ID   TRM2_HHV11              Reviewed;         130 AA.
AC   P10217;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   RecName: Full=Tripartite terminase subunit 2 {ECO:0000255|HAMAP-Rule:MF_04015};
GN   Name=TRM2 {ECO:0000255|HAMAP-Rule:MF_04015}; OrderedLocusNames=UL33;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA   Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1845831; DOI=10.1016/0042-6822(91)90043-b;
RA   Al-Kobaisi M.F., Rixon F.J., McDougall I., Preston V.G.;
RT   "The herpes simplex virus UL33 gene product is required for the assembly of
RT   full capsids.";
RL   Virology 180:380-388(1991).
RN   [3]
RP   FUNCTION.
RX   PubMed=15207632; DOI=10.1016/j.virol.2004.03.044;
RA   Beard P.M., Baines J.D.;
RT   "The DNA cleavage and packaging protein encoded by the UL33 gene of herpes
RT   simplex virus 1 associates with capsids.";
RL   Virology 324:475-482(2004).
RN   [4]
RP   INTERACTION WITH TRM1 AND TRM3.
RX   PubMed=17392365; DOI=10.1128/jvi.00047-07;
RA   Yang K., Homa F., Baines J.D.;
RT   "Putative terminase subunits of herpes simplex virus 1 form a complex in
RT   the cytoplasm and interact with portal protein in the nucleus.";
RL   J. Virol. 81:6419-6433(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=17913813; DOI=10.1128/jvi.01875-07;
RA   Yang K., Poon A.P., Roizman B., Baines J.D.;
RT   "Temperature-sensitive mutations in the putative herpes simplex virus type
RT   1 terminase subunits pUL15 and pUL33 preclude viral DNA cleavage/packaging
RT   and interaction with pUL28 at the nonpermissive temperature.";
RL   J. Virol. 82:487-494(2008).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18559942; DOI=10.1099/vir.0.2008/000448-0;
RA   Higgs M.R., Preston V.G., Stow N.D.;
RT   "The UL15 protein of herpes simplex virus type 1 is necessary for the
RT   localization of the UL28 and UL33 proteins to viral DNA replication
RT   centres.";
RL   J. Gen. Virol. 89:1709-1715(2008).
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 TRM1 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. {ECO:0000255|HAMAP-Rule:MF_04015,
CC       ECO:0000269|PubMed:15207632, ECO:0000269|PubMed:17913813}.
CC   -!- SUBUNIT: Associates with TRM1 and TRM3 to form the tripartite terminase
CC       complex. {ECO:0000255|HAMAP-Rule:MF_04015,
CC       ECO:0000269|PubMed:17392365}.
CC   -!- INTERACTION:
CC       P10217; P10212: TRM1; NbExp=6; IntAct=EBI-7033000, EBI-7032948;
CC       P10217; P04295: TRM3; NbExp=6; IntAct=EBI-7033000, EBI-7032965;
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04015,
CC       ECO:0000269|PubMed:18559942}. Note=Found associated with the external
CC       surface of the viral capsid during assembly and DNA packaging, but
CC       seems absent in extracellular mature virions. {ECO:0000255|HAMAP-
CC       Rule:MF_04015}.
CC   -!- SIMILARITY: Belongs to the herpesviridae TRM2 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04015}.
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DR   EMBL; X14112; CAA32308.1; -; Genomic_DNA.
DR   EMBL; M62932; AAA45829.1; -; Genomic_DNA.
DR   PIR; F30085; WMBEH3.
DR   PDB; 6M5R; EM; 3.50 A; C=12-129.
DR   PDB; 6M5S; EM; 3.90 A; C=12-129.
DR   PDB; 6M5U; EM; 3.80 A; C=12-129.
DR   PDB; 6M5V; EM; 4.50 A; C=13-129.
DR   PDBsum; 6M5R; -.
DR   PDBsum; 6M5S; -.
DR   PDBsum; 6M5U; -.
DR   PDBsum; 6M5V; -.
DR   EMDB; EMD-30090; -.
DR   EMDB; EMD-30091; -.
DR   EMDB; EMD-30093; -.
DR   EMDB; EMD-30094; -.
DR   SMR; P10217; -.
DR   IntAct; P10217; 2.
DR   MINT; P10217; -.
DR   Proteomes; UP000009294; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04015; HSV_TRM2; 1.
DR   InterPro; IPR005208; Herpes_TT2.
DR   Pfam; PF03581; Herpes_UL33; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Host nucleus; Reference proteome; Viral genome packaging;
KW   Viral release from host cell.
FT   CHAIN           1..130
FT                   /note="Tripartite terminase subunit 2"
FT                   /id="PRO_0000116023"
FT   HELIX           17..20
FT                   /evidence="ECO:0007829|PDB:6M5R"
FT   HELIX           27..34
FT                   /evidence="ECO:0007829|PDB:6M5R"
FT   HELIX           53..56
FT                   /evidence="ECO:0007829|PDB:6M5R"
FT   HELIX           62..80
FT                   /evidence="ECO:0007829|PDB:6M5R"
FT   HELIX           102..127
FT                   /evidence="ECO:0007829|PDB:6M5R"
SQ   SEQUENCE   130 AA;  14437 MW;  D04CFDA7A3C585D3 CRC64;
     MAGREGRTRQ RTLRDTIPDC ALRSQTLESL DARYVSRDGA HDAAVWFEDM TPAELEVVFP
     TTDAKLNYLS RTQRLASLLT YAGPIKAPDD AAAPQTPDTA CVHGELLAAK RERFAAVINR
     FLDLHQILRG
//