ID O41289_MPMV Unreviewed; 314 AA.
AC O41289;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Protease {ECO:0000256|ARBA:ARBA00043244};
DE AltName: Full=Proteinase {ECO:0000256|ARBA:ARBA00042135};
DE Flags: Fragment;
GN Name=prot {ECO:0000313|EMBL:AAC97564.1};
OS Simian endogenous retrovirus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus;
OC Mason-Pfizer monkey virus.
OX NCBI_TaxID=1048243 {ECO:0000313|EMBL:AAC97564.1};
RN [1] {ECO:0000313|EMBL:AAC97564.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9094640;
RA van der Kuyl A.C., Mang R., Dekker J.T., Goudsmit J.;
RT "Complete nucleotide sequence of simian endogenous type D retrovirus with
RT intact genome organization: evidence for ancestry to simian retrovirus and
RT baboon endogenous virus.";
RL J. Virol. 71:3666-3676(1997).
CC -!- FUNCTION: Enhances the activity of the reverse transcriptase. May be
CC part of the mature RT. {ECO:0000256|ARBA:ARBA00004001}.
CC -!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
CC {ECO:0000256|ARBA:ARBA00003295}.
CC -!- SUBUNIT: Active as a homodimer. {ECO:0000256|ARBA:ARBA00038675}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the peptidase A2 family. HERV class-II K(HML-2)
CC subfamily. {ECO:0000256|ARBA:ARBA00038141}.
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DR EMBL; U85505; AAC97564.1; -; Genomic_DNA.
DR MEROPS; A02.009; -.
DR Proteomes; UP000114147; Genome.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR InterPro; IPR000467; G_patch_dom.
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 PANTHER; PTHR19422; GAG RETROVIRAL POLYPROTEIN; 1.
DR PANTHER; PTHR19422:SF123; HUMAN ENDOGENOUS RETROVIRUS K ENDOPEPTIDASE; 1.
DR Pfam; PF00692; dUTPase; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF00077; RVP; 1.
DR SMART; SM00443; G_patch; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF51283; dUTPase-like; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AAC97564.1}.
FT DOMAIN 183..259
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 270..314
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC97564.1"
SQ SEQUENCE 314 AA; 34294 MW; E106D611695EEC3E CRC64;
SRKSFISQAG KRDEGPAPGP ETSIWGSQLC SSQQQQYISK LSRATPGSAG LDLSSTSHTV
LTPEMGPQTL NTGIYGPLPP NTFGLLLGRS SVTMRGLQVL PGVIDNDYEG EIKIMARAID
NIITVPQGVR IAQLILLPLV KTDNNIQHSN RNIKGFGSSD IYWVQPITNQ KPSLTLWLDG
KAFTGLIDTG ADVTIIKQED WPSHWPTTET LTHLRGIGQS SNPKQSSKYL TWTDKENNSG
LIKPFVIPYL PVNLWGRDLL AQMKIIMCSP NDIVIAQMLT QGYTPGKGLG KRENGIPQPI
LVSGQFDKKG FGNF
//
