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UniProtKB - A0Q7Q2 (CS12A_FRATN)

Protein

CRISPR-associated endonuclease Cas12a

Gene

cas12a

Organism
Francisella tularensis subsp. novicida (strain U112)
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). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Has endonuclease activity on pre-crRNA and dsDNA, using different active sites. A single-RNA guided endonuclease that is also capable of guiding crRNA processing; correct processing of pre-crRNA requires only this protein and the CRISPR locus (PubMed:26422227, PubMed:27096362). pre-crRNA processing proceeds by an intramolecular nucleophilic attack on the scissile phosphate by the 2'-OH of the upstream ribonucleotide, the divalent cation (which is bound by the crRNA) is probably required for ordering the crRNA pseudoknot and/or increasing RNA binding (PubMed:28431230). RNA mutagenesis studies show pre-crRNA cleavage is highly sequence- and structure-specific (PubMed:27096362). Forms a complex with crRNA and complementary dsDNA, where the crRNA displaces the non-target DNA strand and directs endonucleolytic cleavage of both strands of the DNA (PubMed:26422227, PubMed:27096362, PubMed:28431230). Cleavage results in staggered 5-base 5' overhangs 14-18 and 21-23 bases downstream of the PAM (protospacer adjacent motif) on the non-target and target strands respectively (PubMed:26422227, PubMed:28431230, PubMed:28562584). Both target and non-target strand DNA are probably independently cleaved in the same active site (PubMed:28431230, PubMed:28562584). When this protein is expressed in E.coli it prevents plasmids homologous to the first CRISPR spacer from transforming, formally showing it is responsible for plasmid immunity (PubMed:26422227).4 Publications

Miscellaneous

Part of a type V-A CRISPR-Cas system.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.1 Publication EC:3.1.21.1
  • Endonucleolytic cleavage to 2',3'-cyclic nucleotides.1 Publication EC:3.1.27.2

<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

Ca2+1 Publication, Mg2+4 PublicationsNote: Cleavage of dsDNA requires Mg2+ (PubMed:26422227, PubMed:28562584). Another report shows DNA cleavage occurs equally well in the presence of Ca2+ or Mg2+ (PubMed:27096362). Processing of pre-crRNA requires a divalent cation, preferably Mg2+ which is bound by the crRNA (PubMed:26593719, PubMed:28431230).5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei16crRNA alone and in crRNA-target DNA heteroduplex2 Publications1
Binding sitei131Target strand DNA1 Publication1
Binding sitei295crRNA in crRNA-target DNA heteroduplex1 Publication1
Binding sitei320DNA in crRNA-target DNA heteroduplex1 Publication1
Binding sitei334DNA in crRNA-target DNA heteroduplex1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei410Caps the crRNA-target DNA heteroduplex1 Publication1
Binding sitei589DNA in crRNA-target DNA heteroduplex1 Publication1
Binding sitei613DNA protospacer adjacent motif (PAM)2 Publications1
Binding sitei667Target strand DNA1 Publication1
Binding sitei671PAM2 Publications1
Binding sitei677Target strand DNA2 Publications1
Binding sitei823Target strand DNA2 Publications1
Binding sitei826Target strand DNA; via amide nitrogen2 Publications1
Binding sitei833crRNA1 Publication1
<p>This subsection of the ‘Function’ 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 sitei843For pre-crRNA processing1 Publication1
Active sitei852For pre-crRNA processing1 Publication1
Sitei852Stabilizes transition state for pre-crRNA processing1 Publication1
Active sitei869For pre-crRNA processing1 Publication1
Active sitei917For DNase activity of RuvC domain1 Publication1
Active sitei1006For DNase activity of RuvC domain1 Publication1
Binding sitei1026DNA in crRNA-target DNA heteroduplex2 Publications1
Binding sitei1063DNA in crRNA-target DNA heteroduplex2 Publications1
Active sitei1255For DNase activity of RuvC domain1 Publication1

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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, RNA-binding
Biological processAntiviral defense
LigandCalcium, Magnesium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		FTUL401614:G1G75-1444-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 Cas12a1 Publication (EC:3.1.21.11 Publication, EC:3.1.27.21 Publication)
Alternative name(s):
CRISPR-associated endonuclease Cpf11 Publication
FnCas12a1 Publication
FnCpf11 Publication
<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:cas12a1 Publication
Synonyms:cpf11 Publication
Ordered Locus Names:FTN_1397
<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>OrganismiFrancisella tularensis subsp. novicida (strain U112)
<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 identifieri401614 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Francisellaceae › Francisella ›
<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
  • UP000000762 <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

