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P28720

- TGT_ZYMMO

UniProt

P28720 - TGT_ZYMMO

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Protein

Queuine tRNA-ribosyltransferase

Gene

tgt

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).

Catalytic activityi

Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine.
Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.

Cofactori

Binds 1 zinc ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei102 – 1021Nucleophile
Binding sitei103 – 1031Substrate
Metal bindingi318 – 3181Zinc
Metal bindingi320 – 3201Zinc
Metal bindingi323 – 3231Zinc
Metal bindingi349 – 3491Zinc

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. queuine tRNA-ribosyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. queuosine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Queuosine biosynthesis, tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00392.

Names & Taxonomyi

Protein namesi
Recommended name:
Queuine tRNA-ribosyltransferase (EC:2.4.2.29)
Alternative name(s):
Guanine insertion enzyme
tRNA-guanine transglycosylase
Gene namesi
Name:tgt
Ordered Locus Names:ZMO0363
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
ProteomesiUP000001173: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031S → A: Strongly reduces activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 386385Queuine tRNA-ribosyltransferasePRO_0000135563Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi264203.ZMO0363.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 228
Beta strandi25 – 328
Beta strandi35 – 439
Beta strandi45 – 506
Helixi56 – 616
Beta strandi67 – 704
Helixi71 – 766
Turni77 – 793
Helixi80 – 856
Helixi89 – 935
Beta strandi99 – 1024
Helixi105 – 1084
Turni109 – 1113
Helixi112 – 1143
Beta strandi116 – 1183
Beta strandi122 – 1254
Turni127 – 1293
Beta strandi132 – 1354
Helixi137 – 14711
Beta strandi150 – 1534
Helixi165 – 18723
Helixi190 – 1956
Beta strandi197 – 2026
Helixi208 – 22114
Beta strandi224 – 2285
Beta strandi232 – 2354
Helixi237 – 24711
Helixi248 – 2503
Beta strandi253 – 2553
Beta strandi257 – 2593
Helixi265 – 2739
Beta strandi278 – 2803
Helixi283 – 2897
Beta strandi290 – 2934
Beta strandi298 – 3014
Helixi305 – 3073
Beta strandi314 – 3174
Helixi321 – 3255
Helixi328 – 3369
Helixi340 – 36627
Helixi370 – 38112

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFZX-ray2.00A1-386[»]
1ENUX-ray1.95A1-386[»]
1F3EX-ray1.85A1-386[»]
1K4GX-ray1.70A1-386[»]
1K4HX-ray1.80A1-386[»]
1N2VX-ray2.10A1-386[»]
1OZMX-ray1.95A2-386[»]
1OZQX-ray1.90A2-386[»]
1P0BX-ray1.70A2-386[»]
1P0DX-ray1.90A2-386[»]
1P0EX-ray2.40A2-386[»]
1PUDX-ray1.85A1-386[»]
1PXGX-ray1.70A2-383[»]
1Q2RX-ray2.90A/B/C/D1-386[»]
1Q2SX-ray3.20A/B/C/D1-386[»]
1Q4WX-ray1.93A1-386[»]
1Q63X-ray1.85A1-386[»]
1Q65X-ray2.10A1-386[»]
1Q66X-ray1.75A1-386[»]
1R5YX-ray1.20A1-386[»]
1S38X-ray1.81A1-386[»]
1S39X-ray1.95A1-386[»]
1WKDX-ray2.60A1-386[»]
1WKEX-ray2.20A1-386[»]
1WKFX-ray2.20A1-386[»]
1Y5VX-ray1.58A2-386[»]
1Y5WX-ray1.58A2-386[»]
1Y5XX-ray2.10A/D2-386[»]
2BBFX-ray1.70A1-386[»]
2NQZX-ray1.46A2-386[»]
2NSOX-ray1.60A1-386[»]
2OKOX-ray1.50A2-386[»]
2POTX-ray1.80A1-386[»]
2PWUX-ray1.77A1-386[»]
2PWVX-ray1.70A1-386[»]
2QIIX-ray1.70A1-386[»]
2QZRX-ray1.95A2-386[»]
2Z1VX-ray1.55A1-386[»]
2Z1WX-ray1.63A1-386[»]
2Z1XX-ray1.63A1-386[»]
2Z7KX-ray1.28A1-386[»]
3BL3X-ray2.25A1-386[»]
3BLDX-ray1.19A1-386[»]
3BLLX-ray1.26A1-386[»]
3BLOX-ray1.60A1-386[»]
3C2YX-ray1.78A1-386[»]
3EOSX-ray1.78A1-386[»]
3EOUX-ray1.93A1-386[»]
3GC4X-ray1.80A1-386[»]
3GC5X-ray1.40A1-386[»]
3GE7X-ray1.50A1-386[»]
3HFYX-ray2.00A1-386[»]
3RR4X-ray1.68A1-386[»]
3S1GX-ray1.82A1-386[»]
3SM0X-ray1.57A1-386[»]
3TLLX-ray1.37A1-386[»]
3UNTX-ray1.80A1-386[»]
3UVIX-ray1.55A1-386[»]
4DXXX-ray1.66A1-386[»]
4DY1X-ray2.04A1-386[»]
4E2VX-ray1.18A1-386[»]
4FPSX-ray1.45A1-386[»]
4FR1X-ray1.74A1-386[»]
4FR6X-ray1.59A1-386[»]
4FSAX-ray1.62A1-386[»]
4GCXX-ray1.42A1-386[»]
4GD0X-ray1.29A1-386[»]
4GG9X-ray1.48A1-386[»]
4GH1X-ray1.45A1-386[»]
4GH3X-ray2.06A1-386[»]
4GHRX-ray2.00A1-386[»]
4GI4X-ray1.97A1-386[»]
4GIYX-ray1.75A1-386[»]
4GKTX-ray1.53A1-386[»]
4H6EX-ray1.42A1-386[»]
4H7ZX-ray1.68A1-386[»]
4HQVX-ray1.66A2-386[»]
4HSHX-ray1.56A2-386[»]
4HTBX-ray1.90A1-386[»]
4HVXX-ray1.82A1-386[»]
4IPPX-ray1.33A1-386[»]
4JBRX-ray2.92A1-386[»]
4PUJX-ray1.42A1-386[»]
4PUKX-ray1.49A1-386[»]
4PULX-ray1.65A1-386[»]
4PUMX-ray1.93A1-386[»]
4PUNX-ray1.25A1-386[»]
4Q4OX-ray1.35A1-386[»]
4Q4PX-ray1.54A1-386[»]
4Q4QX-ray1.41A1-386[»]
4Q4RX-ray1.45A1-386[»]
4Q4SX-ray1.25A1-386[»]
ProteinModelPortaliP28720.
SMRiP28720. Positions 11-386.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28720.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0343.
HOGENOMiHOG000223473.
KOiK00773.

