS RWLRGFKADF VLIDEASQAT EPETLVPLFR GEKQVALVGD
HRQLGPVVLS NVAGKKGFAR SLFERLAGAG SEITQLNLQY RTHPFIYRFS SMAFYGGTVL
DGVPAEKRDA SGIFPWPNPE KPMLFYDCSG VEEVGDSGAS FLNEAEARAT ISVVDAVLES
GAVRPDEVGI ISPYRAQCEY MRERLLQWGT AGKDIYEKVE ISTVDAYQGR EKEIIILSCV
RNNEERTVGF IGDERRLNVS LTRARRGLIA IGKAEALRGD KCWSKLLLYM GEHSLAVTGP
IRSLAPLEGW PNKG
//
