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Q9BW92

- SYTM_HUMAN

UniProt

Q9BW92 - SYTM_HUMAN

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Protein

Threonine--tRNA ligase, mitochondrial

Gene

TARS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. threonine-tRNA ligase activity Source: UniProtKB-EC

GO - Biological processi

  1. gene expression Source: Reactome
  2. mitochondrial threonyl-tRNA aminoacylation Source: BHF-UCL
  3. tRNA aminoacylation for protein translation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine--tRNA ligase, mitochondrial (EC:6.1.1.3)
Alternative name(s):
Threonyl-tRNA synthetase
Short name:
ThrRS
Threonyl-tRNA synthetase-like 1
Gene namesi
Name:TARS2
Synonyms:TARSL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:30740. TARS2.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Combined oxidative phosphorylation deficiency 21 (COXPD21) [MIM:615918]: A mitochondrial disorder characterized by a lethal encephalomyopathy. Shortly after birth, affected individuals manifest axial hypotonia, limb hypertonia, psychomotor delay, and increased serum lactate. Additional features include subsarcolemmal lipofuscin-positive deposits in muscle, cerebral spongiosis, and hepatic steatosis.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti282 – 2821P → L in COXPD21; shows decreased mRNA and protein compared to controls. 1 Publication
VAR_071853

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615918. phenotype.
PharmGKBiPA162405200.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 718Threonine--tRNA ligase, mitochondrialPRO_0000254586
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BW92.
PaxDbiQ9BW92.
PRIDEiQ9BW92.

PTM databases

PhosphoSiteiQ9BW92.

Expressioni

Gene expression databases

BgeeiQ9BW92.
CleanExiHS_TARS2.
ExpressionAtlasiQ9BW92. baseline and differential.
GenevestigatoriQ9BW92.

Organism-specific databases

HPAiHPA028626.

Interactioni

Protein-protein interaction databases

BioGridi123188. 10 interactions.
IntActiQ9BW92. 6 interactions.
MINTiMINT-8052579.
STRINGi9606.ENSP00000358060.

Structurei

3D structure databases

ProteinModelPortaliQ9BW92.
SMRiQ9BW92. Positions 59-716.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0441.
GeneTreeiENSGT00390000002149.
HOGENOMiHOG000003878.
HOVERGENiHBG059513.
InParanoidiQ9BW92.
KOiK01868.
OMAiTVYGCGM.
PhylomeDBiQ9BW92.
TreeFamiTF300858.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth.
InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR01047. TRNASYNTHTHR.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00418. thrS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BW92-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALYQRWRCL RLQGLQACRL HTAVVSTPPR WLAERLGLFE ELWAAQVKRL
60 70 80 90 100
ASMAQKEPRT IKISLPGGQK IDAVAWNTTP YQLARQISST LADTAVAAQV
110 120 130 140 150
NGEPYDLERP LETDSDLRFL TFDSPEGKAV FWHSSTHVLG AAAEQFLGAV
160 170 180 190 200
LCRGPSTEYG FYHDFFLGKE RTIRGSELPV LERICQELTA AARPFRRLEA
210 220 230 240 250
SRDQLRQLFK DNPFKLHLIE EKVTGPTATV YGCGTLVDLC QGPHLRHTGQ
260 270 280 290 300
IGGLKLLSNS SSLWRSSGAP ETLQRVSGIS FPTTELLRVW EAWREEAELR
310 320 330 340 350
DHRRIGKEQE LFFFHELSPG SCFFLPRGTR VYNALVAFIR AEYAHRGFSE
360 370 380 390 400
VKTPTLFSTK LWEQSGHWEH YQEDMFAVQP PGSDRPPSSQ SDDSTRHITD
410 420 430 440 450
TLALKPMNCP AHCLMFAHRP RSWRELPLRL ADFGALHRAE ASGGLGGLTR
460 470 480 490 500
LRCFQQDDAH IFCTTDQLEA EIQSCLDFLR SVYAVLGFSF RLALSTRPSG
510 520 530 540 550
FLGDPCLWDQ AEQVLKQALK EFGEPWDLNS GDGAFYGPKI DVHLHDALGR
560 570 580 590 600
PHQCGTIQLD FQLPLRFDLQ YKGQAGALER PVLIHRAVLG SVERLLGVLA
610 620 630 640 650
ESCGGKWPLW LSPFQVVVIP VGSEQEEYAK EAQQSLRAAG LVSDLDADSG
660 670 680 690 700
LTLSRRIRRA QLAHYNFQFV VGQKEQSKRT VNIRTRDNRR LGEWDLPEAV
710
QRLVELQNTR VPNAEEIF
Length:718
Mass (Da):81,036
Last modified:June 1, 2001 - v1
Checksum:iA2F793A60483E7F9
GO
Isoform 2 (identifier: Q9BW92-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     211-340: Missing.

Note: No experimental confirmation available.

