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Entry version 125 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
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Protein

CRISPR-associated endonuclease Cas1

Gene

ygbT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids) (PubMed:21255106, PubMed:24920831, PubMed:24793649). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The Cas1-Cas2 complex is involved in CRISPR adaptation, the first stage of CRISPR immunity, being required for the addition/removal of CRISPR spacers at the leader end of the CRISPR locus (PubMed:24920831, PubMed:25707795, PubMed:24793649). The Cas1-Cas2 complex introduces staggered nicks into both strands of the CRISPR array near the leader repeat and joins the 5'-ends of the repeat strands with the 3'-ends of the new spacer sequence (PubMed:24920831). Spacer DNA integration requires supercoiled target DNA and 3'-OH ends on the inserted (spacer) DNA and probably initiates with a nucleophilic attack of the C 3'-OH end of the protospacer on the minus strand of the first repeat sequence (PubMed:25707795). Expression of Cas1-Cas2 in a strain lacking both genes permits spacer acquisition (PubMed:24793649, PubMed:24920831). Non-specifically binds DNA; the Cas1-Cas2 complex preferentially binds CRISPR-locus DNA (PubMed:24793649). Highest binding is seen to a dual forked DNA complex with 3'-overhangs and a protospacer-adjacent motif-complement specifically positioned (PubMed:26478180). The protospacer DNA lies across a flat surface extending from 1 Cas1 dimer, across the Cas2 dimer and contacting the other Cas1 dimer; the 23 bp-long ds section of the DNA is bracketed by 1 Tyr-22 from each of the Cas1 dimers (PubMed:26478180, PubMed:26503043). Cas1 cuts within the 3'-overhang, to generate a 33-nucleotide DNA that is probably incorporated into the CRISPR leader by a cut-and-paste mechanism (PubMed:26478180). Cas1 alone endonucleolytically cleaves linear ssRNA, ssDNA and short (34 base) dsDNA as well as branched DNA substrates such as Holliday junctions, replication forks and 5'-flap DNA substrates (PubMed:21219465). In vitro catalyzes a concerted transesterification reaction on branched DNA, as would be expected during integration of protospacers into the CRISPR leader sequence; Cas2 is not required in vitro. This reaction requires a 3'-OH group at the branch point (PubMed:26284603). Genetic interactions suggest Cas1 interacts with components of the RecBC and RuvB DNA repair systems (PubMed:21219465).7 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+3 PublicationsNote: Protospacer integration in vitro also occurs with Mn2+ and also requires low concentrations of KCl (PubMed:25707795). The transesterification function works equally well with Mg2+, Mn2+ or Co2+ in vitro (PubMed:26284603).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Nuclease activity partially inhibited by CasE (PubMed:21219465).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1412 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi141MagnesiumBy similarity1
Active sitei2082 Publications1
Metal bindingi208MagnesiumBy similarity1
Active sitei2212 Publications1
Metal bindingi221MagnesiumBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Endonuclease, Hydrolase, Nuclease
Biological processAntiviral defense, DNA damage, DNA repair
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G7425-MONOMER
ECOL316407:JW2725-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
CRISPR-associated endonuclease Cas1 (EC:3.1.-.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ygbT
Synonyms:cas1
Ordered Locus Names:b2755, JW2725
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Not essential. Increased sensitivity to MMC and UV light; double ygbT-ruvA, ruvB or ruvC disruptions have no further phenotype suggesting Cas1 functions in the same DNA repair pathway (PubMed:21219465). Function in DNA repair also seems to require CRISPRs (PubMed:21219465). Cells elongate after 2 hours growth in MMC; they are even longer in double ygbT-ruvA, ruvB or ruvC disruptions, suggesting Cas1 may also function in chromosome segregation (PubMed:21219465). Loss of plasmid silencing (PubMed:21255106).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi22Y → A: Slightly decreased spacer acquisition in vivo. 2 Publications1
