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Entry version 92 (07 Apr 2021)
Sequence version 1 (21 Jul 1986)
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Protein

Terminase, large subunit

Gene

A

Organism
Escherichia phage lambda (Bacteriophage lambda)
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

The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end the packaging reaction (PubMed:11866517, PubMed:23134123).

The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (binding to packaging sequence cos), and a large terminase subunit possessing endonucleolytic, ATPase and helicase activities (DNA maturation and packaging) (PubMed:11866517, PubMed:23134123).

The terminase binds cooperatively with the host factor IHFA/IHFB to the cos site at the junction of adjacent viral genomes (PubMed:22191393, PubMed:15755448, PubMed:28445747).

The endonuclease activity cleaves the viral DNA generating 5'overhangs of 12 bp in length (PubMed:6315731, PubMed:2970303, PubMed:8428984, PubMed:7813453).

The helicase activity separates the cohesive ends generating the single-stranded 'sticky' ends of the mature genome (PubMed:6315731, PubMed:2970303, PubMed:8175794).

IHFA/IHFB is also necessary for the strand separation activity of the terminase (PubMed:22191393).

The terminase remains bound to the left end of the genome to be packaged, forming a stable DNA-terminase complex (PubMed:860405).

In a reaction facilitated by the viral assembly catalyst gpFI, the DNA-terminase complex binds to the portal of the procapsid thereby activating the translocase activity of the terminase (PubMed:2965251).

The terminase packages the viral DNA into the procapsid until the next cos site on the concatemer reaches the complex (PubMed:860405, PubMed:2965251) (Probable).

The downstream cos site is then cut generating the mature right end of the genome, the heterotrimer undocks from the DNA-filled head and remains bound to the left end of concatemer's next genome (PubMed:2970303).

UniRule annotation1 Publication12 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<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+UniRule annotation2 PublicationsNote: Probably binds 2 Mg2+ ions per subunit (By similarity). Necessary for the ATPase activity (PubMed:8428984, PubMed:8175794). Zn2+ Co2+, Cd2+, Cu2+, Ca2+, Sr2+ and Ba2+ do not function as cofactor (PubMed:8428984).By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Inhibited by NaCl and KC1 at concentrations higher than 100 mM and by glutamate at concentrations greater than 150 mM.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

The high affinity ATPase activity corresponds to the packaging ATPase site at the N-terminus.1 Publication1 Publication
  1. KM=4.6 µM for ATP for the high affinity ATPase3 Publications
  2. KM=23 µM for ATP for helicase1 Publication

    pH dependencei

    Optimum pH is 8.0-9.0 for the ATPase and helicase.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Sitei46ATP-bindingUniRule annotation1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei179For ATPase activityUniRule annotation1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi401Magnesium; catalytic; for nuclease activityUniRule annotation1

    <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 functionEndonuclease, Hydrolase, Nuclease
    Biological processViral genome packaging, Viral release from host cell
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Terminase, large subunit1 PublicationUniRule annotation
    Alternative name(s):
    DNA-packaging protein A
    Large terminase proteinUniRule annotation
    gpA
    Including the following 3 domains:
    EndonucleaseUniRule annotation (EC:3.1.21.4UniRule annotation6 Publications)
    HelicaseUniRule annotation (EC:3.6.4.12UniRule annotation2 Publications)
    ATPaseUniRule annotation (EC:3.6.4.-UniRule annotation5 Publications)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:A
    Ordered Locus Names:lambdap02
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 phage lambda (Bacteriophage lambda)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10710 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiVirusesDuplodnaviriaHeunggongviraeUroviricotaCaudoviricetesCaudoviralesSiphoviridaeLambdavirus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiEscherichia coli [TaxID: 562]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000001711 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Genome