Family and domain databases

Gene3Di3.20.20.105. 1 hit.
HAMAPiMF_00168. Q_tRNA_Tgt.
InterProiIPR004803. Queuine_tRNA-ribosylTrfase.
IPR002616. tRNA_ribo_trans-like.
[Graphical view]
PANTHERiPTHR11962. PTHR11962. 1 hit.
PfamiPF01702. TGT. 1 hit.
[Graphical view]
SUPFAMiSSF51713. SSF51713. 1 hit.
TIGRFAMsiTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28720-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVEATAQETD RPRFSFSIAA REGKARTGTI EMKRGVIRTP AFMPVGTAAT
60 70 80 90 100
VKALKPETVR ATGADIILGN TYHLMLRPGA ERIAKLGGLH SFMGWDRPIL
110 120 130 140 150
TDSGGYQVMS LSSLTKQSEE GVTFKSHLDG SRHMLSPERS IEIQHLLGSD
160 170 180 190 200
IVMAFDECTP YPATPSRAAS SMERSMRWAK RSRDAFDSRK EQAENAALFG
210 220 230 240 250
IQQGSVFENL RQQSADALAE IGFDGYAVGG LAVGEGQDEM FRVLDFSVPM
260 270 280 290 300
LPDDKPHYLM GVGKPDDIVG AVERGIDMFD CVLPTRSGRN GQAFTWDGPI
310 320 330 340 350
NIRNARFSED LTPLDSECHC AVCQKWSRAY IHHLIRAGEI LGAMLMTEHN
360 370 380
IAFYQQLMQK IRDSISEGRF SQFAQDFRAR YFARNS
Length:386
Mass (Da):42,843
Last modified:January 23, 2007 - v4
Checksum:i26754E08600BD941
GO

Sequence cautioni

The sequence Z11910 differs from that shown. Reason: Frameshift at several positions.
The sequence AAA27704.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAA27705.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAG29862.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti312 – 3121T → K(PubMed:7665516)Curated
Sequence conflicti312 – 3121T → K1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L33777 Genomic DNA. Translation: AAA27704.1. Different initiation.
L33777 Genomic DNA. Translation: AAA27705.1. Different initiation.
AF313764 Genomic DNA. Translation: AAG29862.1. Different initiation.
AE008692 Genomic DNA. Translation: AAV88987.2.
Z11910 Genomic DNA. No translation available.
PIRiT46898.
RefSeqiYP_162098.2. NC_006526.2.