<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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

This class of CRISPR enzymes recognize a 5' T-rich protospacer adjacent motif (PAM, TTN for this specific enzyme), unlike Cas9 enzymes which recognize 3' G-rich PAMs, thus this enzyme increases the possibilites for genome editing (PubMed:26422227). The simplicity of the Cas12a-crRNA directed DNA endonuclease activity has been used to target and modify DNA sequences in rice and tobacco (PubMed:27905529).1 Publication2 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>Mutagenesisi608G → A or E: 15% DNA cleavage. 1 Publication1
Mutagenesisi663P → A: 25% DNA cleavage, altered non-target strand cleavage products. 1 Publication1
Mutagenesisi666N → A: 80% DNA cleavage, altered non-target strand cleavage products. 1 Publication1
Mutagenesisi667K → A: 30% DNA cleavage. 1 Publication1
Mutagenesisi671K → A: 15% DNA cleavage. 1 Publication1
Mutagenesisi677K → A: 35% DNA cleavage, altered non-target strand cleavage products. 1 Publication1
Mutagenesisi692R → A: Slight decrease in target DNA cleavage, 30% DNA cleavage, altered non-target strand cleavage products. 2 Publications1
Mutagenesisi694H → A: Wild-type DNA cleavage, altered non-target strand cleavage products. 1 Publication1
Mutagenesisi698 – 702TKNGS → AGGGG: Loss of target DNA cleavage. 1 Publication5
Mutagenesisi704Q → A: Significant decrease in target DNA cleavage. 1 Publication1
Mutagenesisi843H → A: Decreased pre-crRNA processing in vitro, binds RNA, no change in DNA cleavage. 1 Publication1
Mutagenesisi852K → A: Decreased pre-crRNA processing in vitro, binds RNA, no change in DNA cleavage. 1 Publication1
Mutagenesisi869K → A: Decreased pre-crRNA processing in vitro, binds RNA, no change in DNA cleavage. 1 Publication1
Mutagenesisi873F → A: Decreased pre-crRNA processing in vitro, no pre-crRNA processing in E.coli, binds RNA, no change in DNA cleavage. 1 Publication1
Mutagenesisi917D → A: Loss of target and non-target strand DNA cleavage, no change in DNA-binding or pre-crRNA processing. 3 Publications1
Mutagenesisi920E → A: No longer cleaves DNA in presence of Ca(2+). 1 Publication1
Mutagenesisi922H → A: Decreased cleavage of target strand in presence of Ca(2+), wild-type cleavage of DNA in presence of Mg(2+). 1 Publication1
Mutagenesisi925Y → A: Decreased cleavage of target strand in presence of Ca(2+), wild-type cleavage of DNA in presence of Mg(2+). 1 Publication1
Mutagenesisi1006E → A: Loss of target and non-target strand DNA cleavage, no change in DNA-binding or pre-crRNA processing. 4 Publications1
Mutagenesisi1006E → Q: Complete loss of DNA cleavage, still binds crRNA; when associated with A-1218. 1 Publication1
Mutagenesisi1024Y → A: No longer cleaves DNA in presence of Ca(2+). 1 Publication1
Mutagenesisi1028E → A: No longer cleaves DNA in presence of Ca(2+), reduced cleavage of non-target strand in presence of Mg(2+). 1 Publication1
Mutagenesisi1065 – 1066KK → AA: 67% DNA cleavage, altered non-target strand cleavage products. 1 Publication2
Mutagenesisi1218R → A: Cleaves both target and non-target strand DNA. Complete loss of DNA cleavage, still binds crRNA; when associated with Q-1006. 2 Publications1
Mutagenesisi1227D → A: No longer cleaves DNA in presence of Ca(2+). 1 Publication1
Mutagenesisi1255D → A: Significant reduction to loss of target and non-target strand DNA cleavage, no change in DNA-binding or pre-crRNA processing. 3 Publications1
Mutagenesisi1255D → N: Significant reduction of target and non-target strand DNA cleavage. 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_00004349021 – 1300CRISPR-associated endonuclease Cas12aAdd BLAST1300

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		A0Q7Q2

<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

Might be a homodimer (PubMed:26422227). Might be a monomer (PubMed:27096362, PubMed:28431230).3 Publications

