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Protein

Ribonuclease H1

Gene

RNASEH1

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

Functioni

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (PubMed:10497183). Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II (PubMed:21700224).2 Publications

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.PROSITE-ProRule annotation

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.

Enzyme regulationi

In the presence of magnesium, manganese is inhibitory.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi145 – 1451Magnesium 1PROSITE-ProRule annotation
Metal bindingi145 – 1451Magnesium 2PROSITE-ProRule annotation
Metal bindingi186 – 1861Magnesium 1PROSITE-ProRule annotation
Metal bindingi210 – 2101Magnesium 1PROSITE-ProRule annotation
Metal bindingi274 – 2741Magnesium 2PROSITE-ProRule annotation

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • nucleic acid binding Source: ProtInc
  • ribonuclease activity Source: ProtInc
  • RNA binding Source: ProtInc
  • RNA-DNA hybrid ribonuclease activity Source: UniProtKB

GO - Biological processi

  • DNA replication, removal of RNA primer Source: GO_Central
  • RNA catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease H1 (EC:3.1.26.4)
Short name:
RNase H1
Alternative name(s):
Ribonuclease H type II
Gene namesi
Name:RNASEH1
Synonyms:RNH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:18466. RNASEH1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal recessive 2 (PEOB2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of progressive external ophthalmoplegia, a mitochondrial myopathy characterized by progressive paralysis of the levator palpebrae, orbicularis oculi, and extraocular muscles. PEOB2 patients manifest exercise intolerance, muscle weakness, and signs and symptoms of spinocerebellar ataxia, such as impaired gait and dysarthria. Some patients may have respiratory insufficiency.
See also OMIM:616479
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti142 – 1421V → I in PEOB2; has partial residual endonuclase activity. 1 Publication
Corresponds to variant rs766294940 [ dbSNP | Ensembl ].
VAR_074561
Natural varianti185 – 1851A → V in PEOB2; has partial residual endonuclase activity. 1 Publication
VAR_074562

Keywords - Diseasei

Disease mutation, Progressive external ophthalmoplegia

Organism-specific databases

MIMi616479. phenotype.
PharmGKBiPA38543.

Chemistry

ChEMBLiCHEMBL5893.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286Ribonuclease H1PRO_0000195433Add
BLAST

Proteomic databases

EPDiO60930.
MaxQBiO60930.
PaxDbiO60930.
PeptideAtlasiO60930.
PRIDEiO60930.

PTM databases

iPTMnetiO60930.
PhosphoSiteiO60930.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO60930.
CleanExiHS_RNASEH1.
HS_RNH1.
ExpressionAtlasiO60930. baseline and differential.
GenevisibleiO60930. HS.

Organism-specific databases

HPAiHPA043037.

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

BioGridi128882. 8 interactions.
IntActiO60930. 4 interactions.
STRINGi9606.ENSP00000313350.

Chemistry

BindingDBiO60930.

