ID G0UV31_TRYCI Unreviewed; 427 AA.
AC G0UV31;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative centromere/microtubule binding protein cbf5 {ECO:0000313|EMBL:CCC93245.1};
GN ORFNames=TCIL3000_10_40 {ECO:0000313|EMBL:CCC93245.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC93245.1};
RN [1] {ECO:0000313|EMBL:CCC93245.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC93245.1};
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 -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000256|ARBA:ARBA00008999}.
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DR EMBL; HE575323; CCC93245.1; -; Genomic_DNA.
DR AlphaFoldDB; G0UV31; -.
DR VEuPathDB; TriTrypDB:TcIL3000_10_40; -.
DR OrthoDB; 5472308at2759; -.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02572; PseudoU_synth_hDyskerin; 1.
DR CDD; cd21148; PUA_Cbf5; 1.
DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR InterPro; IPR012960; Dyskerin-like.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR004802; tRNA_PsdUridine_synth_B_fam.
DR InterPro; IPR032819; TruB_C.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR NCBIfam; TIGR00425; CBF5; 1.
DR NCBIfam; TIGR00451; unchar_dom_2; 1.
DR PANTHER; PTHR23127; CENTROMERE/MICROTUBULE BINDING PROTEIN CBF5; 1.
DR PANTHER; PTHR23127:SF0; H_ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT DKC1; 1.
DR Pfam; PF08068; DKCLD; 1.
DR Pfam; PF01472; PUA; 1.
DR Pfam; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SMART; SM01136; DKCLD; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
FT DOMAIN 29..87
FT /note="Dyskerin-like"
FT /evidence="ECO:0000259|SMART:SM01136"
FT DOMAIN 277..351
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT REGION 405..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 48375 MW; FC489305A4270549 CRC64;
MSSKRLGETQ RKEDFTIPLD GQRSECTLSP EEWPLLLKNY DKLNVRSSHF TLLECGWSPL
RRPLTEYVKY GMINLDKPSN PSSHEVVSWI KRILRCEKTG HAGTLDPKVT GALIICIDRA
TRLVKSQQNA GKTYIGVLRL HDAVGEKKVV AALQRLTGPC FQRPPLIAAV KRQLRIRNIY
SNQLIEYDKH RHLAVFETHC EAGTYIRTLC VHLGLILGVG GHMEELRRIR TGVITEDDHI
STMHDVLDAQ WLYDNEKDET YLRRVILPCE YLLTNYKRVV VKDSAVNAVC YGAKLMIPGL
ARFDNGIERD DIIVLMTTKG EAVALAYAEM STSQMASVDH GIVARSKRVI MDRDTYPRRW
GLGPVAVKKR SLVKDGLLDK YGRPQANTPS DWFYVDYGGV RTNAEGVRYG EAPKKNGKRP
RPEEGET
//
