PRO_SRV2
ID PRO_SRV2 Reviewed; 908 AA.
AC P51518;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Gag-Pro polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp24;
DE Contains:
DE RecName: Full=Phosphorylated protein pp18;
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; Synonyms=prt;
OS Simian retrovirus SRV-2.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=39068;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2435057; DOI=10.1016/0042-6822(87)90274-1;
RA Thayer R.M., Power M.D., Bryant M.L., Gardner M.B., Barr P.J., Luciw P.A.;
RT "Sequence relationships of type D retroviruses which cause simian acquired
RT immunodeficiency syndrome.";
RL Virology 157:317-329(1987).
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=P51518-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P51516-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P51517-1; 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 Phosphorylated protein pp24 and phosphorylated protein pp18 contains
CC one L domain: a PPXY motif which binds to the WW domains of the
CC ubiquitin ligase NEDD4. {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}.
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DR EMBL; M16605; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P51518; -.
DR MEROPS; A02.009; -.
DR Proteomes; UP000007229; 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; Coiled coil; DNA-binding; Hydrolase;
KW Lipoprotein; Magnesium; Metal-binding; Myristate; Nucleotide metabolism;
KW Protease; Repeat; Ribosomal frameshifting; Viral matrix protein;
KW Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT CHAIN 2..908
FT /note="Gag-Pro polyprotein"
FT /id="PRO_0000199552"
FT CHAIN 2..100
FT /note="Matrix protein p10"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT /id="PRO_0000443216"
FT CHAIN 101..213
FT /note="Phosphorylated protein pp24"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT /id="PRO_0000443217"
FT PROPEP 101..159
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT /id="PRO_0000443218"
FT CHAIN 160..213
FT /note="Phosphorylated protein pp18"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT /id="PRO_0000443219"
FT CHAIN 214..297
FT /note="p12"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT /id="PRO_0000443220"
FT CHAIN 298..523
FT /note="Capsid protein p27"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT /id="PRO_0000443221"
FT CHAIN 524..756
FT /note="Nucleocapsid protein-dUTPase"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT /id="PRO_0000443222"
FT CHAIN 757..908
FT /note="Protease 17 kDa"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT /id="PRO_0000443223"
FT CHAIN 757..874
FT /note="Protease 13 kDa"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT /id="PRO_0000443224"
FT PEPTIDE 875..908
FT /note="G-patch peptide"
FT /id="PRO_0000443225"
FT DOMAIN 777..853
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 864..908
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 544..561
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 132..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 215..251
FT /evidence="ECO:0000255"
FT MOTIF 200..203
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT MOTIF 208..211
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT ACT_SITE 782
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT SITE 100..101
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 159..160
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 213..214
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 297..298
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 523..524
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 756..757
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT SITE 874..875
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07570"
SQ SEQUENCE 908 AA; 100877 MW; DF8D823B89B0845F CRC64;
MGQELSQHEL YVEQLKKALK TRGVKVKGND LLKFFDFVKD TCPWFPQEGT IDIKRWRRVG
DCFQDYYNTF GPEKIPVTAF SYWNLIKDLI DKKEADPQVM AAVTQTEKIL KVSSQTDLRD
NSHNKDMDLI SLESDDEEAK APSEKMTMSN KSPKKYPAML ASQNNNTDKD PDLSEVDWDG
LEDEAAKYHN PDWPPFLSRP PPYNRTAATA PAVMAVVNPK EELKEKISQL EEQIKLEELH
QSLIIRLQKL KTGNERVTSS GNIESHSRTP KWPGQCLPKG KYLINKNTEE YPPKDIFPVT
ETMDGQGQAW RHHNGFDFTV IKELKTAVSQ YGATAPYTLA IVESIADNWL TPTDWNTLVR
AVLSGGDHLI WKSEFFENCR DTAKRNQQAG NGWDFDMLTG SGNYANTDAQ MQYDPGLFAQ
IQAAATNAWR KLPVKGDPGA SLTGVKQGPD EPFADFVHRL ITTAGRIFGN AEAGVDYVKQ
LAYENANPAC QAAIRPYRKK TDLTGYIRLC SDIGPSYQQG LAMAAAFSGQ TVKDLLNNKN
KDRGGCFKCG KKGHFAKDCR DHSNKNPESK VPGLCPRCKR GKHWANECKS KTDSQGNPLP
PHQGNRDEGP APGPEASLWG SQLCSSQQQQ SISKLNRASP GSAGLDLCST THTVLTPEMG
PQTLATGVYG PLPPNTFGLI LGRGSTTVKG LQIYPGVIDN DYTGEFKIMA RAISSIITIP
QGERIAQLVL LPLLRTAHKI QHPYRGDKNF GSSDIFWVQP ITHQKPSLVL WLDGKAFTGL
IDTGADVTII KQEDWPSHWP TTETLTNLRG IGQSNNPRQS SKYLTWKDKE NNSGLIKPFV
IPNLPVNLWG RDLLSQMKIM MCSPNDIVTA QMLAQGYSPG KGLGKREDGI LQPIPNSGQL
DRKGFGNF