Mutagenesisi22Y → F: Nearly wild-type spacer acquisition in vivo. 1 Publication1
Mutagenesisi41R → E: Dramatically decreased spacer acquisition in vivo. 1 Publication1
Mutagenesisi59R → A: Loss of spacer acquisition in vivo, decreased protospacer binding. 1 Publication1
Mutagenesisi59R → D: Dramatically decreased spacer acquisition in vitro, 250-fold decreased affinity for protospacer DNA. 1 Publication1
Mutagenesisi66R → D: Dramatically decreased spacer acquisition in vitro, 250-fold decreased affinity for protospacer DNA. 1 Publication1
Mutagenesisi66R → E: Dramatically decreased spacer acquisition in vivo. 1 Publication1
Mutagenesisi84R → A: Decreased spacer acquisition in vivo. 1 Publication1
Mutagenesisi84R → E: Dramatically decreased spacer acquisition in vivo. 1 Publication1
Mutagenesisi141E → A: No cleavage of any substrates, no restoration of UV or mitomycin C (MMC) resistance (PubMed:21219465). Loss of spacer acquisition in vivo (PubMed:24793649). 2 Publications1
Mutagenesisi149Y → A: No effect on in vitro protospacer integration. 1 Publication1
Mutagenesisi165Y → A: No effect on in vitro protospacer integration (PubMed:25707795). Alone significantly decreased protospacer acquisition in vivo (PubMed:26478180). Loss of protospacer acquisition, decreased protospacer binding; in association with A-170, significantly decreased protospacer binding; in association with A-217 (PubMed:26478180). 2 Publications1
Mutagenesisi170W → A: Alone significantly decreased protospacer acquisition in vivo (PubMed:26478180). Decreased protospacer binding; in association with A-170 (PubMed:26478180). 1 Publication1
Mutagenesisi184T → A: No cleavage of any substrates. 1 Publication1
Mutagenesisi188Y → A: Partial inhibition of cleavage (PubMed:21219465). No effect on in vitro protospacer integration (PubMed:25707795). Significantly decreased protospacer acquisition in vivo (PubMed:26478180). 3 Publications1
Mutagenesisi208H → A: No cleavage of any substrates, no restoration of UV or MMC resistance (PubMed:21219465). Loss of spacer acquisition in vivo (PubMed:24793649, PubMed:25707795, PubMed:26478180). 4 Publications1
Mutagenesisi211K → A: No cleavage of any substrates. 1 Publication1
Mutagenesisi217Y → A: No effect on in vitro protospacer integration (PubMed:25707795). Alone significantly decreased protospacer acquisition in vivo (PubMed:26478180). Significantly decreased protospacer binding; in association with A-165 (PubMed:26478180). 2 Publications1
Mutagenesisi218D → A: No cleavage of any substrates, no restoration of UV or MMC resistance (PubMed:21219465). Loss of spacer acquisition in vivo (PubMed:24793649). 2 Publications1
Mutagenesisi221D → A: No cleavage of any substrates (PubMed:21219465). Loss of spacer acquisition in vivo (PubMed:24793649, PubMed:24920831, PubMed:25707795). No cleavage of CRISPR leader in preparation for spacer integration (PubMed:24920831). 4 Publications1
Mutagenesisi224K → A: No cleavage of any substrates (PubMed:21219465). Loss of spacer acquisition in vivo (PubMed:24793649, PubMed:25707795). 3 Publications1
Mutagenesisi245 – 248REVR → AEVA: Loss of spacer acquisition in vivo. 1 Publication4
Mutagenesisi245R → A: No effect on spacer acquisition. 1 Publication1
Mutagenesisi245R → D: Decreased spacer acquisition. 1 Publication1
Mutagenesisi245R → E: Dramatically decreased spacer acquisition in vivo. 1 Publication1
Mutagenesisi248R → E: Dramatically decreased spacer acquisition in vivo. 1 Publication1
Mutagenesisi252R → A: No effect on spacer acquisition. 1 Publication1
Mutagenesisi252R → E: Loss of spacer acquisition, no Cas1-Cas2 complex formation, loss of CRISPR DNA-binding by complex. Protein is stable and dimerizes. 1 Publication1
Mutagenesisi256 – 259RSSK → ASSA: Loss of spacer acquisition in vivo. 1 Publication4
Mutagenesisi256R → A: No effect on spacer acquisition. 1 Publication1
Mutagenesisi256R → E: Loss of spacer acquisition. 1 Publication1
Mutagenesisi282 – 305Missing : No effect on spacer acquisition, Cas1-Cas2 complex formation or CRISPR DNA-binding by complex. 1 PublicationAdd BLAST24
Mutagenesisi291I → G or R: No effect on spacer acquisition. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001693151 – 305CRISPR-associated endonuclease Cas1Add BLAST305

