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 24-JAN-2024, entry version 106. 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; 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] 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-30090; -. DR EMDB; EMD-30091; -. DR EMDB; EMD-30092; -. DR EMDB; EMD-30093; -. DR EMDB; EMD-30094; -. DR SMR; P04295; -. DR IntAct; P04295; 3. DR MINT; 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:UniProtKB-UniRule. 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; P-loop containing nucleotide triphosphate hydrolases; 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 //