TRM3_HHV11
ID TRM3_HHV11 Reviewed; 735 AA.
AC P04295;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Tripartite terminase subunit 3 {ECO:0000255|HAMAP-Rule:MF_04013};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04013};
DE AltName: Full=Terminase large subunit {ECO:0000255|HAMAP-Rule:MF_04013};
GN Name=TRM3 {ECO:0000255|HAMAP-Rule:MF_04013}; OrderedLocusNames=UL15;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-343.
RX PubMed=3010237; DOI=10.1093/nar/14.8.3435;
RA McGeoch D.J., Dolan A., Frame M.C.;
RT "DNA sequence of the region in the genome of herpes simplex virus type 1
RT containing the exonuclease gene and neighbouring genes.";
RL Nucleic Acids Res. 14:3435-3448(1986).
RN [3]
RP INTERACTION WITH PORTAL PROTEIN.
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 [4]
RP SUBCELLULAR LOCATION.
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).
RN [5]
RP INTERACTION WITH TRM1 AND PORTAL PROTEIN, SUBCELLULAR LOCATION, AND NUCLEAR
RP LOCALIZATION SIGNAL.
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 [6]
RP REVIEW.
RX PubMed=18687036; DOI=10.1146/annurev.genet.42.110807.091545;
RA Rao V.B., Feiss M.;
RT "The bacteriophage DNA packaging motor.";
RL Annu. Rev. Genet. 42:647-681(2008).
RN [7]
RP INTERACTION WITH UL6.
RX PubMed=19224991; DOI=10.1128/jvi.00026-09;
RA Yang K., Wills E., Baines J.D.;
RT "The putative leucine zipper of the UL6-encoded portal protein of herpes
RT simplex virus 1 is necessary for interaction with pUL15 and pUL28 and their
RT association with capsids.";
RL J. Virol. 83:4557-4564(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 471-735.
RX PubMed=23596306; DOI=10.1128/jvi.00311-13;
RA Selvarajan Sigamani S., Zhao H., Kamau Y.N., Baines J.D., Tang L.;
RT "The structure of the herpes simplex virus DNA-packaging terminase pUL15
RT nuclease domain suggests an evolutionary lineage among eukaryotic and
RT prokaryotic viruses.";
RL J. Virol. 87:7140-7148(2013).
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 TRM2 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. TRM3 carries an RNase H-like nuclease
CC activity that plays an important role for the cleavage of concatemeric
CC viral DNA into unit length genomes. {ECO:0000255|HAMAP-Rule:MF_04013}.
CC -!- SUBUNIT: Interacts with the terminase subunits TRM1 and TRM2. Interacts
CC with portal protein. {ECO:0000255|HAMAP-Rule:MF_04013,
CC ECO:0000269|PubMed:12743292, ECO:0000269|PubMed:17392365,
CC ECO:0000269|PubMed:19224991}.
CC -!- INTERACTION:
CC P04295; P10212: TRM1; NbExp=8; IntAct=EBI-7032965, EBI-7032948;
CC P04295; P10217: TRM2; NbExp=6; IntAct=EBI-7032965, EBI-7033000;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04013,
CC ECO:0000269|PubMed:16920825, ECO:0000269|PubMed:17392365}.
CC Note=Responsible for the nuclear localization of the two others
CC subunits TRM1 and TRM2. {ECO:0000255|HAMAP-Rule:MF_04013,
CC ECO:0000269|PubMed:17392365}.
CC -!- SIMILARITY: Belongs to the herpesviridae TRM3 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04013}.
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DR EMBL; X14112; CAA32330.1; -; Genomic_DNA.
DR EMBL; X03839; CAA27456.1; ALT_TERM; Genomic_DNA.
DR PIR; A03781; WMBE31.
DR PIR; F30083; WMBET5.
DR RefSeq; YP_009137089.1; NC_001806.2.
DR PDB; 4IOX; X-ray; 2.46 A; A/B/C=471-735.
DR PDB; 5HUW; X-ray; 1.95 A; A/B=181-192.
DR PDB; 6M5R; EM; 3.50 A; A=35-728.
DR PDB; 6M5S; EM; 3.90 A; A=35-727.
DR PDB; 6M5T; EM; 2.46 A; A=471-735.
DR PDB; 6M5U; EM; 3.80 A; A=35-728.
DR PDB; 6M5V; EM; 4.50 A; A=38-727.
DR PDBsum; 4IOX; -.
DR PDBsum; 5HUW; -.
DR PDBsum; 6M5R; -.
DR PDBsum; 6M5S; -.
DR PDBsum; 6M5T; -.
DR PDBsum; 6M5U; -.
