PORTL_EBVG
ID PORTL_EBVG Reviewed; 613 AA.
AC Q3KSR9;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04012};
GN ORFNames=BBRF1;
OS Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10376;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT nasopharyngeal carcinoma patient.";
RL J. Virol. 79:15323-15330(2005).
CC -!- FUNCTION: Forms a portal in the viral capsid through which viral DNA is
CC translocated during DNA packaging. Assembles as a dodecamer at a single
CC fivefold axe of the T=16 icosahedric capsid. Binds to the molecular
CC motor that translocates the viral DNA, termed terminase.
CC {ECO:0000255|HAMAP-Rule:MF_04012}.
CC -!- SUBUNIT: Homododecamerizes. Interacts with terminase subunits TRM1 and
CC TRM3. {ECO:0000255|HAMAP-Rule:MF_04012}.
CC -!- INTERACTION:
CC Q3KSR9; P0CK49: BSRF1; Xeno; NbExp=2; IntAct=EBI-2621338, EBI-2621334;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04012}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04012}.
CC -!- SIMILARITY: Belongs to the herpesviridae portal protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04012}.
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DR EMBL; AY961628; AAY41130.1; -; Genomic_DNA.
DR PDB; 6RVR; EM; 3.46 A; A/B/C/D/E/F/G/H/I/J/K/L=1-613.
DR PDB; 6RVS; EM; 3.59 A; A/B/C/D/E/F/G/H/I/J/K/L=1-613.
DR PDBsum; 6RVR; -.
DR PDBsum; 6RVS; -.
DR SMR; Q3KSR9; -.
DR IntAct; Q3KSR9; 2.
DR MINT; Q3KSR9; -.
DR Proteomes; UP000007641; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; 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 HAMAP; MF_04012; HSV_PORTL; 1.
DR InterPro; IPR002660; Herpes_Portal.
DR Pfam; PF01763; Herpes_UL6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host nucleus; Viral genome packaging;
KW Viral release from host cell; Virion.
FT CHAIN 1..613
FT /note="Portal protein"
FT /id="PRO_0000375973"
FT REGION 577..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 55..69
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 101..131
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 182..202
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:6RVR"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 253..275
FT /evidence="ECO:0007829|PDB:6RVR"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 442..447
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 481..495
FT /evidence="ECO:0007829|PDB:6RVR"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:6RVR"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 516..527
FT /evidence="ECO:0007829|PDB:6RVR"
FT TURN 528..530
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 548..557
FT /evidence="ECO:0007829|PDB:6RVR"
FT HELIX 560..569
FT /evidence="ECO:0007829|PDB:6RVR"
SQ SEQUENCE 613 AA; 68455 MW; 064B83A4F8FFDB72 CRC64;
MFNMNVDESA SGALGSSAIP VHPTPASVRL FEILQGKYAY VQGQTIYANL RNPGVFSRQV
FTHLFKRAIS HCTYDDVLHD WNKFEACIQK RWPSDDSCAS RFRESTFESW STTMKLTVRD
LLTTNIYRVL HSRSVLSYER YVDWICATGM VPAVKKPITQ ELHSKIKSLR DRCVCRELGH
ERTIRSIGTE LYEATREIIE SLNSTFIPQF TEVTIEYLPR SDEYVAYYCG RRIRLHVLFP
PAIFAGTVTF DSPVQRLYQN IFMCYRTLEH AKICQLLNTA PLKAIVGHGG RDMYKDILAH
LEQNSQRKDP KKELLNLLVK LSENKTISGV TDVVEEFITD ASNNLVDRNR LFGQPGETAA
QGLKKKVSNT VVKCLTDQIN EQFDQINGLE KERELYLKKI RSMESQLQAS LGPGGNNPAA
SAPAAVAAEA ASVDILTGST ASAIEKLFNS PSASLGARVS GHNESILNSF VSQYIPPSRE
MTKDLTELWE SELFNTFKLT PVVDNQGQRL YVRYSSDTIS ILLGPFTYLV AELSPVELVT
DVYATLGIVE IIDELYRSSR LAIYIEDLGR KYCPASATGG DHGIRQAPSA RGDAEPDHAK
SKPARDPPPG AGS