Show »
Length:588
Mass (Da):66,372
Checksum:i19A2BD2A6BB8C400
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691A → P in BAD96534. 1 PublicationCurated
Sequence conflicti579 – 5791E → G in BAD96534. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti282 – 2821P → L in COXPD21; shows decreased mRNA and protein compared to controls. 1 Publication
VAR_071853

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei211 – 340130Missing in isoform 2. 1 PublicationVSP_054537Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022590 mRNA. Translation: BAB14117.1.
AK222814 mRNA. Translation: BAD96534.1.
AL356356 Genomic DNA. Translation: CAI15488.1.
CH471121 Genomic DNA. Translation: EAW53549.1.
BC000541 mRNA. Translation: AAH00541.1.
BC007824 mRNA. Translation: AAH07824.2.
BC009997 mRNA. Translation: AAH09997.1.
CCDSiCCDS60252.1. [Q9BW92-2]
CCDS952.1. [Q9BW92-1]
RefSeqiNP_001258825.1. NM_001271896.1. [Q9BW92-2]
NP_079426.2. NM_025150.4. [Q9BW92-1]
UniGeneiHs.288974.

Genome annotation databases

EnsembliENST00000369054; ENSP00000358050; ENSG00000143374. [Q9BW92-2]
ENST00000369064; ENSP00000358060; ENSG00000143374. [Q9BW92-1]
GeneIDi80222.
KEGGihsa:80222.
UCSCiuc001euq.4. human. [Q9BW92-1]
uc009wls.4. human.

Polymorphism databases

DMDMi74752395.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022590 mRNA. Translation: BAB14117.1 .
AK222814 mRNA. Translation: BAD96534.1 .
AL356356 Genomic DNA. Translation: CAI15488.1 .
CH471121 Genomic DNA. Translation: EAW53549.1 .
BC000541 mRNA. Translation: AAH00541.1 .
BC007824 mRNA. Translation: AAH07824.2 .
BC009997 mRNA. Translation: AAH09997.1 .
CCDSi CCDS60252.1. [Q9BW92-2 ]
CCDS952.1. [Q9BW92-1 ]
RefSeqi NP_001258825.1. NM_001271896.1. [Q9BW92-2 ]
NP_079426.2. NM_025150.4. [Q9BW92-1 ]
UniGenei Hs.288974.

3D structure databases

ProteinModelPortali Q9BW92.
SMRi Q9BW92. Positions 59-716.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123188. 10 interactions.
IntActi Q9BW92. 6 interactions.
MINTi MINT-8052579.
STRINGi 9606.ENSP00000358060.

Chemistry

DrugBanki DB00156. L-Threonine.

PTM databases

PhosphoSitei Q9BW92.

Polymorphism databases

DMDMi 74752395.

Proteomic databases

MaxQBi Q9BW92.
PaxDbi Q9BW92.
PRIDEi Q9BW92.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369054 ; ENSP00000358050 ; ENSG00000143374 . [Q9BW92-2 ]
ENST00000369064 ; ENSP00000358060 ; ENSG00000143374 . [Q9BW92-1 ]
GeneIDi 80222.
KEGGi hsa:80222.
UCSCi uc001euq.4. human. [Q9BW92-1 ]
uc009wls.4. human.

Organism-specific databases

CTDi 80222.
GeneCardsi GC01P150459.
HGNCi HGNC:30740. TARS2.
HPAi HPA028626.
MIMi 612805. gene.
615918. phenotype.
neXtProti NX_Q9BW92.
PharmGKBi PA162405200.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0441.
GeneTreei ENSGT00390000002149.
HOGENOMi HOG000003878.
HOVERGENi HBG059513.
InParanoidi Q9BW92.
KOi K01868.
OMAi TVYGCGM.
PhylomeDBi Q9BW92.
TreeFami TF300858.

Enzyme and pathway databases

Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi TARS2. human.
GenomeRNAii 80222.
NextBioi 70637.
PROi Q9BW92.
SOURCEi Search...

Gene expression databases

Bgeei Q9BW92.
CleanExi HS_TARS2.
ExpressionAtlasi Q9BW92. baseline and differential.
Genevestigatori Q9BW92.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPi MF_00184. Thr_tRNA_synth.
InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view ]
Pfami PF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view ]
PRINTSi PR01047. TRNASYNTHTHR.
SMARTi SM00863. tRNA_SAD. 1 hit.
[Graphical view ]
SUPFAMi SSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsi TIGR00418. thrS. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Lung.
  6. "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS."
    Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C., Sissler M.
    Biochemistry 44:4805-4816(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: INVOLVEMENT IN COXPD21, VARIANT COXPD21 LEU-282, CHARACTERIZATION OF VARIANT COXPD21.

Entry informationi

Entry nameiSYTM_HUMAN
AccessioniPrimary (citable) accession number: Q9BW92
Secondary accession number(s): Q53GW7, Q96I50, Q9H9V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3