DR PDBsum; 6M5V; -.
DR SMR; P04295; -.
DR IntAct; P04295; 3.
DR MINT; P04295; -.
DR PRIDE; P04295; -.
DR DNASU; 2703385; -.
DR GeneID; 2703385; -.
DR KEGG; vg:2703385; -.
DR Proteomes; UP000009294; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.420.320; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04013; HSV_TRM3; 1.
DR InterPro; IPR003498; DNA_pack_C.
DR InterPro; IPR038435; DNA_pack_C_sf.
DR InterPro; IPR003499; DNA_pack_N.
DR InterPro; IPR033663; HSV_TRM3.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02499; DNA_pack_C; 1.
DR Pfam; PF02500; DNA_pack_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Host nucleus; Hydrolase; Reference proteome;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..735
FT /note="Tripartite terminase subunit 3"
FT /id="PRO_0000115940"
FT MOTIF 183..189
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013,
FT ECO:0000269|PubMed:17392365"
FT MOTIF 258..265
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT MOTIF 352..357
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 357
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 509
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013,
FT ECO:0000269|PubMed:23596306"
FT ACT_SITE 581
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013,
FT ECO:0000269|PubMed:23596306"
FT ACT_SITE 707
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013,
FT ECO:0000269|PubMed:23596306"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 111..118
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 203..220
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 223..228
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 419..423
FT /evidence="ECO:0007829|PDB:6M5R"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 446..452
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:6M5R"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:6M5R"
FT HELIX 480..488
FT /evidence="ECO:0007829|PDB:4IOX"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:6M5T"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:4IOX"
FT STRAND 502..509
FT /evidence="ECO:0007829|PDB:4IOX"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:4IOX"
FT STRAND 520..529
FT /evidence="ECO:0007829|PDB:4IOX"
FT STRAND 532..542
FT /evidence="ECO:0007829|PDB:4IOX"
FT HELIX 550..568
FT /evidence="ECO:0007829|PDB:4IOX"
FT STRAND 574..581
FT /evidence="ECO:0007829|PDB:4IOX"
FT HELIX 586..600
FT /evidence="ECO:0007829|PDB:4IOX"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:4IOX"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:6M5T"
FT HELIX 640..652
FT /evidence="ECO:0007829|PDB:4IOX"
FT STRAND 656..663
FT /evidence="ECO:0007829|PDB:4IOX"
FT STRAND 665..671
FT /evidence="ECO:0007829|PDB:4IOX"
FT HELIX 673..681
FT /evidence="ECO:0007829|PDB:4IOX"
FT STRAND 686..688
FT /evidence="ECO:0007829|PDB:6M5T"
FT HELIX 707..719
FT /evidence="ECO:0007829|PDB:4IOX"
SQ SEQUENCE 735 AA; 80923 MW; A7B8D69C3E6CD965 CRC64;
MFGQQLASDV QQYLERLEKQ RQLKVGADEA SAGLTMGGDA LRVPFLDFAT ATPKRHQTVV
PGVGTLHDCC EHSPLFSAVA RRLLFNSLVP AQLKGRDFGG DHTAKLEFLA PELVRAVARL
RFKECAPADV VPQRNAYYSV LNTFQALHRS EAFRQLVHFV RDFAQLLKTS FRASSLTETT
GPPKKRAKVD VATHGRTYGT LELFQKMILM HATYFLAAVL LGDHAEQVNT FLRLVFEIPL
FSDAAVRHFR QRATVFLVPR RHGKTWFLVP LIALSLASFR GIKIGYTAHI RKATEPVFEE
IDACLRGWFG SARVDHVKGE TISFSFPDGS RSTIVFASSH NTNGIRGQDF NLLFVDEANF
IRPDAVQTIM GFLNQANCKI IFVSSTNTGK ASTSFLYNLR GAADELLNVV TYICDDHMPR
VVTHTNATAC SCYILNKPVF ITMDGAVRRT ADLFLADSFM QEIIGGQARE TGDDRPVLTK
SAGERFLLYR PSTTTNSGLM APDLYVYVDP AFTANTRASG TGVAVVGRYR DDYIIFALEH
FFLRALTGSA PADIARCVVH SLTQVLALHP GAFRGVRVAV EGNSSQDSAV AIATHVHTEM
HRLLASEGAD AGSGPELLFY HCEPPGSAVL YPFFLLNKQK TPAFEHFIKK FNSGGVMASQ
EIVSATVRLQ TDPVEYLLEQ LNNLTETVSP NTDVRTYSGK RNGASDDLMV AVIMAIYLAA
QAGPPHTFAP ITRVS
