ID Q9Q1X4_9GAMR Unreviewed; 2378 AA.
AC Q9Q1X4;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Gag-Pol polyprotein {ECO:0000256|ARBA:ARBA00018735};
OS Porcine endogenous retrovirus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Porcine type-C oncovirus.
OX NCBI_TaxID=61673 {ECO:0000313|EMBL:CAB65340.1};
RN [1] {ECO:0000313|EMBL:CAB65340.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type C {ECO:0000313|EMBL:CAB65340.1};
RA Czauderna F., Fischer N., Boller K., Krach U., Kurth R., Toenjes R.R.;
RT "Molecular Characterization of Human-tropic and Replication-competent
RT Porcine Endogenous Retroviruses.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes viral DNA integration into the host chromosome, by
CC performing a series of DNA cutting and joining reactions. This enzyme
CC activity takes place after virion entry into a cell and reverse
CC transcription of the RNA genome in dsDNA. The first step in the
CC integration process is 3' processing. This step requires a complex
CC comprising the viral genome, matrix protein and integrase. This complex
CC is called the pre-integration complex (PIC). The integrase protein
CC removes 2 nucleotides from each 3' end of the viral DNA, leaving
CC recessed CA OH's at the 3' ends. In the second step that requires cell
CC division, the PIC enters cell nucleus. In the third step, termed strand
CC transfer, the integrase protein joins the previously processed 3' ends
CC to the 5' ends of strands of target cellular DNA at the site of
CC integration. The last step is viral DNA integration into host
CC chromosome. {ECO:0000256|ARBA:ARBA00002884}.
CC -!- FUNCTION: Forms the spherical core of the virion that encapsulates the
CC genomic RNA-nucleocapsid complex. {ECO:0000256|ARBA:ARBA00002845}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004425}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004425}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; AJ133817; CAB65340.1; -; Genomic_DNA.
DR MEROPS; A02.020; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019031; C:viral envelope; 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:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease 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:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR GO; GO:0019068; P:virion assembly; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd09851; HTLV-1-like_HR1-HR2; 1.
DR CDD; cd09273; RNase_HI_RT_Bel; 1.
DR CDD; cd06095; RP_RTVL_H_like; 1.
DR CDD; cd03715; RT_ZFREV_like; 1.
DR Gene3D; 1.10.287.210; -; 1.
DR Gene3D; 1.10.340.70; -; 1.
DR Gene3D; 2.30.30.850; -; 1.
DR Gene3D; 3.10.20.370; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 3.90.310.10; ENV polyprotein, receptor-binding domain; 1.
DR Gene3D; 1.10.150.180; Gamma-retroviral matrix domain; 1.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR008981; FMuLV_rcpt-bd.
DR InterPro; IPR000840; G_retro_matrix.
DR InterPro; IPR036946; G_retro_matrix_sf.
DR InterPro; IPR003036; Gag_P30.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR040643; MLVIN_C.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041577; RT_RNaseH_2.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR InterPro; IPR015416; Znf_H2C2_histone_UAS-bd.
DR PANTHER; PTHR33166:SF1; CORE SHELL PROTEIN GAG P30 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR33166; GAG_P30 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF02093; Gag_p30; 1.
DR Pfam; PF18697; MLVIN_C; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF00429; TLV_coat; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR Pfam; PF09337; zf-H2C2; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF49830; ENV polyprotein, receptor-binding domain; 1.
DR SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR SUPFAM; SSF58069; Virus ectodomain; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA integration {ECO:0000256|ARBA:ARBA00022908};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Fusion of virus membrane with host cell membrane
KW {ECO:0000256|ARBA:ARBA00022521};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022521};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879};
KW Viral genome integration {ECO:0000256|ARBA:ARBA00023195};
KW Viral matrix protein {ECO:0000256|ARBA:ARBA00023311};
KW Viral nucleoprotein {ECO:0000256|ARBA:ARBA00023086};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022521};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00047}.
