TRM3_PSHV1
ID TRM3_PSHV1 Reviewed; 506 AA.
AC Q6UDI2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 50.
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 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 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 -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04013}.
CC Note=Responsible for the nuclear localization of the two others
CC subunits TRM1 and TRM2. {ECO:0000255|HAMAP-Rule:MF_04013}.
CC -!- SIMILARITY: Belongs to the herpesviridae TRM3 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04013}.
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DR EMBL; AY372243; AAQ73728.1; -; Genomic_DNA.
DR SMR; Q6UDI2; -.
DR Proteomes; UP000006840; 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 HAMAP; MF_04013; HSV_TRM3; 1.
DR InterPro; IPR003498; DNA_pack_C.
DR InterPro; IPR038435; DNA_pack_C_sf.
DR InterPro; IPR033663; HSV_TRM3.
DR Pfam; PF02499; DNA_pack_C; 1.
PE 3: Inferred from homology;
KW DNA-binding; Host nucleus; Hydrolase; Reference proteome;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..506
FT /note="Tripartite terminase subunit 3"
FT /id="PRO_0000406822"
FT ACT_SITE 128
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 282
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 354
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 475
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ SEQUENCE 506 AA; 55025 MW; BA61F84AA5952557 CRC64;
MHRSDSTMWL KYGLSPPTRS PNAALCAAAA TKCASMTRPS CVLDSLTLYS PAWPCLCRYA
IFPCRAWAIY VRAGNFILTK FSRFSFCFCV WSPRPPIAAA ANHPATSTIV ARSQGLRGQD
FNFLFVDEAN FIKPGAMHTI MGFLNQTNCK LFFVSSTNTG QSSTSLLYNL KGSSNSLLNV
VTYICDDHLP EVQQRQNVTT CSCYVLQKPV YVTMDHSVRN TAELFVKDSF MNEIAGGQVG
NTLSARSVIA SRAMDQFLVY RPSTSNSPNV HNLSRVLTAY IDPAFTANRS ASGTGIALVT
ELNGATVLLG MEHFYLEALT GEAAAEIAQC ANLCVAYTCL LHPGVFREVR VAVEGNSSQD
SATAIALRLA DLLAPLQKRL GFSLVFAHTR QHGSSVAHPF YLLNKQKSRA FDLFISRFNS
GNIMASQELV SNTVLLGNDP CEYLVEQIKN LEIVITSGDA NRVYSGKQGG KLADDVLVAV
VMAAYLSFEG APPAGYHTVS GAVCRR