RRP5_BOVIN
ID RRP5_BOVIN Reviewed; 1874 AA.
AC A7MB10;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Protein RRP5 homolog;
DE AltName: Full=Programmed cell death protein 11;
GN Name=PDCD11;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for the generation of mature 18S rRNA, specifically
CC necessary for cleavages at sites A0, 1 and 2 of the 47S precursor.
CC Directly interacts with U3 snoRNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NF-kappa-B p50/NFKB1 and NF-kappa-B p65/RELA.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC151277; AAI51278.1; -; mRNA.
DR RefSeq; NP_001095573.1; NM_001102103.2.
DR AlphaFoldDB; A7MB10; -.
DR SMR; A7MB10; -.
DR STRING; 9913.ENSBTAP00000012818; -.
DR PaxDb; A7MB10; -.
DR PRIDE; A7MB10; -.
DR GeneID; 526867; -.
DR KEGG; bta:526867; -.
DR CTD; 22984; -.
DR eggNOG; KOG1070; Eukaryota.
DR InParanoid; A7MB10; -.
DR OrthoDB; 23482at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.40.50.140; -; 9.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045209; Rrp5.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR23270; PTHR23270; 4.
DR Pfam; PF00575; S1; 5.
DR Pfam; PF05843; Suf; 1.
DR SMART; SM00386; HAT; 7.
DR SMART; SM00316; S1; 13.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50249; SSF50249; 10.
DR PROSITE; PS50126; S1; 12.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; rRNA processing; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14690"
FT CHAIN 2..1874
FT /note="Protein RRP5 homolog"
FT /id="PRO_0000364199"
FT DOMAIN 83..171
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 187..258
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 281..346
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 365..436
FT /note="S1 motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 453..522
FT /note="S1 motif 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 542..611
FT /note="S1 motif 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 634..705
FT /note="S1 motif 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 727..796
FT /note="S1 motif 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 844..909
FT /note="S1 motif 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1034..1107
FT /note="S1 motif 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1148..1222
FT /note="S1 motif 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1230..1298
FT /note="S1 motif 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1324..1396
FT /note="S1 motif 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REPEAT 1602..1634
FT /note="HAT 1"
FT REPEAT 1708..1740
FT /note="HAT 2"
FT REPEAT 1778..1810
FT /note="HAT 3"
FT REPEAT 1812..1847
FT /note="HAT 4"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14690"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14690"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14690"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14690"
FT MOD_RES 1479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS46"
FT MOD_RES 1496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14690"
FT MOD_RES 1501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14690"
FT CROSSLNK 1028
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q14690"
FT CROSSLNK 1416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14690"
SQ SEQUENCE 1874 AA; 208543 MW; D5A3A28DC4BE595E CRC64;
MAAMEESFPR GGTRKTHKSE KAFQQSVEQD NLFDISTEEE STKRKKIQKG PAKTKKLKVE
TRQSSKFVRE KFEILNVESL CEGMRILGCV KEVNELELAI SLPNGLQGYV QVTEICDAYT
EKLNEQVAQE EPLQDLVGLP ELFSPGMLVR CVVSSLDTTK GSKKNVMLSL NPKNVNRVLS
AETLKPGMLL TGTVSSLEDH GYLVDIGVSG ARAFLPLQKA QEYIRQKNKG AKLKVGQYLN
CLIEEVKGSR GVVTLSIGHS EVSAAIATEE QSWTLNSLLP GLVVKAQVQK VTPLGLTLKF
LSFFSGLVDF MHLDPKKAGT YFSNQQVRAC VLCVHPRTRA VRLSLRPVFL QPGRPLTRLL
CQQLGAVLDD VPVQGFFGSA GATFKLKDGT LAYARRNHLS NSKKTFKPEA FKPGNTHKCR
IIDYSQMDEL ALLSLRTSII EAQFLWYHDI KPGALVKGKV LTIKPHGMVV KMGKQIRGLV
PTMHLADILI KNPEKKYHVG DEVKCRVLLC DPKAKKLMMT LKKTLVESKL PAITCYDDAK
PGLQTHGFIL RVKDYGCIVK FYNDVQGLVP RHELSAEYVP DPESVFYTGQ VVKVVVLNCE
PSKERMLLSF RLLSDPKQEG EGQSQKKKKA VSAGQLADVK VLEKTKDGLK VAVLPHNIPG
FLPTAHLSDH VTNGPLLYHW LQTGDTLHRV LCLSVSEERV LLCRKPALVS AVEGGQNPKS
FSEIHPGMLL IGFVKNIKDY GVFVQFPSGL SGLAPKAILS DKFVTSTSDH FVEGQTVVAK
VTNVDEEKQR MLLSLRLSDC TLGDLATTSL LLLSQCLEER QGVRSLMSNR DSVLIQTLAE
MTPGMALDLE VQEVLEDGSV LFSEGPVPGL VLRASKYHRA GQELEPGQKK KAVILNVDML
KLEVHVSLCH DLVNRKAKKL KKGSDLQAIV QHLEESFAVA SLVETGHLAA FSLTSHLNDT
FRFDSEKLQV GQGVSLTLQT TEPGVTGLLL AIEGPAAKRT MRQTRKDSET VDEDEEVDPA
LVVGTVKKHT LSIGDVVTGT VKSIKPTHVV VTLEDGIIGC IHASHILDDV PVGTSPTAKL
KVGKKVTARV IGGRDMKTFK FLPISHPRFI RTIPELSVRP SELKEDGHTT LNTHSVSPLE
KIKQYQPGQT VTCFLKKYNM VKKWLEVEIA PDIRGRIPLL LTSLSFKVLK HPDKKFQIGQ
ALKATVVGPA ESSKAFLCLS LIGPHKLKKG EVAMGRVVKV TPKEGLTVSF PFGRVGRVSM
FHVSDSYSET HLEDFVPQQV VRCYVLSAAT PVLTLSLRSS RTNPETKSKI TDPEINSIED
LEEGQLLRGF VKSVQPSGVL VGLGPSVTGL ARHPHVSQHN QSKNAPYDRH LPEGKLLTAK
VLRLNHQESL VELSLLPDAT GKQDVLSAPL GQPPPKQEGR ETEAVERNHE GKAKEKKKQK
QKEKRTGKGQ EGAQPPSKDK KEPQKPQAKK LGKRPHPESS SEQEIGNKKQ KKAALSEEDD
SGVEVYYREG EEAEEMSMLP KEKLTRPAEA PRLQLSSGFV WDVGLDTLTP ALPPHGDSSD
SEEDEKPEQA TQKKKSKKER ELEKQKAEKE LSRIEEALMD PGRQPESAED FDRLVLSSPS
SSLLWLQYMA FHLQATEIEK ARAVAERALK TISFREEQEK LNVWVALLNL ENMYGSQESL
TKVFERAVQY NEPLKVFLHL ADIYTKSEKF QEAGELYNRM LKRFRQEKAV WVKYGAFLLR
RGKAEASHRV MQRALECLPK KEHVDVIAKF AQLEFQLGDA ERARAIFEST LSIYPKRTDV
WSVYIDMIIK HGSQKEARAI FERVIHLSLA PKRMKFFFKR YLDYEKQHGS EKDVQAVKAK
ALEYVEAKSS MMDD