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 369Combined sources
Beta strandi38 – 425Combined sources
Helixi43 – 508Combined sources
Beta strandi57 – 637Combined sources
Helixi64 – 729Combined sources
Beta strandi139 – 14911Combined sources
Turni150 – 1523Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi157 – 1637Combined sources
Beta strandi172 – 1754Combined sources
Helixi182 – 19918Combined sources
Beta strandi204 – 2107Combined sources
Helixi212 – 2198Combined sources
Helixi221 – 2266Combined sources
Turni227 – 2293Combined sources
Beta strandi235 – 2373Combined sources
Helixi241 – 25111Combined sources
Beta strandi255 – 2606Combined sources
Beta strandi263 – 2653Combined sources
Helixi268 – 28114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QK9X-ray2.55A136-286[»]
2QKBX-ray2.40A/B136-286[»]
2QKKX-ray3.20A/B/E/F/I/J/M/N/R/S/W136-286[»]
3BSUX-ray2.10A/B/C/F/G/H27-76[»]
ProteinModelPortaliO60930.
SMRiO60930. Positions 27-74, 136-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60930.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini136 – 282147RNase HPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RNase H family.Curated
Contains 1 RNase H domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3752. Eukaryota.
COG0328. LUCA.
GeneTreeiENSGT00390000003466.
HOGENOMiHOG000040465.
HOVERGENiHBG002135.
InParanoidiO60930.
KOiK03469.
OMAiECKSQVD.
PhylomeDBiO60930.
TreeFamiTF313356.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.40.970.10. 1 hit.
InterProiIPR009027. Ribosomal_L9/RNase_H1_N.
IPR017067. RNase_H1_euk.
IPR011320. RNase_H1_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamiPF01693. Cauli_VI. 1 hit.
PF00075. RNase_H. 1 hit.
[Graphical view]
PIRSFiPIRSF036852. Ribonuclease_H1_euk. 1 hit.
SUPFAMiSSF53098. SSF53098. 1 hit.
SSF55658. SSF55658. 1 hit.
PROSITEiPS50879. RNASE_H. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWLLFLAHR VALAALPCRR GSRGFGMFYA VRRGRKTGVF LTWNECRAQV
60 70 80 90 100
DRFPAARFKK FATEDEAWAF VRKSASPEVS EGHENQHGQE SEAKASKRLR
110 120 130 140 150
EPLDGDGHES AEPYAKHMKP SVEPAPPVSR DTFSYMGDFV VVYTDGCCSS
160 170 180 190 200
NGRRRPRAGI GVYWGPGHPL NVGIRLPGRQ TNQRAEIHAA CKAIEQAKTQ
210 220 230 240 250
NINKLVLYTD SMFTINGITN WVQGWKKNGW KTSAGKEVIN KEDFVALERL
260 270 280
TQGMDIQWMH VPGHSGFIGN EEADRLAREG AKQSED
Length:286
Mass (Da):32,064
Last modified:April 27, 2001 - v2
Checksum:i400FE04E7E85CA6A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241G → R in AAV38476 (Ref. 5) Curated
Sequence conflicti33 – 331R → K in CAG46619 (Ref. 4) Curated
Sequence conflicti68 – 681W → R in AAV38476 (Ref. 5) Curated
Sequence conflicti89 – 891Q → R in CAA11835 (PubMed:9894807).Curated
Sequence conflicti136 – 1361M → I in CAG46619 (Ref. 4) Curated
Sequence conflicti223 – 2231Q → R in CAA11835 (PubMed:9894807).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41L → F.2 Publications
Corresponds to variant rs1136545 [ dbSNP | Ensembl ].
VAR_023469
Natural varianti142 – 1421V → I in PEOB2; has partial residual endonuclase activity. 1 Publication
Corresponds to variant rs766294940 [ dbSNP | Ensembl ].
VAR_074561
Natural varianti185 – 1851A → V in PEOB2; has partial residual endonuclase activity. 1 Publication
VAR_074562

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF048995 mRNA. Translation: AAC78564.1.
AF048994 mRNA. Translation: AAC78563.1.
AF039652 mRNA. Translation: AAC09261.1.
AJ224117 mRNA. Translation: CAA11835.1.
CR541820 mRNA. Translation: CAG46619.1.
BT019670 mRNA. Translation: AAV38476.1.
AK075490 mRNA. Translation: BAG52156.1.
AC108488 Genomic DNA. Translation: AAX82026.1.
CH471053 Genomic DNA. Translation: EAX01061.1.
BC002973 mRNA. Translation: AAH02973.1.
CCDSiCCDS1647.1.
RefSeqiNP_001273763.1. NM_001286834.1.
NP_001273766.1. NM_001286837.1.
NP_002927.2. NM_002936.4.
UniGeneiHs.568006.

Genome annotation databases

EnsembliENST00000315212; ENSP00000313350; ENSG00000171865.
GeneIDi246243.
KEGGihsa:246243.
UCSCiuc002qxt.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

RNase H entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF048995 mRNA. Translation: AAC78564.1.
AF048994 mRNA. Translation: AAC78563.1.
AF039652 mRNA. Translation: AAC09261.1.
AJ224117 mRNA. Translation: CAA11835.1.
CR541820 mRNA. Translation: CAG46619.1.
BT019670 mRNA. Translation: AAV38476.1.
AK075490 mRNA. Translation: BAG52156.1.
AC108488 Genomic DNA. Translation: AAX82026.1.
CH471053 Genomic DNA. Translation: EAX01061.1.
BC002973 mRNA. Translation: AAH02973.1.
CCDSiCCDS1647.1.
RefSeqiNP_001273763.1. NM_001286834.1.
NP_001273766.1. NM_001286837.1.
NP_002927.2. NM_002936.4.
UniGeneiHs.568006.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QK9X-ray2.55A136-286[»]
2QKBX-ray2.40A/B136-286[»]
2QKKX-ray3.20A/B/E/F/I/J/M/N/R/S/W136-286[»]
3BSUX-ray2.10A/B/C/F/G/H27-76[»]
ProteinModelPortaliO60930.
SMRiO60930. Positions 27-74, 136-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128882. 8 interactions.
IntActiO60930. 4 interactions.
STRINGi9606.ENSP00000313350.

