TRM1_HHV6Z
ID TRM1_HHV6Z Reviewed; 726 AA.
AC P52544; Q9IBR9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=U40;
OS Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison with
RT human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-410.
RX PubMed=7983761; DOI=10.1128/jvi.69.1.589-596.1995;
RA Stamey F.R., Dominguez G., Black J.B., Dambaugh T.R., Pellett P.E.;
RT "Intragenomic linear amplification of human herpesvirus 6B oriLyt suggests
RT acquisition of oriLyt by transposition.";
RL J. Virol. 69:589-596(1995).
CC -!- FUNCTION: Component of the molecular motor that translocates viral
CC genomic DNA in empty capsid during DNA packaging. Forms a tripartite
CC terminase complex together with TRM2 and TRM3 in the host cytoplasm.
CC Once the complex reaches the host nucleus, it interacts with the capsid
CC portal vertex. This portal forms a ring in which genomic DNA is
CC translocated into the capsid. TRM1 carries an endonuclease activity
CC that plays an important role for the cleavage of concatemeric viral DNA
CC into unit length genomes. {ECO:0000255|HAMAP-Rule:MF_04014}.
CC -!- SUBUNIT: Associates with TRM2 and TRM3 to form the tripartite terminase
CC complex. Interacts with portal protein. {ECO:0000255|HAMAP-
CC Rule:MF_04014}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04014}.
CC Note=Found associated with the external surface of the viral capsid
CC during assembly and DNA packaging, but seems absent in extracellular
CC mature virions. {ECO:0000255|HAMAP-Rule:MF_04014}.
CC -!- SIMILARITY: Belongs to the herpesviridae TRM1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04014}.
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DR EMBL; AF157706; AAD49654.1; -; Genomic_DNA.
DR RefSeq; NP_050221.1; NC_000898.1.
DR SMR; P52544; -.
DR PRIDE; P52544; -.
DR DNASU; 1497042; -.
DR GeneID; 1497042; -.
DR KEGG; vg:1497042; -.
DR Proteomes; UP000006930; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016485; P:protein processing; IEA:UniProtKB-UniRule.
DR GO; GO:0019069; P:viral capsid assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0019073; P:viral DNA genome packaging; IEA:InterPro.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04014; HSV_TRM1; 1.
DR InterPro; IPR000501; UL28/UL56.
DR Pfam; PF01366; PRTP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Host nucleus; Late protein; Metal-binding; Nucleotide-binding;
KW Reference proteome; Viral genome packaging; Viral release from host cell;
KW Zinc; Zinc-finger.
FT CHAIN 1..726
FT /note="Tripartite terminase subunit 1"
FT /id="PRO_0000115883"
FT ZN_FING 189..217
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT BINDING 626..633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ SEQUENCE 726 AA; 83037 MW; F4FB10A4BED3204A CRC64;
MNSLQSLCVL CARLNECALD LECLKFCDPV IVLSDMANFK KNGIVILHLY QTFFEGIKEQ
NLLCASALTV YMQVLLKAMY EQVLLLDAAL ESFMVDQDRK KYFEKVLCLK RCAEHLSINI
SLNNGVEFIV QLSTLNDIEQ LISKINSVYA LLLPQEGLQI CGKIIDLLTI MCGACMVAKP
ESYLETKTCM KCYEELTLTP NQGKSLRKRL HGKFCNHLTE QKAFFNIEKN IETIEKDLGE
AILNYGTIQS VVTEIKKIFK QQRSAESLHV SDAEKTLKKY NIFSKVPDVI YSLSEFTYWS
KISETIVRNV AITLQQLNSC HTLYKQLQND VSLYLYGEVS EDFLALSENL LTHDERLYVG
SIYVSPSRLI DLVTGLSIKN LEESPIFKRL AEEDEVQHKI KSLLHDIRDP QTTETPGRLN
TINCMLQTHN LQQEVLARKK AYFQKVSESG YNRVMACIRE QESLINKVVS VNVYGNFIFE
ALSKIMNGFV LRKMYLDGSI RVDSCTYDEH LYIKNNLMPK KLPLELLPDL SEIMYTLLTG
PLSDFHKSAY PLPANISMAY GCDHAEMLPH MKEDLARCIE GTIHPSVWMV CEYNEFFNFS
GVTDVNDMQK KMWNFIRELT LSVALYNDVF GKRLKIVRID EEEDLNGNVV LTFNHESPLL
FHTGGGMTKF KDVYSLLYCD LQAQLSRETV DVPEGVSYSV RTPNLLDLVR ENEQDESIIP
GCLFDE