TRM1_HHV11
ID TRM1_HHV11 Reviewed; 785 AA.
AC P10212;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=UL28;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
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 FUNCTION.
RC STRAIN=F;
RX PubMed=9878624; DOI=10.1006/viro.1998.9475;
RA Taus N.S., Baines J.D.;
RT "Herpes simplex virus 1 DNA cleavage/packaging: the UL28 gene encodes a
RT minor component of B capsids.";
RL Virology 252:443-449(1998).
RN [3]
RP INTERACTION WITH UL15, AND SUBCELLULAR LOCATION.
RC STRAIN=F;
RX PubMed=9882384; DOI=10.1128/jvi.73.2.1704-1707.1999;
RA Koslowski K.M., Shaver P.R., Casey J.T. II, Wilson T., Yamanaka G.,
RA Sheaffer A.K., Tenney D.J., Pederson N.E.;
RT "Physical and functional interactions between the herpes simplex virus UL15
RT and UL28 DNA cleavage and packaging proteins.";
RL J. Virol. 73:1704-1707(1999).
RN [4]
RP INTERACTION WITH UL6.
RC STRAIN=F;
RX PubMed=12743292; DOI=10.1128/jvi.77.11.6351-6358.2003;
RA White C.A., Stow N.D., Patel A.H., Hughes M., Preston V.G.;
RT "Herpes simplex virus type 1 portal protein UL6 interacts with the putative
RT terminase subunits UL15 and UL28.";
RL J. Virol. 77:6351-6358(2003).
RN [5]
RP INTERACTION WITH UL33.
RC STRAIN=F;
RX PubMed=16731912; DOI=10.1128/jvi.00125-06;
RA Yang K., Baines J.D.;
RT "The putative terminase subunit of herpes simplex virus 1 encoded by UL28
RT is necessary and sufficient to mediate interaction between pUL15 and
RT pUL33.";
RL J. Virol. 80:5733-5739(2006).
RN [6]
RP FUNCTION.
RC STRAIN=F;
RX PubMed=16920825; DOI=10.1128/jvi.01364-06;
RA Wills E., Scholtes L., Baines J.D.;
RT "Herpes simplex virus 1 DNA packaging proteins encoded by UL6, UL15, UL17,
RT UL28, and UL33 are located on the external surface of the viral capsid.";
RL J. Virol. 80:10894-10899(2006).
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 ECO:0000269|PubMed:16920825, ECO:0000269|PubMed:9878624}.
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, ECO:0000269|PubMed:12743292,
CC ECO:0000269|PubMed:16731912, ECO:0000269|PubMed:9882384}.
CC -!- INTERACTION:
CC P10212; P10217: TRM2; NbExp=6; IntAct=EBI-7032948, EBI-7033000;
CC P10212; P04295: TRM3; NbExp=8; IntAct=EBI-7032948, EBI-7032965;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04014,
CC ECO:0000269|PubMed:9882384}. 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_04014}.
CC -!- SIMILARITY: Belongs to the herpesviridae TRM1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04014}.
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DR EMBL; X14112; CAA32321.1; -; Genomic_DNA.
DR PIR; A30085; WMBEW8.
DR RefSeq; YP_009137103.1; NC_001806.2.
DR PDB; 6M5R; EM; 3.50 A; B=2-775.
DR PDB; 6M5S; EM; 3.90 A; B=2-775.
DR PDB; 6M5U; EM; 3.80 A; B=2-775.
DR PDB; 6M5V; EM; 4.50 A; B=2-772.
DR PDBsum; 6M5R; -.
DR PDBsum; 6M5S; -.
DR PDBsum; 6M5U; -.
DR PDBsum; 6M5V; -.
DR SMR; P10212; -.
DR BioGRID; 971470; 1.
DR IntAct; P10212; 3.
DR MINT; P10212; -.
DR PRIDE; P10212; -.
DR DNASU; 2703457; -.
DR GeneID; 2703457; -.
DR KEGG; vg:2703457; -.
DR Proteomes; UP000009294; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Host nucleus; Late protein; Metal-binding;
KW Nucleotide-binding; Reference proteome; Viral genome packaging;
KW Viral release from host cell; Zinc; Zinc-finger.
FT CHAIN 1..785
FT /note="Tripartite terminase subunit 1"
FT /id="PRO_0000115874"
FT ZN_FING 197..225
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT REGION 433..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 696..703
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT HELIX 7..32
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 75..100
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 108..116
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 163..168
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 308..313
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 325..354
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 415..431
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 485..506
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 512..530
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 539..559
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 562..566
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 575..586
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 596..607
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 615..619
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 623..633
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 642..645
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 677..699
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 725..728
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 737..742
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 754..760
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 761..772
FT /evidence="ECO:0007829|PDB:6M5R"
SQ SEQUENCE 785 AA; 85578 MW; CFE8868BAA86F616 CRC64;
MAAPVSEPTV ARQKLLALLG QVQTYVFQIE LLRRCDPHIG RGKLPQLKLN ALQVRALRRR
LRPGLEAQAG AFLTPLSVTL ELLLEYAWRE GERLLGSLET FATAGDVAAF FTETMGLARP
CPYHQRVRLD TYGGTVHMEL CFLHDVENFL KQLNYCHLIT PSRGATAALE RVREFMVGAV
GSGLIVPPEL SDPSHPCAVC FEELCVTANQ GATIARRLAD RICNHVTQQA QVRLDANELR
RYLPHAAGLS DADRARALSV LDHALARTAG GDGQPHPSPE NDSVRKEADA LLEAHDVFQA
TTPGLYAISE LRFWLASGDR AGQTTMDAFA SNLTALARRE LQQETAAVAV ELALFGRRAE
HFDRAFGSHL AALDMVDALI IGGQATSPDD QIEALIRACY DHHLTTPLLR RLVSPEQCDE
EALRRVLARM GAGGAADAPK GGAGPDDDGD RVAVEEGARG LGAPGGGGED EDRRRGPGGQ
GPETWGDIAT QAAADVRERR RLYADRLTKR SLASLGRCVR EQRGELEKML RVSVHGEVLP
ATFAAVANGF AARARFCALT AGAGTVIDNR SAPGVFDAHR FMRASLLRHQ VDPALLPSIT
HRFFELVNGP LFDHSTHSFA QPPNTALYYS VENVGLLPHL KEELARFIMG AGGSGADWAV
SEFQRFYCFD GISGITPTQR AAWRYIRELI IATTLFASVY RCGELELRRP DCSRPTSEGR
YRYPPGVYLT YDSDCPLVAI VESAPDGCIG PRSVVVYDRD VFSILYSVLQ HLAPRLPDGG
HDGPP