    <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

    Keywords - Cellular componenti

    Host 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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi18G → E: Lethal, 97% defective in cos cleavage; 84% loss of DNA packaging. 1 Publication1
    Mutagenesisi46Y → A or E: Complete loss of high affinity ATPase activity and packaging; no significant effect on endonuclease or strand separation activities. 1 Publication1
    Mutagenesisi46Y → F: Complete loss of high affinity ATPase activity and packaging; no significant effect on endonuclease or strand separation activities. 40% decreased velocity of translocation and about 10 times more frequent slipping during DNA translocation. 2 Publications1
    Mutagenesisi76K → A: Complete loss of DNA packaging. 1 Publication1
    Mutagenesisi76K → R: Complete loss of DNA packaging, no effect on cos cleavage, slight increase in strand separation activity. 1 Publication1
    Mutagenesisi76K → R: Lethal, 85% defective in cos cleavage; complete loss of DNA packaging. 3 Publications1
    Mutagenesisi77S → V: Complete loss of DNA packaging probably due to a loss of DNA packaging initiation efficiency. 1 Publication1
    Mutagenesisi78A → V: Almost complete loss of DNA packaging; more frequent pausing during packaging. 1 Publication1
    Mutagenesisi79R → A: Complete loss of ATPase and DNA packaging activities. 1 Publication1
    Mutagenesisi79R → K: Almost complete loss of DNA packaging; much lower motor velocity and more frequent pausing during packaging. 1 Publication1
    Mutagenesisi80V → A: Intermediate loss of DNA packaging; more frequent pausing during packaging. 1 Publication1
    Mutagenesisi81G → A: Almost complete loss of DNA packaging; much lower motor velocity. 1 Publication1
    Mutagenesisi82Y → A: Intermediate loss of DNA packaging; much lower motor velocity. 1 Publication1
    Mutagenesisi83S → A: Almost complete loss of ATPase and DNA packaging activities. 1 Publication1
    Mutagenesisi83S → T: Intermediate loss of DNA packaging. 1 Publication1
    Mutagenesisi84K → A: 40% decreased velocity of translocation and 95% loss of DNA packaging. 1 Publication1
    Mutagenesisi84K → E: Complete loss of high affinity ATPase activity and packaging; no significant effect on endonuclease activity and slight decrease in strand separation. 1 Publication1
    Mutagenesisi166N → Y: Lethal, 95% defective in cos cleavage; almost complete loss of DNA packaging. 1 Publication1
    Mutagenesisi179E → A or Q: Lethal; very weak ATP hydrolysis and complete loss of packaging. 1 Publication1
    Mutagenesisi179E → C, G, I, L, N, P, R or V: Lethal. 1 Publication1
    Mutagenesisi179E → D: Lethal; weak ATP hydrolysis and complete loss of packaging, translocation does not seem to be impaired. 1 Publication1
    Mutagenesisi180L → F: Lethal, 91% defective in cos cleavage; 99% loss of DNA packaging, incomplete packaging. 1 Publication1
    Mutagenesisi191G → S: Lethal, 83% defective in cos cleavage; complete loss of DNA packaging. 1 Publication1
    Mutagenesisi194T → M: Lethal, 66% defective in cos cleavage; 99% loss of DNA packaging, incomplete packaging. 1 Publication1
    Mutagenesisi212G → S: Lethal, 77% defective in cos cleavage; 96% loss of DNA packaging, slow and incomplete packaging. 1 Publication1
    Mutagenesisi225R → H: Lethal, 78% defective in cos cleavage; 84% loss of DNA packaging. 1 Publication1
    Mutagenesisi328T → I: Lethal, 90% defective in cos cleavage; 83% loss of DNA packaging. 1 Publication1
    Mutagenesisi349D → G: Lethal, 89% defective in cos cleavage; 90% loss of DNA packaging. 1 Publication1
    Mutagenesisi401D → G: Completely defective in cos cleavage. 1 Publication1
    Mutagenesisi497K → A: Lethal, 1000x reduced cos cleavage, no effect on DNA translocation, increased Km for ATPase to 9.8. 2 Publications1
    Mutagenesisi497K → D: Lethal, 2000x reduced cos cleavage, no effect on DNA translocation, increased Km for ATPase to 24.4. 2 Publications1
    Mutagenesisi497K → R: Km for ATPase increased to 68. 1 Publication1
    Mutagenesisi586E → K: Completely defective in cos 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000776731 – 641Terminase, large subunitAdd BLAST641

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Heterotrimer of two small and one large terminase subunits (Probable) (PubMed:6315731, PubMed:15755448, PubMed:8428984, PubMed:30541105). The catalytically competent terminase is composed of a tetramer of heterotrimers (PubMed:30541105, PubMed:28445747, PubMed:8175794, PubMed:8794874, PubMed:9705918, PubMed:10993723). The tetramer forms a ring structure large enough to encircle duplex DNA (PubMed:30541105). Host IHFA/IHFB induces bending of viral DNA to facilitate the assembly of the terminase tetramer of heterotrimers (PubMed:17176048, PubMed:28445747).

    Interacts (via N-terminus) with the terminase small subunit (via C-terminus) (PubMed:2969839).

    Interacts (via C-terminus) with the portal protein; this interaction allows the packaging of viral DNA (PubMed:7799432).

