ID M1Q730_9CAUD Unreviewed; 681 AA.
AC M1Q730;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Terminase, large subunit {ECO:0000256|HAMAP-Rule:MF_04144};
DE AltName: Full=DNA-packaging protein {ECO:0000256|HAMAP-Rule:MF_04144};
DE AltName: Full=Large terminase protein {ECO:0000256|HAMAP-Rule:MF_04144};
DE Includes:
DE RecName: Full=Endonuclease {ECO:0000256|HAMAP-Rule:MF_04144};
DE EC=3.1.21.4 {ECO:0000256|HAMAP-Rule:MF_04144};
DE Includes:
DE RecName: Full=Helicase {ECO:0000256|HAMAP-Rule:MF_04144};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_04144};
DE Includes:
DE RecName: Full=ATPase {ECO:0000256|HAMAP-Rule:MF_04144};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_04144};
GN ORFNames=CDPG_00064 {ECO:0000313|EMBL:AGF91668.1}, Phi47:1_gp04
GN {ECO:0000313|EMBL:AGO49741.1};
OS Cellulophaga phage phi47:1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=756281 {ECO:0000313|EMBL:AGF91668.1, ECO:0000313|Proteomes:UP000297571};
RN [1] {ECO:0000313|EMBL:AGF91668.1, ECO:0000313|Proteomes:UP000297571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Henn M.R., Reimann L., Holmfelt K., Levin J., Malboeuf C., Casali M.,
RA Russ C., Lennon N., Chapman S., Erlich R., Young S.K., Yandava C., Zeng Q.,
RA Fitzgerald M., Alvarado L., Anderson S., Berlin A., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Green L., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D., Hollinger A., Howarth C., Larson L., Mehta T., Neiman D.,
RA Pearson M., Roberts A., Ryan E., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., White J., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cellulophaga phage phi47:1.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGO49741.1, ECO:0000313|Proteomes:UP000014738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phi47:1 {ECO:0000313|EMBL:AGO49741.1};
RX PubMed=23858439; DOI=10.1073/pnas.1305956110;
RA Holmfeldt K., Solonenko N., Shah M., Corrier K., Riemann L.,
RA Verberkmoes N.C., Sullivan M.B.;
RT "Twelve previously unknown phage genera are ubiquitous in global oceans.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:12798-12803(2013).
RN [3] {ECO:0000313|Proteomes:UP000014738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Holmfeldt K., Solonenko N., Shah M., Corrier K., Riemann L.,
RA VerBerkmoes N.C., Sullivan M.B.;
RT "The Cellulophaga phages: a novel, diverse, and globally ubiquitous model
RT system.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The terminase large subunit acts as an ATP driven molecular
CC motor necessary for viral DNA translocation into empty capsids and as
CC an endonuclease that cuts the viral genome from the concetamer to
CC initiate and to end the packaging reaction. The terminase lies at a
CC unique vertex of the procapsid and is composed of two subunits, a small
CC terminase subunit involved in viral DNA recognition, and a large
CC terminase subunit possessing endonucleolytic, ATPase and helicase
CC activities (DNA maturation and packaging). The endonuclease activity
CC cleaves the viral DNA generating 5'overhangs. The helicase activity
CC separates the cohesive ends generating the single-stranded 'sticky'
CC ends of the mature genome. The DNA-terminase complex binds to the
CC portal of the procapsid thereby activating the translocase activity of
CC the terminase. The terminase packages the viral DNA into the procapsid
CC until the next concatemer reaches the complex. The downstream site is
CC then cut generating the mature right end of the genome, the
CC heterotrimer undocks from the DNA-filled head and remains bound to the
CC left end of concatemer's next genome. {ECO:0000256|HAMAP-
CC Rule:MF_04144}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_04144};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04144};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04144};
CC -!- SUBUNIT: Interacts (via N-terminus) with the terminase small subunit
CC (via C-terminus); the active complex is probably heterooligomeric.
CC Interacts (via C-terminus) with the portal protein; this interaction
CC allows the packaging of viral DNA. {ECO:0000256|HAMAP-Rule:MF_04144}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04144}.