Chemistry

BindingDBiO60930.
ChEMBLiCHEMBL5893.

PTM databases

iPTMnetiO60930.
PhosphoSiteiO60930.

Proteomic databases

EPDiO60930.
MaxQBiO60930.
PaxDbiO60930.
PeptideAtlasiO60930.
PRIDEiO60930.

Protocols and materials databases

DNASUi246243.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315212; ENSP00000313350; ENSG00000171865.
GeneIDi246243.
KEGGihsa:246243.
UCSCiuc002qxt.5. human.

Organism-specific databases

CTDi246243.
GeneCardsiRNASEH1.
H-InvDBHIX0039191.
HGNCiHGNC:18466. RNASEH1.
HPAiHPA043037.
MIMi604123. gene.
616479. phenotype.
neXtProtiNX_O60930.
PharmGKBiPA38543.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3752. Eukaryota.
COG0328. LUCA.
GeneTreeiENSGT00390000003466.
HOGENOMiHOG000040465.
HOVERGENiHBG002135.
InParanoidiO60930.
KOiK03469.
OMAiECKSQVD.
PhylomeDBiO60930.
TreeFamiTF313356.

Miscellaneous databases

EvolutionaryTraceiO60930.
GeneWikiiRNASEH1.
GenomeRNAii246243.
PROiO60930.
SOURCEiSearch...

Gene expression databases

BgeeiO60930.
CleanExiHS_RNASEH1.
HS_RNH1.
ExpressionAtlasiO60930. baseline and differential.
GenevisibleiO60930. HS.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.40.970.10. 1 hit.
InterProiIPR009027. Ribosomal_L9/RNase_H1_N.
IPR017067. RNase_H1_euk.
IPR011320. RNase_H1_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamiPF01693. Cauli_VI. 1 hit.
PF00075. RNase_H. 1 hit.
[Graphical view]
PIRSFiPIRSF036852. Ribonuclease_H1_euk. 1 hit.
SUPFAMiSSF53098. SSF53098. 1 hit.
SSF55658. SSF55658. 1 hit.
PROSITEiPS50879. RNASE_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and mapping of ribonucleases H of human and mouse related to bacterial RNase HI."
    Cerritelli S.M., Crouch R.J.
    Genomics 53:300-307(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-4.
  2. "Molecular cloning and expression of cDNA for human RNase H."
    Wu H., Lima W.F., Crooke S.T.
    Antisense Nucleic Acid Drug Dev. 8:53-61(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning, subcellular localization and functional expression of human RNase HII."
    Frank P., Braunshofer-Reiter C., Poltl A., Holzmann K.
    Biol. Chem. 379:1407-1412(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-4.
  6. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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].
    Tissue: Lung.
  10. "Properties of cloned and expressed human RNase H1."
    Wu H., Lima W.F., Crooke S.T.
    J. Biol. Chem. 274:28270-28278(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  11. "Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination."
    Skourti-Stathaki K., Proudfoot N.J., Gromak N.
    Mol. Cell 42:794-805(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  14. "RNASEH1 mutations impair mtDNA replication and cause adult-onset mitochondrial encephalomyopathy."
    Reyes A., Melchionda L., Nasca A., Carrara F., Lamantea E., Zanolini A., Lamperti C., Fang M., Zhang J., Ronchi D., Bonato S., Fagiolari G., Moggio M., Ghezzi D., Zeviani M.
    Am. J. Hum. Genet. 97:186-193(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PEOB2, VARIANTS PEOB2 ILE-142 AND VAL-185, CHARACTERIZATION OF VARIANTS PEOB2 ILE-142 AND VAL-185.

Entry informationi

Entry nameiRNH1_HUMAN
AccessioniPrimary (citable) accession number: O60930
Secondary accession number(s): B3KQU4
, O60523, O60857, Q57Z93, Q5U0C1, Q6FHD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 6, 2016
This is version 155 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.