    UniRule annotation1 Publication12 Publications

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    P03708, 10 interactors

    <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

    <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 – 48Interaction with the terminase small subunitUniRule annotation1 PublicationAdd BLAST48
    Regioni166 – 353DNA packaging/ATPaseUniRule annotationAdd BLAST188
    Regioni166 – 349DNA packaging/ATPase1 Publication1 PublicationAdd BLAST184
    Regioni401 – 586Endonuclease/helicaseUniRule annotation1 Publication1 PublicationAdd BLAST186
    Regioni491 – 498ATP-bindingUniRule annotation3 Publications8
    Regioni573 – 584Basic1 PublicationAdd BLAST12
    Regioni588 – 616Leucine zipperUniRule annotationAdd BLAST29
    Regioni610 – 641Prohead bindingUniRule annotationAdd BLAST32

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi42 – 51Q motif1 Publication10
    Motifi76 – 83Walker A motifUniRule annotation1 Publication4 Publications8
    Motifi174 – 179Walker B motifUniRule annotation1 Publication6

    <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

    The N-terminus is involved in the formation of the heterotrimer with the small subunit (PubMed:2969839). The N-terminus part contains the translocase activity involved in DNA packaging (PubMed:11866517). At the N-terminus, there is a high affinity ATPase center that is probably needed for the packaging activity (PubMed:8611586, PubMed:8794874, PubMed:19706522, PubMed:9705918, PubMed:10993723). The Walker A motif of the ATPase center is responsible for interacting with the ATP phosphate and the Q motif governs force generation and the interaction with DNA (PubMed:19706522). The C-terminus contains the site specific endonuclease (cos-cleavage) and strand separation (helicase) activities required for genome maturation (PubMed:17870092). A second ATPase catalytic site regulates the genome maturation (PubMed:17870092). The C-terminus very end is involved in binding to the procapsid (PubMed:2969839). Contains a basic leucine zipper (bZIP) that may be involved in the formation of the terminase (PubMed:1534952) (Probable).UniRule annotation1 Publication9 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 lambdavirus large terminase family.UniRule annotation

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_04144, TERL_LAMBDA, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR008866, Phage_lambda_GpA-like

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF05876, Terminase_GpA, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P03708-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNISNSQVNR LRHFVRAGLR SLFRPEPQTA VEWADANYYL PKESAYQEGR
    60 70 80 90 100
    WETLPFQRAI MNAMGSDYIR EVNVVKSARV GYSKMLLGVY AYFIEHKQRN
    110 120 130 140 150
    TLIWLPTDGD AENFMKTHVE PTIRDIPSLL ALAPWYGKKH RDNTLTMKRF
    160 170 180 190 200
    TNGRGFWCLG GKAAKNYREK SVDVAGYDEL AAFDDDIEQE GSPTFLGDKR
    210 220 230 240 250
    IEGSVWPKSI RGSTPKVRGT CQIERAASES PHFMRFHVAC PHCGEEQYLK
    260 270 280 290 300
    FGDKETPFGL KWTPDDPSSV FYLCEHNACV IRQQELDFTD ARYICEKTGI
    310 320 330 340 350
    WTRDGILWFS SSGEEIEPPD SVTFHIWTAY SPFTTWVQIV KDWMKTKGDT
    360 370 380 390 400
    GKRKTFVNTT LGETWEAKIG ERPDAEVMAE RKEHYSAPVP DRVAYLTAGI
    410 420 430 440 450
    DSQLDRYEMR VWGWGPGEES WLIDRQIIMG RHDDEQTLLR VDEAINKTYT
    460 470 480 490 500
    RRNGAEMSIS RICWDTGGID PTIVYERSKK HGLFRVIPIK GASVYGKPVA
    510 520 530 540 550
    SMPRKRNKNG VYLTEIGTDT AKEQIYNRFT LTPEGDEPLP GAVHFPNNPD
    560 570 580 590 600
    IFDLTEAQQL TAEEQVEKWV DGRKKILWDS KKRRNEALDC FVYALAALRI
    610 620 630 640
    SISRWQLDLS ALLASLQEED GAATNKKTLA DYARALSGED E
    Length:641
    Mass (Da):73,302
    Last modified:July 21, 1986 - 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:i4C5719C9A2D87B7A
    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
    J02459 Genomic DNA Translation: AAA96534.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    D04333, JVBPAL

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_040581.1, NC_001416.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    2703524

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    vg:2703524

    <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
    J02459 Genomic DNA Translation: AAA96534.1
    PIRiD04333, JVBPAL
    RefSeqiNP_040581.1, NC_001416.1

    3D structure databases

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    SWISS-MODEL Interactive Workspace

    More...
    SWISS-MODEL-Workspacei
    Submit a new modelling project...

    Protein-protein interaction databases

    IntActiP03708, 10 interactors

    Genome annotation databases

    GeneIDi2703524
    KEGGivg:2703524

    Family and domain databases

    HAMAPiMF_04144, TERL_LAMBDA, 1 hit
    InterProiView protein in InterPro
    IPR008866, Phage_lambda_GpA-like
    PfamiView protein in Pfam
    PF05876, Terminase_GpA, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    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 nameiTERL_LAMBD
    <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: P03708
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: April 7, 2021
    This is version 92 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 programViral 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

    Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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