TRM3_ALHV1
ID TRM3_ALHV1 Reviewed; 686 AA.
AC O36378;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=29;
OS Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX NCBI_TaxID=654901;
OH NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA Ensser A., Pflanz R., Fleckenstein B.;
RT "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL J. Virol. 71:6517-6525(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 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; AF005370; AAC58075.1; -; Genomic_DNA.
DR PIR; T03123; T03123.
DR RefSeq; NP_065527.1; NC_002531.1.
DR SMR; O36378; -.
DR GeneID; 911744; -.
DR KEGG; vg:911744; -.
DR Proteomes; UP000000941; 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 3: Inferred from homology;
KW DNA-binding; Host nucleus; Hydrolase; Reference proteome;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..686
FT /note="Tripartite terminase subunit 3"
FT /id="PRO_0000405716"
FT MOTIF 220..227
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT MOTIF 315..320
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 320
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 474
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 546
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 658
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ SEQUENCE 686 AA; 76860 MW; BA86EEBEFC202460 CRC64;
MFYVKVMPAL QKACEELQNQ WSAKSGKWPV PETPLVAVET RRSERWPHPY LGLLPGVAAY
SSTLEDYCHL YNPYIDALTR CDLGQTHRRV ATQPVLSDQL CQQLKKLFSC PRNTSVKAKL
EFEAAVRTHQ ALDNSQVFLE LKTFVLNLSA FLNKRYSDRS SHIELFQKQL IMHTFFFLVS
IKAPELCEKF CNIFKLYFNI DTMDQATLDI FKQKASVFLI PRRHGKTWIV VAIISILLAS
VQDLRIGYVA HQKHVANAVF TEVINTLHTF FPGKYMDVKK ENGTIIFGLP NKKPSTLLCA
TCFNKNSIRG QTFQLLFVDE ANFIKKDALP TILGFMLQKD AKIIFISSSN SSDQSTSFLY
NLKGASERML NVVSYVCSNH KEDFSMQDGL ISCPCYSLHV PSYISIDEQI KTTTNLFLDG
VFDTELMGDS SCGTLSTFQI ISESALSQFE LCRIDTASPQ VQAHLNSTVH MYIDPAFTNN
LDASGTGISV IGRLGAKTKV ILGCEHFFLQ KLTGTAALQI ASCATSLLRS VVIIHPMIKC
AQITIEGNSS QDSAVAIANF IDECAPIPVT FYHQSDKTKG VLCPLYLLGQ EKAVAFESFI
YAMNLGLCKA SQLIVSHTIK LSFDPVTYLL EQVRAIKCQS LRDGSHTYHA KQKNLSDDLL
VSVVMSLYLS SANTLPFKPL HIERFF