ID A0A898BDZ4_9CAUD Unreviewed; 482 AA. AC A0A898BDZ4; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. DE RecName: Full=Terminase, large subunit {ECO:0000256|HAMAP-Rule:MF_04148}; DE AltName: Full=DNA-packaging protein gp2 {ECO:0000256|HAMAP-Rule:MF_04148}; DE Includes: DE RecName: Full=Endonuclease {ECO:0000256|HAMAP-Rule:MF_04148}; DE EC=3.1.21.- {ECO:0000256|HAMAP-Rule:MF_04148}; DE Includes: DE RecName: Full=ATPase {ECO:0000256|HAMAP-Rule:MF_04148}; DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_04148}; OS Pseudomonas phage vB_PaeP_fHoPae04. OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Caudovirales; Podoviridae; Bruynoghevirus; unclassified Bruynoghevirus. OX NCBI_TaxID=2811507 {ECO:0000313|EMBL:QSH71736.1, ECO:0000313|Proteomes:UP000663196}; RN [1] {ECO:0000313|EMBL:QSH71736.1} RP NUCLEOTIDE SEQUENCE. RA Patpatia S., Yilmaz O., Ylanne M., Kiljunen S.; RT "The isolation and genomic analysis of a lytic phage vB_PaeP_fHoPae04 RT infecting Pseudomonas aeruginosa."; RL Submitted (DEC-2020) 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 to initiate and to end a CC packaging reaction. The terminase lies at a unique vertex of the CC procapsid and is composed of two subunits, a small terminase subunit CC involved in viral DNA recognition (packaging sequence), and a large CC terminase subunit possessing endonucleolytic and ATPase activities. CC Both terminase subunits heterooligomerize and are docked on the portal CC protein to form the packaging machine. Once the capsid is packaged with CC the DNA, the terminase cleaves the viral genome concatemer and is CC substituted by the tail. {ECO:0000256|HAMAP-Rule:MF_04148}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_04148}; CC Note=Nuclease activity probably requires 2 Mg(2+) ions per subunit. CC {ECO:0000256|HAMAP-Rule:MF_04148}; CC -!- SUBUNIT: Interacts with the terminase small subunit; the active complex CC is composed of a monomer of the terminase large subunit and a nonamer CC ring of terminase small subunits. Interacts with the portal protein; CC this interaction allows the packaging of viral DNA. {ECO:0000256|HAMAP- CC Rule:MF_04148}. CC -!- DOMAIN: The ATPase region is in the N-terminus, whereas the nuclease CC region is in the C-terminus. {ECO:0000256|HAMAP-Rule:MF_04148}. CC -!- SIMILARITY: Belongs to the Lederbergvirus large terminase family. CC {ECO:0000256|HAMAP-Rule:MF_04148}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MW329986; QSH71736.1; -; Genomic_DNA. DR Proteomes; UP000663196; Genome. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_04148; TERL_BPP22; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR035421; Terminase_6C. DR InterPro; IPR044265; Terminase_large_su_BPP22. DR Pfam; PF17289; Terminase_6C; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_04148}; Endonuclease {ECO:0000256|HAMAP-Rule:MF_04148}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04148}; KW Late protein {ECO:0000256|HAMAP-Rule:MF_04148}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04148}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04148}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_04148}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_04148}; Viral genome packaging {ECO:0000256|HAMAP-Rule:MF_04148}; KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04148}. FT DOMAIN 290..450 FT /note="Terminase_6C" FT /evidence="ECO:0000259|Pfam:PF17289" FT MOTIF 49..56 FT /note="Walker A motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04148" FT MOTIF 171..176 FT /note="Walker B motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04148" FT ACT_SITE 176 FT /note="For ATPase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04148" FT METAL 293 FT /note="Magnesium; catalytic; for nuclease activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04148" FT METAL 439 FT /note="Magnesium; catalytic; for nuclease activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04148" SQ SEQUENCE 482 AA; 54620 MW; F3E3FE6397D4F6FF CRC64; MDTQERLRNL VRELAERQKY FRMKQYTPYG WQEKFIAASS NCAQLLAMTG NRCGKTYTGA FIMACHLTGR YPEWWTGRKF DKPVNCWAAG ISTDTTRDIL QSELLGDWKN PEAFGTGMIP KEDIVKTERR EGKPGCVQAV MVRHASGGLS SLIFKSYEMS QDKFMGTAID VIWLDEECPK DIYTQCVTRT ATTGGIVYLT FTPEHGLTEI VKDFLQDLKP GQFLIHASWE DAPHLSPEVK EQLLSVYSPA ERRMRAEGIP MLGSGVVFPI LEEKFVCEPF DIPDHFHRII GIDLGFDHPN AIACVAWDAE KDKYYLYDER SESGETLGMH ADAIYLKGGH QIPVVVPHDA FKHDGATSGR RFVDLLKDDH NLNVVYEPFS NPPGPDGKHG GNSVEFGVNW MLTRMENGDL KVFNTCTNFL KEMKMYHRKD GKIVDRNDDM ISATRYALLM ASRHARPGAV RNSGYYRSDT ARLIPDWFGS IV //