CBF5_ASPFU
ID CBF5_ASPFU Reviewed; 487 AA.
AC O43102; Q4WTQ3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit cbf5 {ECO:0000305};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:P33322};
DE AltName: Full=Centromere-binding factor 5;
DE AltName: Full=H/ACA snoRNP protein cbf5;
DE AltName: Full=Small nucleolar RNP protein cbf5;
GN Name=cbf5; ORFNames=AFUA_5G05710;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jiang W., Clifford J., Koltin Y.;
RT "A highly conserved nucleolar protein Cbf5p may be involved in the
RT centromere DNA-binding activity of protein complex CBF3.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein
CC (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This
CC involves the isomerization of uridine such that the ribose is
CC subsequently attached to C5, instead of the normal N1. Pseudouridine
CC ('psi') residues may serve to stabilize the conformation of rRNAs and
CC play a central role in ribosomal RNA processing. The H/ACA snoRNP
CC complex also mediates pseudouridylation of other types of RNAs.
CC Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes
CC pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide
CC pseudouridylation of mRNAs. {ECO:0000250|UniProtKB:P33322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA;
CC Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:P33322};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine in snRNA = pseudouridine in snRNA;
CC Xref=Rhea:RHEA:51124, Rhea:RHEA-COMP:12891, Rhea:RHEA-COMP:12892,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:P33322};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA = a pseudouridine in mRNA;
CC Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:P33322};
CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particles
CC containing H/ACA-type snoRNAs (H/ACA snoRNPs).
CC {ECO:0000250|UniProtKB:P33322}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P33322}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; U59150; AAB94298.1; -; mRNA.
DR EMBL; AAHF01000003; EAL92023.1; -; Genomic_DNA.
DR RefSeq; XP_754061.1; XM_748968.1.
DR AlphaFoldDB; O43102; -.
DR SMR; O43102; -.
DR STRING; 330879.O43102; -.
DR EnsemblFungi; EAL92023; EAL92023; AFUA_5G05710.
DR GeneID; 3510768; -.
DR KEGG; afm:AFUA_5G05710; -.
DR VEuPathDB; FungiDB:Afu5g05710; -.
DR HOGENOM; CLU_032087_3_2_1; -.
DR InParanoid; O43102; -.
DR OMA; GPFKEDE; -.
DR OrthoDB; 1070373at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000495; P:box H/ACA RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IEA:EnsemblFungi.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central.
DR Gene3D; 2.30.130.10; -; 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 PANTHER; PTHR23127; PTHR23127; 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; SSF55120; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00425; CBF5; 1.
DR TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR PROSITE; PS50890; PUA; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Isomerase; Microtubule; Nucleus; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..487
FT /note="H/ACA ribonucleoprotein complex subunit cbf5"
FT /id="PRO_0000121977"
FT DOMAIN 273..348
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT REGION 400..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P60340"
SQ SEQUENCE 487 AA; 54726 MW; 3B38D74A4EF2FFD0 CRC64;
MAVSVTKEEM DYTIKPEAGA SNISTEDWPL LLKNYDKLMV RTGHFTPIPA GCSPLKRDLK
SYISSGVINL DKPSNPSSHE VVAWMKRILR AEKTGHSGTL DPKVTGCLIV CIDRATRLVK
SQQGAGKEYV CVIRLHDKIP GGEAQFKRAL ETLTGALFQR PPLISAVKRQ LRIRTIHESK
LYEFDNDRHL GVFWVSCEAG TYIRTLCVHL GLLLGVGAHM QELRRVRSGA MDENNGLVTL
HDVLDAQWMY DNQRDESYLR RVIQPLESLL TTYKRIVVKD SAVNAVCYGA KLMIPGLLRF
EAGIEVNEEV VLMTTKGEAI AIGIAQMSTV ELSTCDHGVV AKVKRCIMER DLYPRRWGLG
PVALEKKKLK SAGKLDKYGR ANEDTPAKWK TEYKDYSAPE EASAHAASES TAKEDVAAAL
TTEQDEAPSS PQSKMDVDET KEEKKRKRHE GETAEERAER KRKKKEKKEK KERRKSKQEK
EDSDDSD
