ID D6PUZ5_HHV2 Unreviewed; 808 AA.
AC D6PUZ5;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Ubiquitin E3 ligase ICP0 {ECO:0000313|EMBL:ADG01888.1};
GN Name=RL2 {ECO:0000313|EMBL:ADG01888.1};
OS Human herpesvirus 2 (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC Simplexvirus humanalpha2.
OX NCBI_TaxID=10310 {ECO:0000313|EMBL:ADG01888.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ADG01888.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VRC9154_1998_16293 {ECO:0000313|EMBL:ADG01888.1};
RA Corey L., Laing K.J., Magaret A.S., Mueller D.E., Zhao L., Johnston C.,
RA De Rosa S.C., Koelle D.M., Wald A.;
RT "Diversity in CD8+ T cell function and epitope breadth among persons with
RT genital herpes.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GU979901; ADG01888.1; -; Genomic_DNA.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-KW.
DR CDD; cd23130; RING-HC_EHV1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022711};
KW Ligase {ECO:0000313|EMBL:ADG01888.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Modulation of host ubiquitin pathway by viral E3 ligase
KW {ECO:0000256|ARBA:ARBA00022711};
KW Modulation of host ubiquitin pathway by virus
KW {ECO:0000256|ARBA:ARBA00022662};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 126..167
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 80658 MW; 6509CD6904556670 CRC64;
MEPRPGTSSR ADPGPERPPR QTPGTQPAAP HAWGMLNDMQ WLASSDSEEE TEVGISDDDL
HRDSTSEAGS TDTEMFEAGL MDAATPPARP PAERQGSPTP ADAQGSCGGG PVGEEEAEAG
GGGDVCAVCT DEIAPPLRCQ SFPCLHPFCI PCMKTWIPLR NTCPLCNTPV AYLIVGVTAS
GSFSTIPIVN DPRTRVEAEA AVRSGTAVDF IWTGNPRTAP RSLSLGGHTV RALSPTPPWP
GTDDEDDDLA DVDYVPPAPR RAPRRGGGGA GATRGTSQPA ATRPAPPGAP RSSSSGGAPL
RAGVGSGSGG GPAVAAVVPR VASLPPAAGG GRAQARRVGE DAAAAEGRTP PARQPRAAQE
PPIVISDSPP PSPRRPAGPG PLSFFSSSSA QVSSGPGGGG LPQSSGRAAR PRAAVAPRVR
SPPRAAAAPV VSASADAAGP APPAVPVDAH RAPRSRMTQA QTDTQAQSLG RAGATDARGS
GGPGAEGGPG VPRGTNTPGA APHAAEGAAA RPRKRRGSDS GPAASSSASS SAAPRSPLAP
QGVGAKRAAP RRAPDSDSGD RGHGPLAPAP ADAAPPSASP SSQAAVAAAA SSSSSAASSS
SSSSSSASSS AGGAGGSVAS ASGAGERRET SLGPRAAAPR GPRKCARKTR HAEGGPEPGA
RDPAPGLTRY LPIAGASSVV ALAPYVNKTV TGDCLPVLDM ETGHIGAYVV LVDQTGNVAD
LLRAAAPAWS RRTLLPEHAR NCVRPPDYPT PPASEWNSLW MTPVGNMLFD QGTLVGALDF
HGLRSRHPWS REQGAPAPAG DAPAGHGE
//