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q46896

PRoteomics IDEntifications database

More...
PRIDEi
Q46896

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Repressed by H-NS (PubMed:20132443). Activated by LeuO (PubMed:19429622). Activated by the BaeSR two-component regulatory system, possibly due to envelope stress (PubMed:21255106). Part of the casABCDE-ygbT-ygbF operon (PubMed:19429622).3 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:21219465). Part of the Cas1-Cas2 complex (PubMed:24920831, PubMed:24793649, PubMed:25707795, Ref. 11, PubMed:26478180, PubMed:26503043).

Interacts with RecB, RecC, RuvB, CasC and CasE (PubMed:21219465).

Forms a hexamer with 2 Cas1 dimers sandwiching a Cas2 dimer (PubMed:24793649, PubMed:26478180). The DNA lies across a flat surface extending from 1 Cas1 dimer, across the Cas2 dimer and contacting the other Cas1 dimer. Only 1 Cas1 protein from each dimer is catalytic, the other interacts with the Cas2 dimer and possibly target DNA (PubMed:26478180, PubMed:26503043).

1 Publication6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261582, 279 interactors
851560, 13 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-996 Cas1-Cas2 complex

Database of interacting proteins

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DIPi
DIP-12118N

Protein interaction database and analysis system

More...
IntActi
Q46896, 16 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2755

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1305
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q46896

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni96 – 278Sufficient for cleavage of ssRNA, ssDNA and Holliday junction DNAAdd BLAST183

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Substrate DNA-binding induces large structural changes that generate a surface for DNA-binding across the Cas2 dimer and formation of an optimal catalytic site (PubMed:26478180).1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG4105TZK Bacteria
COG1518 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000015862

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q46896

KEGG Orthology (KO)

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KOi
K15342

Family and domain databases

Conserved Domains Database

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CDDi
cd09719 Cas1_I-E, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.120.920, 1 hit
3.100.10.20, 1 hit

HAMAP database of protein families

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HAMAPi
MF_01470 Cas1, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR033641 Cas1_I-E
IPR002729 CRISPR-assoc_Cas1
IPR042206 CRISPR-assoc_Cas1_C
IPR019851 CRISPR-assoc_Cas1_ECOLI
IPR042211 CRISPR-assoc_Cas1_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01867 Cas_Cas1, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00287 cas1, 2 hits
TIGR03638 cas1_ECOLI, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q46896-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTWLPLNPIP LKDRVSMIFL QYGQIDVIDG AFVLIDKTGI RTHIPVGSVA
60 70 80 90 100
CIMLEPGTRV SHAAVRLAAQ VGTLLVWVGE AGVRVYASGQ PGGARSDKLL
110 120 130 140 150
YQAKLALDED LRLKVVRKMF ELRFGEPAPA RRSVEQLRGI EGSRVRATYA
160 170 180 190 200
LLAKQYGVTW NGRRYDPKDW EKGDTINQCI SAATSCLYGV TEAAILAAGY
210 220 230 240 250
APAIGFVHTG KPLSFVYDIA DIIKFDTVVP KAFEIARRNP GEPDREVRLA
260 270 280 290 300
CRDIFRSSKT LAKLIPLIED VLAAGEIQPP APPEDAQPVA IPLPVSLGDA

