ID H8ZMB0_9CAUD Unreviewed; 139 AA.
AC H8ZMB0;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Head completion nuclease {ECO:0000256|HAMAP-Rule:MF_04160};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_04160};
GN ORFNames=Syn7803C43_4 {ECO:0000313|EMBL:AIX14399.1}, Syn7803C97_6
GN {ECO:0000313|EMBL:AIX22559.1}, Syn7803C98_5
GN {ECO:0000313|EMBL:AIX22773.1}, Syn7803US88_4
GN {ECO:0000313|EMBL:AIX38005.1};
OS Synechococcus phage ACG-2014c.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae; Namakavirus; Namakavirus smbcm6.
OX NCBI_TaxID=1079998 {ECO:0000313|EMBL:AFD02621.1, ECO:0000313|Proteomes:UP000007596};
RN [1] {ECO:0000313|Proteomes:UP000185277, ECO:0000313|Proteomes:UP000185278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Syn7803C43 {ECO:0000313|EMBL:AIX14399.1}, Syn7803C97
RC {ECO:0000313|EMBL:AIX22559.1}, Syn7803C98
RC {ECO:0000313|EMBL:AIX22773.1}, and Syn7803US88
RC {ECO:0000313|EMBL:AIX38005.1};
RA Gregory A.C., LaButti K., Copeland A., Woyke T., Sullivan M.B.;
RT "Ecological redundancy of diverse viral populations within a natural
RT community.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFD02621.1, ECO:0000313|Proteomes:UP000007596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25043051; DOI=10.1038/nature13459;
RA Deng L., Ignacio Espinoza J.C., Gregory A.C., Poulos B.T., Weitz J.S.,
RA Hugenholtz P., Sullivan M.B.;
RT "Viral tagging reveals discrete populations in Synechococcus viral genome
RT sequence space.";
RL Nature 513:242-245(2014).
CC -!- FUNCTION: During phage morphogenesis, plays an essential role in the
CC head-tail joining step. The associated nuclease activity is essential
CC for morphogenesis, possibly by cleaving packaged DNA to enable the
CC joining of heads to tails. Displays both exo- and endonuclease
CC activity. {ECO:0000256|HAMAP-Rule:MF_04160}.
CC -!- SIMILARITY: Belongs to the Caudovirales head completion nuclease
CC family. {ECO:0000256|HAMAP-Rule:MF_04160}.
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DR EMBL; JN371768; AFD02621.1; -; Genomic_DNA.
DR EMBL; KJ019027; AIX14399.1; -; Genomic_DNA.
DR EMBL; KJ019063; AIX22559.1; -; Genomic_DNA.
DR EMBL; KJ019064; AIX22773.1; -; Genomic_DNA.
DR EMBL; KJ019128; AIX38005.1; -; Genomic_DNA.
DR RefSeq; YP_007001731.1; NC_019444.1.
DR GeneID; 14005505; -.
DR KEGG; vg:14005505; -.
DR OrthoDB; 13184at10239; -.
DR Proteomes; UP000007596; Genome.
DR Proteomes; UP000185277; Genome.
DR Proteomes; UP000185278; Genome.
DR Proteomes; UP000185279; Genome.
DR Proteomes; UP000185280; Genome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.91.30; -; 1.
DR HAMAP; MF_04160; NUCL_HEAD_T4; 1.
DR InterPro; IPR046390; NUCL_HEAD_T4.
DR InterPro; IPR014833; TnsA_N.
DR Pfam; PF08722; Tn7_TnsA-like_N; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_04160};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_04160};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04160};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_04160}.
FT DOMAIN 40..134
FT /note="TnsA endonuclease N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08722"
FT ACT_SITE 29
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04160"
FT ACT_SITE 68
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04160"
FT ACT_SITE 83
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04160"
SQ SEQUENCE 139 AA; 16979 MW; FD493471B558B60D CRC64;
MRYQGRYTPS MPHKYRGDPN NIVYRSSWEY KFMKWCEMTP TVEEWGSEEI IIPYISPVDG
RRHRYFPDFY VKIKNKKYLV EVKPLKQTKE PKTQKRITKR YINEVVTWSV NQAKWKAATE
FCADHNWEFM LITEKELKV
//