ID   TRM1_SUHVF              Reviewed;         724 AA.
AC   P11871;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014};
OS   Suid herpesvirus 1 (strain Indiana-Funkhauser / Becker) (SuHV-1)
OS   (Pseudorabies virus (strain Indiana-Funkhauser / Becker)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31523;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2542904; DOI=10.1093/nar/17.9.3597;
RA   Pederson N.E., Enquist L.W.;
RT   "The nucleotide sequence of a pseudorabies virus gene similar to ICP18.5 of
RT   herpes simplex virus type 1.";
RL   Nucleic Acids Res. 17:3597-3597(1989).
RN   [2]
RP   INTERACTION WITH UL15, AND SUBCELLULAR LOCATION.
RX   PubMed=9371568; DOI=10.1128/jvi.71.12.9118-9123.1997;
RA   Koslowski K.M., Shaver P.R., Wang X.Y., Tenney D.J., Pederson N.E.;
RT   "The pseudorabies virus UL28 protein enters the nucleus after coexpression
RT   with the herpes simplex virus UL15 protein.";
RL   J. Virol. 71:9118-9123(1997).
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       ECO:0000269|PubMed:9371568}. 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; X14573; CAA32712.1; -; Genomic_DNA.
DR   PIR; A33779; WMBEPR.
DR   RefSeq; YP_068331.1; NC_006151.1.
DR   SMR; P11871; -.
DR   GeneID; 2952557; -.
DR   KEGG; vg:2952557; -.
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   ATP-binding; Host nucleus; Late protein; Metal-binding; Nucleotide-binding;
KW   Viral genome packaging; Viral release from host cell; Zinc; Zinc-finger.
FT   CHAIN           1..724
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115888"
FT   ZN_FING         175..203
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   REGION          410..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         652..659
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   724 AA;  78882 MW;  87C16178DC5BADB4 CRC64;
     MAERRLVAVL GQVQTYVFQL EMLKRCDPAV VRELAPRVKL NALMCRYLAR RLPLEAQTTP
     LTCALRLALA YARAEGDRVL GALAAAGDDA EAYFERTMGG ACRFHARVAL DTYGGRVETE
     LQFLHDAENL LKQLNYCHLI TPHAVDLSAV DEFLARTIGG GLVVPPELYD PAQPCAVCFE
     ELCVTANQGE ATHRRLLGCV CDHLTRQLAV RVDPEDVAKN LPHVHGLDEA RRGRALAALA
     AVDAAEAREA EAASTAAAGA EAGDAGETAR RRADALLDAH DVFRPASRRL YAVSELQFWL
     ASTNQAVRAL DLFTHNLDDL ERRERRAEVR AAAVELALFG RRPEHFDRAR AARELDIIDG
     LLVGGCAASP DERLEALIRA CYDHHMSTPM LRMLDPDRAN RDALERLLEG GDDADADGGA
     AGGADAGDGG VGDEDGPGAP PPADAVAWAD LPAAALRDAE RRRRLYADRL SRRSAASLAQ
     CVREQRRELE KTLRVNVYGD ALLHTYVAVA AGFRARRAFC EAAARAGTVV DERETGCFDA
     HSFMKATVQR HPVDAALLPA VTRKFFELVN GPLFAHDTHA FAQPPNTALY FAVENVGLLP
     HLKEELARFM VARDWCVSEF RGFYRFQTAG VTATQRQAWR YIRELVLAVA VFRSVFHCGD
     VEVLRADRFA GRDGLYLTYE ASCPLVAVFG AGPGGIGPGT TAVLASDVFG LLHTTLQLRG
     APSR