FT TRANSMEM 2322..2344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 493..508
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 546..616
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 724..915
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1157..1303
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT DOMAIN 1422..1580
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 132..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1973..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2221..2248
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 132..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1995..2011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2378 AA; 267308 MW; 6EC8DAEC1B4ED18A CRC64;
MGQTVTTPLS LTLDHWTEVR SRAHNLSVQV KKGPWQTFCA SEWPTFDVGW PSEGTFNSEI
ILAVKAIIFQ TGPGSHPDQE PYILTWQDLA EDPPPWVKPW LNKPRKPGPR ILALGEKNKH
SAEKVEPSPR IYPEIEEPPT WPEPQPVPPP PYPAQGAVRG PSAPPGAPVV EGPAAGTRSR
RGATPERTDE IAILPLRTYG PPMPGGQLQP LQYWPFSSAD LYNWKTNHPP FSEDPQRLTG
LVESLMFSHQ PTWDDCQQLL QTLFTTEERE RILLEARKNV PGADGRPTQL QNEIDMGFPL
TRPGWDYNTA EGRESLKIYR QALVAGLRGA SRRPTNLAKV REVMQGPNEP PSVFLERLME
AFRRFTPFDP TSEAQKASVA LAFIGQSALD IRKKLQRLEG LQEAELRDLV REAEKVYYRR
ETEEEKEQRK EKEREEREER RDRRQEKNLT KILAAVVEGK SSRERERDFR KIRSGPRQSG
NLGNRTPLDK DQCAYCKEKG HWARNCPKKG NKGPKVLALE EDKDGRRGSD PLPEPRVTLK
VEGQPVEFLV DTGAEHSVLL QPLGKLKEKK SWVMGATGQR QYPWTTRRTV DLGVGRVTHS
FLVIPECPVP LLGRDLLTKM GAQISFEQGR PEVSVNNKPI TVLTLQLDDE YRLYSPQVKP
DQDIQSWLEQ FPQAWAETAG MGLAKQVPPQ VIQLKASATP VSVRQYPLSR EAREGIWPHV
QRLIQQGILV PVQSPWNTPL LPVRKPGTND YRPVQDLREV NKRVQDIHPT VPNPYNLLSA
LPPERNWYTV LDLKDAFFCL RLHPTSQPLF AFEWRDPGTG RTGQLTWTRL PQGFKNSPTI
FDEALHRDLA NFKIQHPQVT LLQYVDDLLL AGATKQDCLE GTKALLLELS DLGYRASAKK
AQICRREVTY LGYSLRGGQR WLTEARKKTV VQIPAPTTAK QVREFLGTAG FCRLWIPGFA
TLAAPLYPLT KEKGEFSWAP EHQKAFDAIK KALLSAPALA LPDVTKPFTL YVDERKGVAR
GVLTQTLGPW RRPVAYLSKK LDPVASGWPV CLKAIAAVAI LVKDADKLTL GQNITVIAPH
ALENIVRQPP DRWMTNARMT HYQSLLLTER VTFAPPAALN PATLLPEETD EPVTHDCHQL
LIEETGVRKD LTDIPLTGEV LTWFTDGSSY VVEGKRMAGA AVVDGTRTIW ASSLPEGTSA
QKAELMALTQ ALRLAEGKSI NIYTDSRYAF ATAHVHGAIY KQRGLLTSAG REIKNKEEIL
SLLEALHLPK RLAIIHCPGH QKAKDLISRG NQMADRVAKQ AAQAVNLLPI IETPKAPEPR
RQYTLEDWQE IKKIDQFSET PEGTCYTSYG KEILPHKEGL EYVQQIHRLT HLGTKHLQQL
VRTSPYHVLR LPGVADSVVK HCVPCQLVNA NPSRIPPGKR LRGSHPGAHW EVDFTEVKPA
KYGNKYLLVF VDTFSGWVEA YPTKKETSTV VAKKILEEIF PRFGIPKVIG SDNGPAFVAQ
VSQGLAKILG IDWKLHCAYR PQSSGQVERM NRTIKETLTK LTTETGINDW MALLPFVLFR
VRNTPGQFGL TPYELLYGGP PPLVEIASVH SADVLLSQPL FSRLKALEWV RQRAWKQLRE
AYSGEGDLQV PHRFQVGDSV YVRRHRAGNL ETRWKGPYLV LLTTPTAVKV ERIPTWIHAS
HVKPAPPPDS GWKAEKTENP LKLRLHRVVP YSVNNSSSMH PTLSRRHLPI RGGKPKRLKI
PLSFASIAWF LTLSITPQVN GKRLVDSPNS HKPLSLTWLL TDSGTGININ STQGEAPLGT
WWPELYVCLR SVIPGLNDQA TPPDVLRAYG FYVCPGPPNN EEYCGNPQDF FCKQWSCITS
NDGNWKWPVS QQDRVSYSFV NNPTSYNQFN YGHGRWKDWQ QRVQKDVRNK QISCHSLDLD
YLKISFTEKG KQENIQKWVN GISWGIVYYG GSGRKKGSVL TIRLRIETQM EPPVAIGPNK
GLAEQGPPIQ EQRPSPNPSD YNTTSGSVPT EPNITIKTGA KLFSLIQGAF QALNSTTPEA
TSSCWLCLAS GPPYYEGMAR GGKFNVTKEH RDQCTWGSQN KLTLTEVSGK GTCIGMVPPS
HQHLCNHTEA FNRTSESQYL VPGYDRWWAC NTGLTPCVST LVFNQTKDFC VMVQIVPRVY
YYPEKAVLDK YDYRYNRPKR EPISLTLAVM LGLGVAAGVG TGTAALITGP QQLEKGLSNL
HRIVTEDLQA LEKSVSNLEE SLTSLSEVVL QNRRGLDLLF LKEGGLCVAL KEECCFYVDH
SGAIRDSMSK LRERLERRRR EREADQGWFE GWFNRSPWMT TLLSALTGPL VVLLLLLTVG
PCLINRFVAF VRERVSAVQI MVLRQQYQGL LSQGETDL
//