GHRSS
Length:305
Mass (Da):33,194
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i01A31BA98453D8A5
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U29579 Genomic DNA Translation: AAA69265.1
U00096 Genomic DNA Translation: AAC75797.1
AP009048 Genomic DNA Translation: BAE76832.1

Protein sequence database of the Protein Information Resource

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PIRi
G65056

NCBI Reference Sequences

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RefSeqi
NP_417235.1, NC_000913.3
WP_000220066.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
AAC75797; AAC75797; b2755
BAE76832; BAE76832; BAE76832

Database of genes from NCBI RefSeq genomes

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GeneIDi
947228

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ecj:JW2725
eco:b2755

Pathosystems Resource Integration Center (PATRIC)

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PATRICi
fig|1411691.4.peg.3983

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29579 Genomic DNA Translation: AAA69265.1
U00096 Genomic DNA Translation: AAC75797.1
AP009048 Genomic DNA Translation: BAE76832.1
PIRiG65056
RefSeqiNP_417235.1, NC_000913.3
WP_000220066.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NKDX-ray1.95A/B1-305[»]
3NKEX-ray1.40A/B/C92-291[»]
4P6IX-ray2.30C/D/E/F1-305[»]
4QDLX-ray2.70A/B/C/D1-305[»]
5DLJX-ray2.60A/B/C/D2-281[»]
5DQTX-ray3.10A/B/C/D/I/J/K/L1-305[»]
5DQUX-ray4.50A/B/C/D1-305[»]
5DQZX-ray2.70A/B/C/D1-305[»]
5DS4X-ray3.20A/B/C/D1-305[»]
5DS5X-ray2.95A/B/C/D1-305[»]
5DS6X-ray3.35A/B/C/D1-305[»]
5VVJX-ray3.89A/B/C/D1-305[»]
5VVKX-ray2.90A/B/C/D1-305[»]
5VVLX-ray3.31A/B/C/D1-305[»]
5WFEelectron microscopy3.64A/B/C/D1-305[»]
SMRiQ46896
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4261582, 279 interactors
851560, 13 interactors
ComplexPortaliCPX-996 Cas1-Cas2 complex
DIPiDIP-12118N
IntActiQ46896, 16 interactors
STRINGi511145.b2755

Proteomic databases

PaxDbiQ46896
PRIDEiQ46896

Genome annotation databases

EnsemblBacteriaiAAC75797; AAC75797; b2755
BAE76832; BAE76832; BAE76832
GeneIDi947228
KEGGiecj:JW2725
eco:b2755
PATRICifig|1411691.4.peg.3983

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

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EchoBASEi
EB2915

Phylogenomic databases

eggNOGiENOG4105TZK Bacteria
COG1518 LUCA
HOGENOMiHOG000015862
InParanoidiQ46896
KOiK15342

Enzyme and pathway databases

BioCyciEcoCyc:G7425-MONOMER
ECOL316407:JW2725-MONOMER

Miscellaneous databases

Protein Ontology

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PROi
PR:Q46896

Family and domain databases

CDDicd09719 Cas1_I-E, 1 hit
Gene3Di1.20.120.920, 1 hit
3.100.10.20, 1 hit
HAMAPiMF_01470 Cas1, 1 hit
InterProiView protein in InterPro
IPR033641 Cas1_I-E
IPR002729 CRISPR-assoc_Cas1
IPR042206 CRISPR-assoc_Cas1_C
IPR019851 CRISPR-assoc_Cas1_ECOLI
IPR042211 CRISPR-assoc_Cas1_N
PfamiView protein in Pfam
PF01867 Cas_Cas1, 1 hit
TIGRFAMsiTIGR00287 cas1, 2 hits
TIGR03638 cas1_ECOLI, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCAS1_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q46896
Secondary accession number(s): Q2MA74
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1996
Last modified: December 11, 2019
This is version 125 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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