<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

11300
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		A0Q7Q2

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

More...SMRi		A0Q7Q2

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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>Regioni1 – 24Wedge region 12 PublicationsAdd BLAST24
Regioni25 – 339Recognition domain 12 PublicationsAdd BLAST315
Regioni47 – 51Binds crRNA alone and in crRNA-target DNA heteroduplex2 Publications5
Regioni182 – 186Binds crRNA alone and in crRNA-target DNA heteroduplex2 Publications5
Regioni301 – 305Binds DNA in crRNA-target DNA heteroduplex1 Publication5
Regioni326 – 329Binds crRNA in crRNA-target DNA heteroduplex2 Publications4
Regioni340 – 591Recognition domain 22 PublicationsAdd BLAST252
Regioni538 – 541Binds crRNA in crRNA-target DNA heteroduplex1 Publication4
Regioni591 – 595Binds crRNA1 Publication5
Regioni592 – 662Wedge region 22 PublicationsAdd BLAST71
Regioni662 – 679LKL, important for PAM recognition and DNA unwinding1 PublicationAdd BLAST18
Regioni663 – 762PAM-interacting domain (PI)2 PublicationsAdd BLAST100
Regioni671 – 677Binds DNA protospacer adjacent motif (PAM) on target DNA2 Publications7
Regioni692 – 704Binds single-strand non-target DNA1 PublicationAdd BLAST13
Regioni763 – 892Wedge region 32 PublicationsAdd BLAST130
Regioni791 – 794Binds crRNA1 Publication4
Regioni803 – 804Binds crRNA1 Publication2
Regioni851 – 853Binds crRNA2 Publications3
Regioni865 – 873Binds crRNA2 Publications9
Regioni893 – 953RuvC-I2 PublicationsAdd BLAST61
Regioni954 – 971Bridge helix2 PublicationsAdd BLAST18
Regioni972 – 1078RuvC-II2 PublicationsAdd BLAST107
Regioni1079 – 1254Nuclease domain2 PublicationsAdd BLAST176
Regioni1255 – 1300RuvC-III2 PublicationsAdd BLAST46

<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

Has bilobed structure, with the REC lobe (residues 25-591) connected to the NUC lobe (662-1300) by a discontinuous wedge domain (PubMed:28431230, PubMed:28562584). The REC lobe binds the (pre-)crRNA and the crRNA-target DNA heteroduplex (PubMed:28431230, PubMed:28562584). The heteroduplex as well as part of the DNA downstream of the heteroduplex is protected in the central cavity formed by the NUC and REC lobes, which also positions target and non-target DNA for cleavage after domain rearrangement (PubMed:28431230, PubMed:28562584). The LKL region (residues 662 to 679) inserts into target dsDNA initiating its disruption to allow crRNA hybridization, is also involved in determining the non-target strand cleavage site (PubMed:28562584). A 'septum' formed by resdiues 197-204 and 1061-1070 separates the 2 DNA strands, preventing their reannealing, this region also influences the non-target cleavage site (PubMed:28562584).2 Publications

<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

Belongs to the CRISPR-associated endonuclease Cas12a family.1 Publication

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000066230

Identification of Orthologs from Complete Genome Data

More...OMAi		QIYNKDF

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027620 Cas12a

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR04330 cas_Cpf1, 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>.<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.

