PRO_JSRV
ID PRO_JSRV Reviewed; 866 AA.
AC P31625;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Gag-Pro polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein;
DE Contains:
DE RecName: Full=p12;
DE Contains:
DE RecName: Full=Capsid protein p27;
DE Contains:
DE RecName: Full=Nucleocapsid protein-dUTPase;
DE Short=NC-dUTPase;
DE EC=3.6.1.23 {ECO:0000250|UniProtKB:P07570};
DE Contains:
DE RecName: Full=Protease 17 kDa {ECO:0000250|UniProtKB:P07570};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE Contains:
DE RecName: Full=Protease 13 kDa {ECO:0000250|UniProtKB:P07570};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE Contains:
DE RecName: Full=G-patch peptide {ECO:0000250|UniProtKB:P07570};
GN Name=pro;
OS Sheep pulmonary adenomatosis virus (Jaagsiekte sheep retrovirus) (JSRV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11746;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=JSRV-SA;
RX PubMed=1629959; DOI=10.1128/jvi.66.8.4930-4939.1992;
RA York D.F., Vigne R., Verwoerd D.W., Querat G.;
RT "Nucleotide sequence of the jaagsiekte retrovirus, an exogenous and
RT endogenous type D and B retrovirus of sheep and goats.";
RL J. Virol. 66:4930-4939(1992).
RN [2]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=24298557; DOI=10.1155/2013/984028;
RA Huang X., Cheng Q., Du Z.;
RT "A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
RT ribosomal frameshifting or readthrough in animal viruses.";
RL Biomed. Res. Int. 2013:984028-984028(2013).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
CC {ECO:0000305}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
CC -!- FUNCTION: [Protease 17 kDa]: The aspartyl protease mediates proteolytic
CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell.
CC {ECO:0000250|UniProtKB:P07570, ECO:0000255|PROSITE-ProRule:PRU00275}.
CC -!- FUNCTION: [Protease 13 kDa]: The aspartyl protease mediates proteolytic
CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell.
CC {ECO:0000250|UniProtKB:P07570, ECO:0000255|PROSITE-ProRule:PRU00275}.
CC -!- FUNCTION: [G-patch peptide]: Enhances the activity of the reverse
CC transcriptase. May be part of the mature RT.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC Evidence={ECO:0000250|UniProtKB:P07570};
CC -!- SUBUNIT: [Protease 17 kDa]: Homodimer. {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBUNIT: [G-patch peptide]: Interacts with the reverse
CC transcriptase/ribonuclease H. {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBUNIT: [Nucleocapsid protein-dUTPase]: Homotrimer.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag-Pro polyprotein;
CC IsoId=P31625-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P31622-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P31623-1; Sequence=External;
CC -!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle release. They can occur
CC individually or in close proximity within structural proteins. They
CC interacts with sorting cellular proteins of the multivesicular body
CC (MVB) pathway. Most of these proteins are class E vacuolar protein
CC sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC Gag-p12 contains two L domains: a PTAP/PSAP motif which interacts with
CC the UEV domain of TSG101, and a PPXY motif which binds to the WW
CC domains of the ubiquitin ligase NEDD4. Gag-p27 contains one L domain: a
CC PTAP/PSAP motif which interacts with the UEV domain of TSG101.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- DOMAIN: [Protease 17 kDa]: The glycine-rich G-patch domain (GPD) is
CC present at the C-terminus of the protease from which it is then
CC detached by the protease itself. {ECO:0000250|UniProtKB:P07570}.
CC -!- PTM: [Protease 17 kDa]: Released by autocatalytic processing. The
CC protease can undergo further autoprocessing to yield 2 shorter but
CC enzymatically active forms of 12 kDa and 13 kDa without the GDP domain.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- PTM: [Gag-Pro polyprotein]: Myristoylated. Myristoylation of the matrix
CC (MA) domain mediates the transport and binding of Gag polyproteins to
CC the host plasma membrane and is required for the assembly of viral
CC particles. {ECO:0000250|UniProtKB:P10258}.
CC -!- PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000250|UniProtKB:P07570}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal
CC frameshifting between gag-pro. {ECO:0000305|PubMed:24298557}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the dUTPase family.
CC {ECO:0000305}.