Genome annotation databases

EnsemblBacteriaiAAV88987; AAV88987; ZMO0363.
GeneIDi3188564.
KEGGizmo:ZMO0363.
PATRICi32566062. VBIZymMob102260_0345.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L33777 Genomic DNA. Translation: AAA27704.1 . Different initiation.
L33777 Genomic DNA. Translation: AAA27705.1 . Different initiation.
AF313764 Genomic DNA. Translation: AAG29862.1 . Different initiation.
AE008692 Genomic DNA. Translation: AAV88987.2 .
Z11910 Genomic DNA. No translation available.
PIRi T46898.
RefSeqi YP_162098.2. NC_006526.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EFZ X-ray 2.00 A 1-386 [» ]
1ENU X-ray 1.95 A 1-386 [» ]
1F3E X-ray 1.85 A 1-386 [» ]
1K4G X-ray 1.70 A 1-386 [» ]
1K4H X-ray 1.80 A 1-386 [» ]
1N2V X-ray 2.10 A 1-386 [» ]
1OZM X-ray 1.95 A 2-386 [» ]
1OZQ X-ray 1.90 A 2-386 [» ]
1P0B X-ray 1.70 A 2-386 [» ]
1P0D X-ray 1.90 A 2-386 [» ]
1P0E X-ray 2.40 A 2-386 [» ]
1PUD X-ray 1.85 A 1-386 [» ]
1PXG X-ray 1.70 A 2-383 [» ]
1Q2R X-ray 2.90 A/B/C/D 1-386 [» ]
1Q2S X-ray 3.20 A/B/C/D 1-386 [» ]
1Q4W X-ray 1.93 A 1-386 [» ]
1Q63 X-ray 1.85 A 1-386 [» ]
1Q65 X-ray 2.10 A 1-386 [» ]
1Q66 X-ray 1.75 A 1-386 [» ]
1R5Y X-ray 1.20 A 1-386 [» ]
1S38 X-ray 1.81 A 1-386 [» ]
1S39 X-ray 1.95 A 1-386 [» ]
1WKD X-ray 2.60 A 1-386 [» ]
1WKE X-ray 2.20 A 1-386 [» ]
1WKF X-ray 2.20 A 1-386 [» ]
1Y5V X-ray 1.58 A 2-386 [» ]
1Y5W X-ray 1.58 A 2-386 [» ]
1Y5X X-ray 2.10 A/D 2-386 [» ]
2BBF X-ray 1.70 A 1-386 [» ]
2NQZ X-ray 1.46 A 2-386 [» ]
2NSO X-ray 1.60 A 1-386 [» ]
2OKO X-ray 1.50 A 2-386 [» ]
2POT X-ray 1.80 A 1-386 [» ]
2PWU X-ray 1.77 A 1-386 [» ]
2PWV X-ray 1.70 A 1-386 [» ]
2QII X-ray 1.70 A 1-386 [» ]
2QZR X-ray 1.95 A 2-386 [» ]
2Z1V X-ray 1.55 A 1-386 [» ]
2Z1W X-ray 1.63 A 1-386 [» ]
2Z1X X-ray 1.63 A 1-386 [» ]
2Z7K X-ray 1.28 A 1-386 [» ]
3BL3 X-ray 2.25 A 1-386 [» ]
3BLD X-ray 1.19 A 1-386 [» ]
3BLL X-ray 1.26 A 1-386 [» ]
3BLO X-ray 1.60 A 1-386 [» ]
3C2Y X-ray 1.78 A 1-386 [» ]
3EOS X-ray 1.78 A 1-386 [» ]
3EOU X-ray 1.93 A 1-386 [» ]
3GC4 X-ray 1.80 A 1-386 [» ]
3GC5 X-ray 1.40 A 1-386 [» ]
3GE7 X-ray 1.50 A 1-386 [» ]
3HFY X-ray 2.00 A 1-386 [» ]
3RR4 X-ray 1.68 A 1-386 [» ]
3S1G X-ray 1.82 A 1-386 [» ]
3SM0 X-ray 1.57 A 1-386 [» ]
3TLL X-ray 1.37 A 1-386 [» ]
3UNT X-ray 1.80 A 1-386 [» ]
3UVI X-ray 1.55 A 1-386 [» ]
4DXX X-ray 1.66 A 1-386 [» ]
4DY1 X-ray 2.04 A 1-386 [» ]
4E2V X-ray 1.18 A 1-386 [» ]
4FPS X-ray 1.45 A 1-386 [» ]
4FR1 X-ray 1.74 A 1-386 [» ]
4FR6 X-ray 1.59 A 1-386 [» ]
4FSA X-ray 1.62 A 1-386 [» ]
4GCX X-ray 1.42 A 1-386 [» ]
4GD0 X-ray 1.29 A 1-386 [» ]
4GG9 X-ray 1.48 A 1-386 [» ]
4GH1 X-ray 1.45 A 1-386 [» ]
4GH3 X-ray 2.06 A 1-386 [» ]
4GHR X-ray 2.00 A 1-386 [» ]
4GI4 X-ray 1.97 A 1-386 [» ]
4GIY X-ray 1.75 A 1-386 [» ]
4GKT X-ray 1.53 A 1-386 [» ]
4H6E X-ray 1.42 A 1-386 [» ]
4H7Z X-ray 1.68 A 1-386 [» ]
4HQV X-ray 1.66 A 2-386 [» ]
4HSH X-ray 1.56 A 2-386 [» ]
4HTB X-ray 1.90 A 1-386 [» ]
4HVX X-ray 1.82 A 1-386 [» ]
4IPP X-ray 1.33 A 1-386 [» ]
4JBR X-ray 2.92 A 1-386 [» ]
4PUJ X-ray 1.42 A 1-386 [» ]
4PUK X-ray 1.49 A 1-386 [» ]
4PUL X-ray 1.65 A 1-386 [» ]
4PUM X-ray 1.93 A 1-386 [» ]
4PUN X-ray 1.25 A 1-386 [» ]
4Q4O X-ray 1.35 A 1-386 [» ]
4Q4P X-ray 1.54 A 1-386 [» ]
4Q4Q X-ray 1.41 A 1-386 [» ]
4Q4R X-ray 1.45 A 1-386 [» ]
4Q4S X-ray 1.25 A 1-386 [» ]
ProteinModelPortali P28720.
SMRi P28720. Positions 11-386.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264203.ZMO0363.

