Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

60 kDa SS-A/Ro ribonucleoprotein

Gene

trove2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs. May stabilize some of these RNAs and protect them from degradation.2 Publications
May play roles in cilia formation and/or maintenance.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi378Divalent metal cation2 Publications1
Metal bindingi380Divalent metal cation2 Publications1
Metal bindingi445Divalent metal cation2 Publications1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • misfolded RNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
60 kDa SS-A/Ro ribonucleoprotein
Short name:
60 kDa Ro protein
Short name:
60 kDa ribonucleoprotein Ro
Short name:
RoRNP
Alternative name(s):
TROVE domain family member 2
Gene namesi
Name:trove2
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-968761. trove2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001741711 – 53860 kDa SS-A/Ro ribonucleoproteinAdd BLAST538

Proteomic databases

PRIDEiP42700.

Structurei

Secondary structure

1538
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 21Combined sources3
Beta strandi23 – 26Combined sources4
Helixi29 – 39Combined sources11
Beta strandi46 – 48Combined sources3
Helixi50 – 66Combined sources17
Turni67 – 69Combined sources3
Helixi70 – 83Combined sources14
Helixi90 – 100Combined sources11
Beta strandi101 – 103Combined sources3
Helixi105 – 118Combined sources14
Helixi122 – 134Combined sources13
Helixi146 – 157Combined sources12
Helixi161 – 168Combined sources8
Beta strandi174 – 176Combined sources3
Helixi179 – 185Combined sources7
Helixi193 – 203Combined sources11
Helixi206 – 212Combined sources7
Turni213 – 215Combined sources3
Helixi220 – 236Combined sources17
Helixi241 – 251Combined sources11
Helixi255 – 257Combined sources3
Helixi262 – 264Combined sources3
Helixi266 – 274Combined sources9
Helixi278 – 290Combined sources13
Turni291 – 294Combined sources4
Helixi299 – 308Combined sources10
Helixi311 – 316Combined sources6
Helixi321 – 333Combined sources13
Helixi347 – 359Combined sources13
Beta strandi371 – 376Combined sources6
Helixi379 – 382Combined sources4
Beta strandi383 – 385Combined sources3
Helixi392 – 406Combined sources15
Beta strandi408 – 420Combined sources13
Helixi430 – 437Combined sources8
Helixi449 – 456Combined sources8
Beta strandi462 – 468Combined sources7
Beta strandi474 – 476Combined sources3
Helixi479 – 490Combined sources12
Beta strandi495 – 500Combined sources6
Beta strandi502 – 509Combined sources8
Beta strandi516 – 520Combined sources5
Helixi526 – 534Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YVPX-ray2.20A/B1-538[»]
1YVRX-ray1.95A1-538[»]
2I91X-ray2.65A/B1-538[»]
ProteinModelPortaliP42700.
SMRiP42700.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42700.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 369TROVEPROSITE-ProRule annotationAdd BLAST354

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni120 – 284RNA-binding2 PublicationsAdd BLAST165
Regioni361 – 538VWFA-like domainCuratedAdd BLAST178

Domaini

The horseshoe-shaped TROVE domain is built with 7 helical HEAT-like repeats, and is closed by the VWFA-like domain giving rise to a ring-shaped monomer. Single-stranded RNA is bound in the positively charged central cavity.
The MIDAS-like motif in the VWFA-like domain binds divalent metal cations.2 Publications

Sequence similaritiesi

Belongs to the Ro 60 kDa family.Curated
Contains 1 TROVE domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG013234.
KOiK11089.

Family and domain databases

InterProiIPR008858. TROVE_dom.
IPR002035. VWF_A.
[Graphical view]
PfamiPF05731. TROVE. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50988. TROVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEATMDQTQP LNEKQVPNSE GCYVWQVSDM NRLRRFLCFG SEGGTYYIEE
60 70 80 90 100
KKLGQENAEA LLRLIEDGKG CEVVQEIKTF SQEGRAAKQE PTLFALAVCS
110 120 130 140 150
QCSDIKTKQA AFRAVPEVCR IPTHLFTFIQ FKKDLKEGMK CGMWGRALRK
160 170 180 190 200
AVSDWYNTKD ALNLAMAVTK YKQRNGWSHK DLLRLSHIKP ANEGLTMVAK
210 220 230 240 250
YVSKGWKEVQ EAYKEKELSP ETEKVLKYLE ATERVKRTKD ELEIIHLIDE
260 270 280 290 300
YRLVREHLLT IHLKSKEIWK SLLQDMPLTA LLRNLGKMTA DSVLAPASSE
310 320 330 340 350
VSSVCERLTN EKLLKKARIH PFHILVALET YKKGHGNRGK LRWIPDTSIV
360 370 380 390 400
EALDNAFYKS FKLVEPTGKR FLLAIDVSAS MNQRVLGSIL NASVVAAAMC
410 420 430 440 450
MLVARTEKDS HMVAFSDEML PCPITVNMLL HEVVEKMSDI TMGSTDCALP
460 470 480 490 500
MLWAQKTNTA ADIFIVFTDC ETNVEDVHPA TALKQYREKM GIPAKLIVCA
510 520 530
MTSNGFSIAD PDDRGMLDIC GFDSGALDVI RNFTLDLI
Length:538
Mass (Da):60,688
Last modified:November 1, 1995 - v1
Checksum:i548C17B0AE9EBFD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15430 mRNA. Translation: AAC38001.1.
PIRiI51560.
RefSeqiNP_001079344.1. NM_001085875.2.
UniGeneiXl.303.

Genome annotation databases

GeneIDi378688.
KEGGixla:378688.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15430 mRNA. Translation: AAC38001.1.
PIRiI51560.
RefSeqiNP_001079344.1. NM_001085875.2.
UniGeneiXl.303.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YVPX-ray2.20A/B1-538[»]
1YVRX-ray1.95A1-538[»]
2I91X-ray2.65A/B1-538[»]
ProteinModelPortaliP42700.
SMRiP42700.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP42700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi378688.
KEGGixla:378688.

Organism-specific databases

CTDi6738.
XenbaseiXB-GENE-968761. trove2.

Phylogenomic databases

HOVERGENiHBG013234.
KOiK11089.

Miscellaneous databases

EvolutionaryTraceiP42700.

Family and domain databases

InterProiIPR008858. TROVE_dom.
IPR002035. VWF_A.
[Graphical view]
PfamiPF05731. TROVE. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50988. TROVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRO60_XENLA
AccessioniPrimary (citable) accession number: P42700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.