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DR EMBL; M80216; AAA89181.1; -; Genomic_RNA.
DR PIR; B42740; PRMVJA.
DR RefSeq; NP_041185.1; NC_001494.1.
DR SMR; P31625; -.
DR GeneID; 1490019; -.
DR KEGG; vg:1490019; -.
DR Proteomes; UP000007215; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00692; dUTPase; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF02337; Gag_p10; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Capsid protein; DNA-binding; Hydrolase; Lipoprotein;
KW Magnesium; Metal-binding; Multifunctional enzyme; Myristate;
KW Nucleotide metabolism; Protease; Repeat; Ribosomal frameshifting;
KW Viral matrix protein; Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT CHAIN 2..866
FT /note="Gag-Pro polyprotein"
FT /id="PRO_0000199548"
FT CHAIN 2..99
FT /note="Matrix protein p10"
FT /id="PRO_0000443182"
FT CHAIN 100..167
FT /note="Phosphorylated protein"
FT /id="PRO_0000443183"
FT CHAIN 168..256
FT /note="p12"
FT /id="PRO_0000443184"
FT CHAIN 257..477
FT /note="Capsid protein p27"
FT /id="PRO_0000443185"
FT CHAIN 478..713
FT /note="Nucleocapsid protein-dUTPase"
FT /id="PRO_0000443186"
FT CHAIN 714..866
FT /note="Protease 17 kDa"
FT /id="PRO_0000443187"
FT CHAIN 714..831
FT /note="Protease 13 kDa"
FT /id="PRO_0000443188"
FT PEPTIDE 832..866
FT /note="G-patch peptide"
FT /id="PRO_0000443189"
FT DOMAIN 734..810
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 821..866
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 507..524
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 103..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 202..205
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000305"
FT MOTIF 208..211
FT /note="PPXY motif"
FT /evidence="ECO:0000305"
FT MOTIF 287..290
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P10258"
FT COMPBIAS 115..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 739
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT SITE 99..100
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 256..257
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 477..478
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 713..714
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT SITE 831..832
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07570"
SQ SEQUENCE 866 AA; 95245 MW; 50C1920E2C6C335E CRC64;
MGHTHSRQLF VHMLSVMLKH RGITVSKTKL INFLSFIEEV CPWFPREGTV NLETWKKVGE
QIRTHYTLHG PEKVPVETLS FWTLIRDCLD FDNDELKRLG NLLKQEEDPL HTPDSVPSYD
PPPPPPPSLK MHPSDNDDSL SSTDEAELDE EAAKYHQEDW GFLAQEKGAL TSKDELVECF
KNLTIALQNA GIQLPSNNNT FPSAPPFPPA YTPTVMAGLD PPPGFPPPSK HMSPLQKALR
QAQRLGEVVS DFSLAFPVFE NNNQRYYESL PFKQLKELKI ACSQYGPTAP FTIAMIESLG
TQALPPNDWK QTARACLSGG DYLLWKSEFF EQCARIADVN RQQGIQTSYE MLIGEGPYQA
TDTQLNFLPG AYAQISNAAR QAWKKLPSSS TKTEDLSKVR QGPDEPYQDF VARLLDTIGK
IMSDEKAGMV LAKQLAFENA NSACQAALRP YRKKGDLSDF IRICADIGPS YMQGIAMAAA
LQGKSIKEVL FQQQARNKKG LQKSGNSGCF VCGQPGHRAA VCPQKHQTSV NTPNLCPRCK
KGKHWARDCR SKTDVQGNPL PPVSGNLGEG PAPGPETMLW GNTAGSKRTI ADLCRATRGS
AGLDLCATSY TVLTPEMGVQ TLATGVFGPL PPGTVGLLLG RSSASLKGIL IHPGVIDSDY
TGEIKILASA PNKIIVINAG QRIAQLLLVP LVIQGKTINR DRQDKGFGSS DAYWVQNVTE
ARPELELRIN ANFFRGVLDT GADISVISDK YWPTTWPKQM AISTLQGIGQ TTNPEQSSSL
LTWKDKDGHT GQFKPYILPY LPVNLWGRDI LSKMGVYLYS PSPTVTDLML DQGLLPNQGL
GKQHQGIILP LDLKPNQDRK GLGCFP
