ID A0A0V1CVN1_TRIBR Unreviewed; 472 AA.
AC A0A0V1CVN1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=H/ACA ribonucleoprotein complex subunit 4 {ECO:0000313|EMBL:KRY53303.1};
GN Name=Nop60B {ECO:0000313|EMBL:KRY53303.1};
GN ORFNames=T03_359 {ECO:0000313|EMBL:KRY53303.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY53303.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY53303.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY53303.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000256|ARBA:ARBA00008999}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY53303.1}.
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DR EMBL; JYDI01000088; KRY53303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CVN1; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Ribonucleoprotein {ECO:0000313|EMBL:KRY53303.1}.
FT DOMAIN 17..75
FT /note="Dyskerin-like"
FT /evidence="ECO:0000259|SMART:SM01136"
FT DOMAIN 278..352
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT REGION 401..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 53643 MW; D2944E845E1CC76B CRC64;
MSEENWIKPS EKPPKLKTSE WPLLLKDYER LNSRSNHFTP IVAGSSPLNR NIKDYISAGF
INLDKPANPS SHEVVSWIKR ILRVPKTGHS GTLDPKVSGC LIVCIDRATR LVKSQQSAGK
EYVCVFKLHG SVESKRKVVE VYFMLFCFCL LLALERLTGA LFQRPPLISA VKRQLRIRTV
YENKLLEYDE ERNMGVFIVK CEAGTYVRTL CVHLGYILGV GGVMQELRRI RSGHTSEKDN
MVTMHDVMDA QWLYDNCQDE SYLRYVISPL EKLLVGMKRI VVKDSAVNAI CYGAKILLPG
ILKYESGIEL NDDVVVMSTK GEAVCLGIAL MTSSTIAGCD HGVVAKIKRV IMERDVYPRR
WCLGPVAMKK KQMIKAGLLD EFGKPNERTP SDWHKIYINP NVKETSESEN AENEKDKRND
DEEEDDGNQP AKKMKIETLQ TVQNDSDDEA QVEIPEKKKK KKKKKEKAFE NE
//
