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Protein

Prolyl 3,4-dihydroxylase TPA1

Gene

TPA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Prolyl 3,4-dihydroxylase that catalyzes 3,4-dihydroxylation of 'Pro-64' of small ribosomal subunit RPS23 (RPS23A and RPS23B), thereby regulating protein translation termination efficiency. Part of a messenger ribonucleoprotein (mRNP) complex at the 3'-UTR of mRNAs. It associates specifically with components of the translation termination complex and is involved in both translation termination and in regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.3 Publications

Catalytic activityi

Peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl 3,4-hydroxy-L-proline + succinate + CO2.1 Publication

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi159IronPROSITE-ProRule annotation1 Publication1
Metal bindingi161IronPROSITE-ProRule annotation1 Publication1
Binding sitei1732-oxoglutaratePROSITE-ProRule annotation1 Publication1
Metal bindingi227IronPROSITE-ProRule annotation1 Publication1
Binding sitei2382-oxoglutaratePROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

  • ferrous iron binding Source: SGD
  • L-ascorbic acid binding Source: UniProtKB-KW
  • oxidative DNA demethylase activity Source: SGD
  • peptidyl-proline dioxygenase activity Source: UniProtKB
  • poly(A) binding Source: SGD

GO - Biological processi

  • DNA dealkylation involved in DNA repair Source: SGD
  • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: SGD
  • oxidative demethylation Source: SGD
  • peptidyl-proline di-hydroxylation Source: UniProtKB
  • regulation of translational termination Source: UniProtKB
  • translational termination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Enzyme and pathway databases

BioCyciYEAST:G3O-30228-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl 3,4-dihydroxylase TPA1 (EC:1.14.11.-)
Alternative name(s):
Termination and polyadenylation protein 1
Gene namesi
Name:TPA1
Ordered Locus Names:YER049W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER049W.
SGDiS000000851. TPA1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Decrease of translation termination efficacy and an increase in mRNAs half-lives and longer mRNA poly(A) tails.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi159 – 161HDD → ADN or ADA: Loss of function. 2 Publications3
Mutagenesisi159H → A: Loss of function. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002066701 – 644Prolyl 3,4-dihydroxylase TPA1Add BLAST644

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei607PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40032.
PRIDEiP40032.

PTM databases

iPTMnetiP40032.

Interactioni

Subunit structurei

Monomer and homodimer. Interacts with FRK1, eRF1 (SUP1), eRF3 (SUP35) and polyadenylate-binding protein PAB1. Interacts with ETT1.4 Publications

Protein-protein interaction databases

BioGridi36788. 57 interactors.
DIPiDIP-2878N.
IntActiP40032. 5 interactors.
MINTiMINT-516781.

Structurei

Secondary structure

1644
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 29Combined sources3
Helixi32 – 35Combined sources4
Helixi37 – 48Combined sources12
Beta strandi51 – 53Combined sources3
Beta strandi56 – 60Combined sources5
Helixi64 – 77Combined sources14
Beta strandi81 – 84Combined sources4
Beta strandi86 – 92Combined sources7
Helixi111 – 120Combined sources10
Helixi123 – 132Combined sources10
Beta strandi139 – 142Combined sources4
Beta strandi145 – 150Combined sources6
Beta strandi155 – 159Combined sources5
Beta strandi166 – 173Combined sources8
Helixi183 – 185Combined sources3
Beta strandi189 – 191Combined sources3
Beta strandi194 – 196Combined sources3
Beta strandi205 – 208Combined sources4
Beta strandi214 – 219Combined sources6
Turni222 – 224Combined sources3
Beta strandi227 – 229Combined sources3
Beta strandi238 – 246Combined sources9
Helixi252 – 254Combined sources3
Helixi259 – 268Combined sources10
Helixi269 – 277Combined sources9
Helixi278 – 282Combined sources5
Helixi294 – 304Combined sources11
Helixi332 – 339Combined sources8
Helixi344 – 346Combined sources3
Helixi349 – 362Combined sources14
Beta strandi363 – 369Combined sources7
Helixi373 – 389Combined sources17
Helixi396 – 398Combined sources3
Turni409 – 411Combined sources3
Beta strandi415 – 417Combined sources3
Beta strandi419 – 421Combined sources3
Helixi428 – 436Combined sources9
Helixi443 – 457Combined sources15
Turni461 – 463Combined sources3
Helixi466 – 479Combined sources14
Helixi481 – 491Combined sources11
Beta strandi492 – 495Combined sources4
Beta strandi497 – 505Combined sources9
Turni507 – 509Combined sources3
Helixi521 – 523Combined sources3
Beta strandi527 – 540Combined sources14
Turni546 – 550Combined sources5
Beta strandi555 – 558Combined sources4
Beta strandi588 – 592Combined sources5
Beta strandi596 – 604Combined sources9
Beta strandi609 – 612Combined sources4
Beta strandi623 – 634Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KT1X-ray2.50A21-644[»]
3KT4X-ray2.73A21-644[»]
3KT7X-ray1.77A21-644[»]
3MGUX-ray2.80A1-644[»]
4NHKX-ray1.90A21-644[»]
4NHLX-ray2.84A21-644[»]
4NHMX-ray1.90A21-644[»]
ProteinModelPortaliP40032.
SMRiP40032.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40032.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini141 – 247Fe2OG dioxygenasePROSITE-ProRule annotationAdd BLAST107

Sequence similaritiesi

Belongs to the TPA1 family.Curated
Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000002349.
HOGENOMiHOG000165892.
InParanoidiP40032.
OMAiAEGSRWD.
OrthoDBiEOG092C608K.