CC Note=The terminase lies at a unique vertex of the procapsid during
CC viral DNA packaging. {ECO:0000256|HAMAP-Rule:MF_04144}.
CC -!- DOMAIN: The N-terminus is involved in the formation of the heterotrimer
CC with the small subunit. The N-terminus part contains the translocase
CC activity involved in DNA packaging. At the N-terminus, there is a high
CC affinity ATPase center that is probably needed for the packaging
CC activity. The Walker A motif of the ATPase center is responsible for
CC interacting with the ATP phosphate and the Q motif governs force
CC generation and the interaction with DNA. The C-terminus contains the
CC site specific endonuclease (cos-cleavage) and strand separation
CC (helicase) activities required for genome maturation. A second ATPase
CC catalytic site regulates the genome maturation. The C-terminus very end
CC is involved in binding to the procapsid. Contains a basic leucine
CC zipper (bZIP) that may be involved in the formation of the terminase.
CC {ECO:0000256|HAMAP-Rule:MF_04144}.
CC -!- SIMILARITY: Belongs to the lambdavirus large terminase family.
CC {ECO:0000256|HAMAP-Rule:MF_04144}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04144}.
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DR EMBL; HQ670749; AGF91668.1; -; Genomic_DNA.
DR EMBL; KC821634; AGO49741.1; -; Genomic_DNA.
DR Proteomes; UP000014738; Genome.
DR Proteomes; UP000297571; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098009; C:viral terminase, large subunit; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_04144; TERL_LAMBDA; 1.
DR InterPro; IPR046453; GpA_ATPase.
DR InterPro; IPR046454; GpA_endonuclease.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008866; Phage_lambda_GpA-like.
DR Pfam; PF05876; GpA_ATPase; 1.
DR Pfam; PF20454; GpA_nuclease; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04144};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_04144};
KW Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04144};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04144};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04144};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04144};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_04144};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04144};
KW Reference proteome {ECO:0000313|Proteomes:UP000297571};
KW Viral genome packaging {ECO:0000256|HAMAP-Rule:MF_04144};
KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04144}.
FT DOMAIN 44..307
FT /note="Phage terminase large subunit GpA ATPase"
FT /evidence="ECO:0000259|Pfam:PF05876"
FT DOMAIN 319..655
FT /note="Terminase large subunit GpA endonuclease"
FT /evidence="ECO:0000259|Pfam:PF20454"
FT BINDING 414
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04144"
SQ SEQUENCE 681 AA; 78504 MW; B72D71D789FCEC41 CRC64;
MNLKDIWKQQ LNFFNSKLYS YKTIKAIPSE WVEKTIILDP EVSRFSGRYS YDLSPYAREI
IDNLHPSNPY KIISVMKGAQ SGITQGVIVP GMAWIISEHP DNFLFTASDK EIAKLTITTR
FDNIMQSSGL KHLIRPNTSR SKGQRSGDTD FSKEFAGGSA IIEGTNNAGK FRFFSVKTVF
MDDFDNAPRA DKKEGSIRKL VEGRQTSYGN LAKTFYVSTP TITQTSNVYE MYLQGDQRKW
HWPCPECNEF VPSDWRIKKA DGSFAGIVYE LDSENRLIEE SVFFKCPCCG HNISNNEKHD
LNNKGKWIAT AIPKDKYYRS YYMNSLIIPP GFINWVDLVK EWLEACPPNK KPNSDLLKVF
NNVRLGLPFE EKGEAPKMMQ LMENIRDYRV GIVPDRTSIE DGNGEIILIT LAADLGGIMN
NETEDVRIDW EIMAHAANGA TYSINQGSLG TFKRSRTRTE EDKVKESDRI KYTYMHGMKH
SVWPLLEKII KEDLIGESGD LYDIKLSVID TGHFTKHAYE FIKKTHDSEN WVFGIKGIPE
INYRRNTKDV ALVKKSANIQ NLYLLDVEQL KDNLAANMKL RRADDETQES GFMNFPVQEK
NKYAMNTYFK HFQSEVRKEV IENGESTGWK WEKKNSSVEN HFWDVRIYNN AARDMFIDLI
KRTDPSQFKD LTWDLFVESL N
//
