ID   TRM1_PSHV1              Reviewed;         859 AA.
AC   Q6UDK3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 53.
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   Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS   (Pacheco's disease virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX   NCBI_TaxID=670426;
OH   NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA   Thureen D.R., Keeler C.L. Jr.;
RT   "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT   Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL   J. Virol. 80:7863-7872(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   -!- 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       Note=Found associated with the external surface of the viral capsid
CC       during assembly and DNA packaging, but seems absent in extracellular
CC       mature virions. {ECO:0000255|HAMAP-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; AY372243; AAQ73707.1; -; Genomic_DNA.
DR   RefSeq; NP_944401.1; NC_005264.1.
DR   SMR; Q6UDK3; -.
DR   GeneID; 2656987; -.
DR   KEGG; vg:2656987; -.
DR   Proteomes; UP000006840; 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   3: Inferred from homology;
KW   ATP-binding; Host nucleus; Late protein; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Viral genome packaging; Viral release from host cell;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..859
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000406842"
FT   ZN_FING         231..259
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   REGION          512..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         782..789
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   859 AA;  95189 MW;  E8C0EB72EBCD336C CRC64;
     MPPAPKNGSA ANAWRSERNA RPREVWRAIV PKNLMADDTT RRLLAVAGQL QTLLFQIELL
     KRCDPEVLVK RALRAKIKHN ALMVLYLHSR LAGDLAAQAA HRLTVGIYCL WMWLRRACSE
     AAALANEIDT YATYRDKDRF FSATMNLSPG GTCRLHSLVG LSLYGRTQDV TRELGLINDA
     ENLLKQINYC HLIVSTESAE AALVGVDEFL TATVGGGMVA SPETYDHTQP CCICLDELSV
     TANQGDTIYK RLGYSVCDHL VKQVKVNVTP DDVLRHMPFL NSVDANTLRG AIDKLRGSSG
     GEVGGGRRLA GVVPTGCRAE VGRSEQEDGA PAGDDRADLE HEARASRILD SYDVFTEAPG
     PVYRLSELRY WLASGKAAGA KTRGSCAHAT HQATVLQKLD TDLSAMFARA ETFERECRSA
     EREIFGTSFA HFHRHVASKI ASVRGVGGGG EALIDKLLAG SPATAPEAEI ETLISSCYSH
     HMSLPLFSRL GNPEKADTDA LVEILKSYRD QTRPRADKAG GRAEDGAGDC DDEGYPGAAD
     ATRRGQRDWI GRVRVDTAAV ADEHEDKVKK LLDRAERDLT TRRKNYAERL SARSFSNLDR
     CVKNQRAELE KLLRVNVYGA ALPAMYVELK NGFLARQAFM KAVTSDESQH IRRCRLARED
     VEGYEQHQYV RSALMRTSLD PAALPHLASR FYELVSGPMF RRHVERFPQP PNTSLYFTVE
     NVGLLPHLKE ELASFTRTYA HAEWMVSEFR EFYDFSGISG VSETQRAAYA YIREAVFAAA
     LFESIFQCGR AKLMRADSVE VDAGGPLLTD GIYLTFEERF PLIAIWGVGE DRRLCATSVV
     VTEKDLYAVL YAVLHKQDK