Family and domain databases

InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR019601. Oxoglutarate/Fe-dep_Oase_C.
IPR006620. Pro_4_hyd_alph.
[Graphical view]
PfamiPF10637. Ofd1_CTDD. 1 hit.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40032-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRKTAEVKG EKERNSKQIS LEEDKIKGMF NPKIWDKTFQ DGLKKEIEDS
60 70 80 90 100
QPYNWGTIHE LVNDDLLRAV RKEIETEIHF TKKETDIYRV NQSGDLANLS
110 120 130 140 150
GLDWDDLSRL PNLFKLRQIL YSKQYRDFFG YVTKAGKLSG SKTDMSINTY
160 170 180 190 200
TKGCHLLTHD DVIGSRRISF ILYLPDPDRK WKSHYGGGLR LFPSILPNVP
210 220 230 240 250
HSDPSAKLVP QFNQIAFFKV LPGFSFHDVE EVKVDKHRLS IQGWYHIPQV
260 270 280 290 300
GEEGYIPGEE EAWVRNNTST LAQIESNVLE DFEFPKDERN ILSFHEVKHF
310 320 330 340 350
EKMLKGDAGA KTDNTPKESM TSVISDSVKL SEAEFTYLSQ YISPEHLSSK
360 370 380 390 400
GIEKLQKQFV ENSSLQIESF LNDDKSELLK KVIKQKELEQ ECPYHSKDVK
410 420 430 440 450
APWKTAIPPH KARYLYIDGK EYRNFQTEAD ILEALNNNDL PNFQFTKDAI
460 470 480 490 500
KIISDASGNS RENNFDAELA LIDLAVFHKS TIFKKYLALL TSLCPVSEQI
510 520 530 540 550
LIRRFRPGMD FTLATKCRFN ELLKSNPDII DAVLEGTLCL TPSAGWESGE
560 570 580 590 600
LGGYELYMMD DDEDNKQYLK EDVEDASVYR ADDSGDSVLI NDPPAWNTFN
610 620 630 640
LVLRDESVLE FVKYVSWSAK SSRWDVKMKW DVKSCDEDGQ EDEA
Length:644
Mass (Da):74,041
Last modified:February 1, 1995 - v1
Checksum:i1273410E75479A46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18796 Genomic DNA. Translation: AAB64584.1.
BK006939 Genomic DNA. Translation: DAA07705.1.
PIRiS50552.
RefSeqiNP_010969.1. NM_001178940.1.

Genome annotation databases

EnsemblFungiiYER049W; YER049W; YER049W.
GeneIDi856775.
KEGGisce:YER049W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18796 Genomic DNA. Translation: AAB64584.1.
BK006939 Genomic DNA. Translation: DAA07705.1.
PIRiS50552.
RefSeqiNP_010969.1. NM_001178940.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KT1X-ray2.50A21-644[»]
3KT4X-ray2.73A21-644[»]
3KT7X-ray1.77A21-644[»]
3MGUX-ray2.80A1-644[»]
4NHKX-ray1.90A21-644[»]
4NHLX-ray2.84A21-644[»]
4NHMX-ray1.90A21-644[»]
ProteinModelPortaliP40032.
SMRiP40032.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36788. 57 interactors.
DIPiDIP-2878N.
IntActiP40032. 5 interactors.
MINTiMINT-516781.

PTM databases

iPTMnetiP40032.

Proteomic databases

MaxQBiP40032.
PRIDEiP40032.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER049W; YER049W; YER049W.
GeneIDi856775.
KEGGisce:YER049W.

Organism-specific databases

EuPathDBiFungiDB:YER049W.
SGDiS000000851. TPA1.

Phylogenomic databases

GeneTreeiENSGT00390000002349.
HOGENOMiHOG000165892.
InParanoidiP40032.
OMAiAEGSRWD.
OrthoDBiEOG092C608K.

Enzyme and pathway databases

BioCyciYEAST:G3O-30228-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40032.
PROiP40032.

Family and domain databases

InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR019601. Oxoglutarate/Fe-dep_Oase_C.
IPR006620. Pro_4_hyd_alph.
[Graphical view]
PfamiPF10637. Ofd1_CTDD. 1 hit.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTPA1_YEAST
AccessioniPrimary (citable) accession number: P40032
Secondary accession number(s): D3DLV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8910 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

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.