A0Q7Q2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSIYQEFVNK YSLSKTLRFE LIPQGKTLEN IKARGLILDD EKRAKDYKKA 
        60         70         80         90        100
KQIIDKYHQF FIEEILSSVC ISEDLLQNYS DVYFKLKKSD DDNLQKDFKS 
       110        120        130        140        150
AKDTIKKQIS EYIKDSEKFK NLFNQNLIDA KKGQESDLIL WLKQSKDNGI 
       160        170        180        190        200
ELFKANSDIT DIDEALEIIK SFKGWTTYFK GFHENRKNVY SSNDIPTSII 
       210        220        230        240        250
YRIVDDNLPK FLENKAKYES LKDKAPEAIN YEQIKKDLAE ELTFDIDYKT 
       260        270        280        290        300
SEVNQRVFSL DEVFEIANFN NYLNQSGITK FNTIIGGKFV NGENTKRKGI 
       310        320        330        340        350
NEYINLYSQQ INDKTLKKYK MSVLFKQILS DTESKSFVID KLEDDSDVVT 
       360        370        380        390        400
TMQSFYEQIA AFKTVEEKSI KETLSLLFDD LKAQKLDLSK IYFKNDKSLT 
       410        420        430        440        450
DLSQQVFDDY SVIGTAVLEY ITQQIAPKNL DNPSKKEQEL IAKKTEKAKY 
       460        470        480        490        500
LSLETIKLAL EEFNKHRDID KQCRFEEILA NFAAIPMIFD EIAQNKDNLA 
       510        520        530        540        550
QISIKYQNQG KKDLLQASAE DDVKAIKDLL DQTNNLLHKL KIFHISQSED 
       560        570        580        590        600
KANILDKDEH FYLVFEECYF ELANIVPLYN KIRNYITQKP YSDEKFKLNF 
       610        620        630        640        650
ENSTLANGWD KNKEPDNTAI LFIKDDKYYL GVMNKKNNKI FDDKAIKENK 
       660        670        680        690        700
GEGYKKIVYK LLPGANKMLP KVFFSAKSIK FYNPSEDILR IRNHSTHTKN 
       710        720        730        740        750
GSPQKGYEKF EFNIEDCRKF IDFYKQSISK HPEWKDFGFR FSDTQRYNSI 
       760        770        780        790        800
DEFYREVENQ GYKLTFENIS ESYIDSVVNQ GKLYLFQIYN KDFSAYSKGR 
       810        820        830        840        850
PNLHTLYWKA LFDERNLQDV VYKLNGEAEL FYRKQSIPKK ITHPAKEAIA 
       860        870        880        890        900
NKNKDNPKKE SVFEYDLIKD KRFTEDKFFF HCPITINFKS SGANKFNDEI 
       910        920        930        940        950
NLLLKEKAND VHILSIDRGE RHLAYYTLVD GKGNIIKQDT FNIIGNDRMK 
       960        970        980        990       1000
TNYHDKLAAI EKDRDSARKD WKKINNIKEM KEGYLSQVVH EIAKLVIEYN 
      1010       1020       1030       1040       1050
AIVVFEDLNF GFKRGRFKVE KQVYQKLEKM LIEKLNYLVF KDNEFDKTGG 
      1060       1070       1080       1090       1100
VLRAYQLTAP FETFKKMGKQ TGIIYYVPAG FTSKICPVTG FVNQLYPKYE 
      1110       1120       1130       1140       1150
SVSKSQEFFS KFDKICYNLD KGYFEFSFDY KNFGDKAAKG KWTIASFGSR 
      1160       1170       1180       1190       1200
LINFRNSDKN HNWDTREVYP TKELEKLLKD YSIEYGHGEC IKAAICGESD 
      1210       1220       1230       1240       1250
KKFFAKLTSV LNTILQMRNS KTGTELDYLI SPVADVNGNF FDSRQAPKNM 
      1260       1270       1280       1290       1300
PQDADANGAY HIGLKGLMLL GRIKNNQEGK KLNLVIKNEE YFEFVQNRNN
Length:1,300
Mass (Da):151,915
Last modified:January 9, 2007 - 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:i601E903DE68C80DE
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
CP000439 Genomic DNA Translation: ABK90267.1

NCBI Reference Sequences

More...RefSeqi		WP_003040289.1, NZ_CP009633.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		ABK90267; ABK90267; FTN_1397

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ftn:FTN_1397
ftx:AW25_605

<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
CP000439 Genomic DNA Translation: ABK90267.1
RefSeqiWP_003040289.1, NZ_CP009633.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5MGAX-ray3.00A1-1300[»]
5NFVX-ray2.50A2-1300[»]
5NG6X-ray3.34A/C/E/G2-1300[»]
ProteinModelPortaliA0Q7Q2
SMRiA0Q7Q2
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA0Q7Q2

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK90267; ABK90267; FTN_1397
KEGGiftn:FTN_1397
ftx:AW25_605

Phylogenomic databases

HOGENOMiHOG000066230
OMAiQIYNKDF

Enzyme and pathway databases

BioCyciFTUL401614:G1G75-1444-MONOMER

Family and domain databases

InterProiView protein in InterPro
IPR027620 Cas12a
TIGRFAMsiTIGR04330 cas_Cpf1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiCS12A_FRATN
<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: A0Q7Q2
<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: December 9, 2015
Last sequence update: January 9, 2007
Last modified: December 5, 2018
This is version 53 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, Complete 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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