Chemistry

BindingDBi P28720.
ChEMBLi CHEMBL2987.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV88987 ; AAV88987 ; ZMO0363 .
GeneIDi 3188564.
KEGGi zmo:ZMO0363.
PATRICi 32566062. VBIZymMob102260_0345.

Phylogenomic databases

eggNOGi COG0343.
HOGENOMi HOG000223473.
KOi K00773.

Enzyme and pathway databases

UniPathwayi UPA00392 .

Miscellaneous databases

EvolutionaryTracei P28720.

Family and domain databases

Gene3Di 3.20.20.105. 1 hit.
HAMAPi MF_00168. Q_tRNA_Tgt.
InterProi IPR004803. Queuine_tRNA-ribosylTrfase.
IPR002616. tRNA_ribo_trans-like.
[Graphical view ]
PANTHERi PTHR11962. PTHR11962. 1 hit.
Pfami PF01702. TGT. 1 hit.
[Graphical view ]
SUPFAMi SSF51713. SSF51713. 1 hit.
TIGRFAMsi TIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis and overexpression of the Zymomonas mobilis tgt gene encoding tRNA-guanine transglycosylase: purification and biochemical characterization of the enzyme."
    Reuter K.K.H., Ficner R.
    J. Bacteriol. 177:5284-5288(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, CHARACTERIZATION.
  2. "Sequence analysis of 44B6 fosmid clone of Zymomonas mobilis ZM4."
    Ahn J.Y., Kang H.S.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 31821 / ZM4 / CP4.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31821 / ZM4 / CP4.
  4. "Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis."
    Shark K.B., Conway T.
    FEMS Microbiol. Lett. 75:19-26(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 31821 / ZM4 / CP4.
  5. "Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange."
    Romier C., Reuter K., Suck D., Ficner R.
    EMBO J. 15:2850-2857(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
  6. "Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity."
    Graedler U., Ficner R., Garcia G.A., Stubbs M.T., Klebe G., Reuter K.
    FEBS Lett. 454:142-146(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-382, MUTAGENESIS OF SER-103.
  7. "A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase."
    Graedler U., Gerber H.-D., Goodenough-Lashua D.M., Garcia G.A., Ficner R., Reuter K., Stubbs M.T., Klebe G.
    J. Mol. Biol. 306:455-467(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
  8. "De novo design, synthesis, and in vitro evaluation of inhibitors for prokaryotic tRNA-guanine transglycosylase: a dramatic sulfur effect on binding affinity."
    Meyer E.A., Brenk R., Castellano R.K., Furler M., Klebe G., Diederich F.
    ChemBioChem 3:250-253(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-386.
  9. "Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on a new unexpected binding mode detected by crystal structure analysis."
    Brenk R., Naerum L., Graedler U., Gerber H.-D., Garcia G.A., Reuter K., Stubbs M.T., Klebe G.
    J. Med. Chem. 46:1133-1143(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-386.

Entry informationi

Entry nameiTGT_ZYMMO
AccessioniPrimary (citable) accession number: P28720
Secondary accession number(s): Q5NQL7, Q60247, Q9F5L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3